A guide to selecting high-performing antibodies for MMP7 (UniProt ID: P09237) for use in western blot and immunoprecipitation

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Elevated MMP7 expression is a hallmark of idiopathic pulmonary fibrosis and other interstitial lung diseases, where it has emerged as a candidate biomarker for disease progression. Identifying high-quality research antibodies is therefore essential to enable robust investigation of MMP7 biology and its translational potential. In this study, we systematically evaluated ten commercial antibodies for western blot and immunoprecipitation using a standardized knockout validation approach in human A549 cells, comparing readouts in MMP7 knockout lines with isogenic parental controls. These experiments form part of a larger collaborative initiative to address antibody reproducibility by characterizing commercial antibodies for human proteins and making the results openly available to the community. While antibody use and protocol conditions will vary between laboratories, this report provides a resource to guide selection of the most suitable reagents for studies of MMP7 in health and disease." } { "@context": "http://schema.org", "@type": "BreadcrumbList", "itemListElement": [ { "@type": "ListItem", "position": "1", "item": { "@id": "https://f1000research.com/", "name": "Home" } }, { "@type": "ListItem", "position": "2", "item": { "@id": "https://f1000research.com/browse/articles", "name": "Browse" } }, { "@type": "ListItem", "position": "3", "item": { "@id": "https://f1000research.com/articles/15-74", "name": "A guide to selecting high-performing antibodies for MMP7 (UniProt..." } } ] } Home Browse A guide to selecting high-performing antibodies for MMP7 (UniProt... ALL Metrics - Views Downloads Get PDF Get XML Cite How to cite this article Biddle M, Cooper J, Jones C et al. A guide to selecting high-performing antibodies for MMP7 (UniProt ID: P09237) for use in western blot and immunoprecipitation [version 1; peer review: 2 approved] . F1000Research 2026, 15 :74 ( https://doi.org/10.12688/f1000research.175973.1 ) NOTE: If applicable, it is important to ensure the information in square brackets after the title is included in all citations of this article. Close Copy Citation Details Export Export Citation Sciwheel EndNote Ref. Manager Bibtex ProCite Sente EXPORT Select a format first Track Share ▬ ✚ Data Note A guide to selecting high-performing antibodies for MMP7 (UniProt ID: P09237) for use in western blot and immunoprecipitation [version 1; peer review: 2 approved] Michael Biddle https://orcid.org/0000-0002-9853-8815 1 , Jemma Cooper https://orcid.org/0009-0007-8915-379X 1 , Carolyn Jones 2 , Katie Dixon 1 , Harvinder Virk https://orcid.org/0000-0002-9739-9593 1 Michael Biddle https://orcid.org/0000-0002-9853-8815 1 , Jemma Cooper https://orcid.org/0009-0007-8915-379X 1 , [...] Carolyn Jones 2 , Katie Dixon 1 , Harvinder Virk https://orcid.org/0000-0002-9739-9593 1 PUBLISHED 19 Jan 2026 Author details Author details 1 University of Leicester College of Life Sciences, Leicester, England, UK 2 Institute for Precision Health, University of Leicester, Leicester, England, UK Michael Biddle Roles: Conceptualization, Data Curation, Formal Analysis, Funding Acquisition, Investigation, Methodology, Project Administration, Resources, Supervision, Validation, Visualization, Writing – Original Draft Preparation, Writing – Review & Editing Jemma Cooper Roles: Data Curation, Formal Analysis, Investigation, Methodology, Validation, Writing – Review & Editing Carolyn Jones Roles: Investigation, Methodology, Project Administration, Writing – Review & Editing Katie Dixon Roles: Data Curation, Writing – Original Draft Preparation, Writing – Review & Editing Harvinder Virk Roles: Conceptualization, Funding Acquisition, Project Administration, Resources, Supervision, Writing – Review & Editing OPEN PEER REVIEW DETAILS REVIEWER STATUS This article is included in the YCharOS (Antibody Characterization through Open Science) gateway. Abstract Matrix metallopeptidase 7 (MMP7, also known as matrilysin) is a secreted zinc-dependent endopeptidase implicated in extracellular matrix remodelling and fibrotic processes. Elevated MMP7 expression is a hallmark of idiopathic pulmonary fibrosis and other interstitial lung diseases, where it has emerged as a candidate biomarker for disease progression. Identifying high-quality research antibodies is therefore essential to enable robust investigation of MMP7 biology and its translational potential. In this study, we systematically evaluated ten commercial antibodies for western blot and immunoprecipitation using a standardized knockout validation approach in human A549 cells, comparing readouts in MMP7 knockout lines with isogenic parental controls. These experiments form part of a larger collaborative initiative to address antibody reproducibility by characterizing commercial antibodies for human proteins and making the results openly available to the community. While antibody use and protocol conditions will vary between laboratories, this report provides a resource to guide selection of the most suitable reagents for studies of MMP7 in health and disease. READ ALL READ LESS Keywords P09237, MMP7, Matrilysin, matrix metallopeptidase 7, antibody validation, western blot, immunoprecipitation, interstitial lung disease, idiopathic pulmonary fibrosis Corresponding Author(s) Michael Biddle ( [email protected] ) Harvinder Virk ( [email protected] ) Close Corresponding authors: Michael Biddle, Harvinder Virk Competing interests: For this project, the authors developed partnerships with leading antibody manufacturers and KO cell line providers. The partners provide antibodies and KO cell lines to this project at no cost. These partners include: Abcam, ABCD antibodies, ABclonal, Addgene, Aviva Systems Biology, BioTechne, Cell Signaling Technology, Developmental Studies Hybridoma Bank, GeneTex, Horizon Discovery, Institute for Protein Innovation, MilliporeSigma, Proteintech, Synaptic Systems, Thermo Fisher Scientific. Grant information: This work was supported by a grant from the National Centre for the Replacement, Refinement and Reduction of Animals in Research (NC3Rs) and MRC (NC3Rs Ref: NC/NAM0019/1, MRC UKRI076) alongside support from the Leicester Institute for Precision Health. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. Copyright: © 2026 Biddle M et al . This is an open access article distributed under the terms of the Creative Commons Attribution License , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. How to cite: Biddle M, Cooper J, Jones C et al. A guide to selecting high-performing antibodies for MMP7 (UniProt ID: P09237) for use in western blot and immunoprecipitation [version 1; peer review: 2 approved] . F1000Research 2026, 15 :74 ( https://doi.org/10.12688/f1000research.175973.1 ) First published: 19 Jan 2026, 15 :74 ( https://doi.org/10.12688/f1000research.175973.1 ) Latest published: 19 Jan 2026, 15 :74 ( https://doi.org/10.12688/f1000research.175973.1 ) Introduction Interstitial lung diseases (ILDs) comprise a heterogenous group of pulmonary disorders characterised by varying degrees of inflammation and fibrosis of the lung interstitium, with idiopathic pulmonary fibrosis (IPF) representing one of the most severe and progressive forms. Matrix Metallopeptidase 7 (MMP7, also known as Matrilysin), encoded by the MMP7 gene, is a secreted zinc-dependent endopeptidase that degrades multiple components of the extracellular matrix. 1 In IPF, MMP7 is predominantly expressed by hyperplastic epithelium, with increased protein abundance in lung base tissue compared with non-diseased controls. 2 The role of MMP7 is thought to be pro-fibrotic, as MMP7 knockout mice are protected from bleomycin-induced pulmonary fibrosis. 3 Clinically, elevated levels of MMP7 in serum and bronchoalveolar lavage fluid have been associated with disease progression and severity, supporting its potential as a promising biomarker for both diagnosis and prognosis. 4 This research is part of a broader collaborative initiative in which academics, funders and commercial antibody manufacturers are working together to address antibody reproducibility issues by characterising commercial antibodies for human proteins using standardized protocols 5 and openly sharing the data. 6 Here we evaluated the performance of ten commercial antibodies for MMP7 for use in western blot and immunoprecipitation, enabling biochemical and cellular assessment of MMP7 properties and function. The platform for antibody characterisation used to carry out this study was endorsed by a committee of industry academic representatives. It consists of identifying human cell lines with adequate target protein expression and the development/contribution of equivalent knockout (KO) cell lines, followed by antibody characterisation procedures using most commercially available renewable antibodies against the corresponding protein. The standardised consensus antibody characterisation protocols are openly available on Protocols.io (DOI: dx.doi.org/10.21203/rs.3.pex-2607/v1 ). The authors do not engage in result analysis or offer explicit antibody recommendations. Our primary aim is to deliver top-tier data to the scientific community, grounded in Open Science principles. This empowers experts to interpret the characterisation data independently, enabling them to make informed choices regarding the most suitable antibodies for their specific experimental needs. Guidelines on how to interpret the antibody characterisation data found in this study are featured on the YCharOS gateway. 7 Results and discussion Our standard protocol involves comparing readouts from WT (wild type) and KO cells. 8 , 9 The first step is to identify a cell line(s) that expresses sufficient levels of a given protein to generate a measurable signal using antibodies. To this end, we examined the DepMap transcriptomics database to identify all cell lines that express the target at levels greater than 2.5 log 2 (transcript per million “TPM” + 1), which we have found to be a suitable cut-off (Cancer Dependency Map Portal, RRID:SCR_017655). The cell line A549 expresses the MMP7 transcript at 4.3 log 2 (TPM+1) and thus was identified as a suitable cell line and was modified by CRISPR/Cas9 to KO the corresponding MMP7 gene ( Table 1 ). Table 1. Summary of the cell lines used. Institution Catalogue number RRID (Cellosaurus) Cell line Genotype Abcam ab288558 CVCL_0023 A549 WT University of Leicester - CVCL_F0RJ A549 MMP7 KO According to the UniProt database, MMP7 is secreted into the extracellular space. As such, clarified concentrated medium from both A549 WT control and MMP7 KO cell lines was run on SDS-PAGE, transferred onto nitrocellulose membranes and probed in parallel with ten MMP7 antibodies ( Figure 1 ). Antibodies were then assessed for their ability to detect intracellular MMP7 using protein lysates from WT control and MMP7 knockout cells ( Figure 2 ). MMP7 expression was detected in the protein lysates but required a longer exposure time, indicating that MMP7 is predominantly secreted by A549 cells. Therefore, the performance of antibodies by immunofluorescence and flow cytometry was not evaluated in this study. Figure 1. MMP7 antibody screening by western blot using concentrated conditioned culture media. Culture media from A549 WT and MMP7 KO cells were collected, and 30 μg of protein was processed for western blot with the indicated MMP7 antibodies. The Ponceau stained transfers of each blot are presented to show equal loading of WT and KO samples. Antibody dilutions were chosen according to the recommendations of the antibody supplier. Antibody dilutions used: ab176325** at 1/1000, ab205525** at 1/1000, ab207299** at 1/1000, 71031 at 1/1000, GTX104658 at 1/1000, NB110-60988* at 1/1000, 10374-2-AP at 1/1000, 67990-1-Ig* at 1/2000, MAB9071* at 1/500 and MA5-51356** at 1/1000. Predicted band size: 29.7 kDa. *Monoclonal antibody; **Recombinant antibody. Figure 2. MMP7 antibody screening by western blot using protein lysates. Protein lysates from A549 WT and MMP7 KO cells were collected, and 30μg of protein was used for western blot with the indicated MMP7 antibodies. The Ponceau stained transfers of each blot are presented to show equal loading of WT and KO samples. Antibody dilutions were chosen according to the recommendations of the antibody supplier. Antibody dilutions used: ab176325** at 1/1000, ab205525** at 1/1000, ab207299** at 1/1000, 71031 at 1/1000, GTX104658 at 1/1000, NB110-60988* at 1/1000, 10374-2-AP at 1/1000, 67990-1-Ig* at 1/2000, MAB9071* at 1/500 and MA5-51356** at 1/1000. Predicted band size: 29.7 kDa. *Monoclonal antibody; **Recombinant antibody. We next assessed the ability of all ten antibodies to capture MMP7 from A549 culture medium by immunoprecipitation, followed by western blot analysis. For the immunoblot, a specific MMP7 antibody identified previously ( Figure 1 ) was used. Equal amounts of the starting material (SM) and unbound fraction (UB), along with the complete immunoprecipitated (IP) eluate, were separated by SDS-PAGE ( Figure 3 ). Figure 3. MMP7 antibody screening by immunoprecipitation of culture medium. Conditioned culture medium was collected from A549 WT cells, and immunoprecipitation was performed for 18 hours using 0.5 mg of protein and 2.0 μg of the indicated MMP7 antibodies pre-coupled to Dynabeads protein A or protein G. Samples were washed and processed for western blot with the anti-MMP7 ab207299** diluted at 1/1000. The Ponceau stained transfers of each blot are shown. SM = 4% starting material; UB = 4% unbound fraction; IP = immunoprecipitate. *Monoclonal antibody; **Recombinant antibody. In conclusion, we screened ten MMP7 commercial antibodies by western blot and immunoprecipitation by comparing the signal produced using human A549 WT and MMP7 KO cells. High-quality and renewable antibodies capable of successfully detecting MMP7 were identified. Limitations Inherent limitations are associated with the antibody characterization platform used in this study. Firstly, the YCharOS project focuses on renewable (recombinant and monoclonal) antibodies and does not test all commercially available MMP7 antibodies. YCharOS partners provide approximately 80% of all renewable antibodies, but some top-cited polyclonal antibodies may not be available through these partners. We encourage readers to consult vendor documentation to identify the specific antigen each antibody is raised against, where such information is available. Secondly, the YCharOS effort employs a non-biased approach that is agnostic to the protein for which antibodies have been characterized. The aim is to provide objective data on antibody performance without preconceived notions about how antibodies should perform or the molecular weight that should be observed in western blot. As the authors are not experts in MMP7, only a brief overview of the protein’s function and its relevance in disease is provided. MMP7 experts are invited to analyse and interpret observed banding patterns in western blots. Thirdly, YCharOS experiments are not performed in replicates primarily due to the use of multiple antibodies targeting various epitopes. Once a specific antibody is identified, it validates the protein expression of the intended target in the selected cell line, confirms the lack of protein expression in the KO cell line and supports conclusions regarding the specificity of the other antibodies. All experiments are performed using master mixes, and meticulous attention is paid to sample preparation and experimental execution. In instances where antibodies yield no signal, a repeat experiment is conducted following titration. Additionally, our independent data is performed subsequently to the antibody manufacturers internal validation process, therefore making our characterization process a repeat. Lastly, as comprehensive and standardized procedures are respected, any conclusions remain confined to the experimental conditions and cell line used for this study. The use of a single cell type for evaluating antibody performance poses as a limitation, as factors such as target protein abundance significantly impact results. Additionally, the use of cancer cell lines containing gene mutations poses a potential challenge, as these mutations may be within the epitope coding sequence or other regions of the gene responsible for the intended target. Such alterations can impact the binding affinity of antibodies. This represents an inherent limitation of any approach that employs cancer cell lines. Methods The standardized protocols used to carry out this KO cell line-based antibody characterization platform was established and approved by a collaborative group of academics, industry researchers and antibody manufacturers. The detailed materials and step-by-step protocols used to characterize antibodies in western blot, immunoprecipitation and immunofluorescence are openly available on Protocols.io (DOI: dx.doi.org/10.21203/rs.3.pex-2607/v1 ). Antibodies All MMP7 antibodies are listed in Table 2 , together with their corresponding Research Resource Identifiers (RRID), to ensure antibodies are cited properly. 10 Secondary antibodies used in this study are provided in Table 3 . To ensure consistency with manufacturer recommendations and account for proprietary formulations (where antibody concentrations are not disclosed), antibody usage is reported as dilution ratios rather than absolute concentrations. Table 2. Summary of the MMP7 antibodies tested. Company Catalogue number Lot number RRID (Antibody registry) Clonality Clone ID Host Stock concentration (μg/mL) Vendor recommended applications Abcam ab176325 ** 1081135-3 AB_3668828 Recombinant Monoclonal EPR1251(2) Rabbit 1636 FC-Intra, WB Abcam ab205525 ** 1029001-2 AB_2861279 Recombinant Monoclonal EPR17888-101 Rabbit 1537 IHC, WB Abcam ab207299 ** 1001762-3 AB_2894849 Recombinant Monoclonal EPR17888-71 Rabbit 1370 ICC/IF, IHC, WB Cell signaling Technology 71031 1 AB_2799796 Polyclonal - Rabbit 160 WB GeneTex GTX104658 44377 AB_1241062 Polyclonal - Rabbit 450 ELISA, IHC, WB Novus Biologicals NB110-60988 * 2020071501 AB_925513 Monoclonal MM0022-4C21 Mouse 200 IHC, WB Proteintech 10374-2-AP 00079668 AB_2144452 Polyclonal - Rabbit 600 ICC/IF, IHC, WB Proteintech 67990-1-Ig * 10022681 AB_2918739 Monoclonal 2E6D6 Mouse 1000 ELISA, ICC/IF, IHC, WB R & D Systems MAB9071 * DRG0624021 AB_2282021 Monoclonal 111433 Mouse 500 IHC, IP, WB Thermo Fisher Scientific MA5-51356 ** ZJ4521735A AB_3093027 Recombinant Monoclonal 8T4R8 Rabbit 1000 ELISA, IHC, WB * Monoclonal antibody. ** Recombinant antibody. Table 3. Summary of the secondary antibodies used. Company Secondary antibody Catalogue number RRID (Antibody registry) Clonality Application Stock concentration (μg/mL) Working concentration (μg/mL) Proteintech HRP-Goat Anti-Rabbit Secondary Antibody (H+L) RGAR001 AB_3073505 Recombinant Polyclonal Western blot 1000 0.1 Proteintech HRP-Goat Anti-Mouse Secondary Antibody (H+L) RGAM001 AB_3068333 Recombinant Polyclonal Western blot 1000 0.1 Abcam Veriblot ab131366 AB_2892718 Not specified Immunoprecipitation 40 0.04 Cell culture All cell lines used in this study are listed in Table 1 , alongside their corresponding RRIDs, to ensure proper citation. 11 Cells were cultured in DMEM high-glucose (Capricorn Scientific #DMEM-HPSTA) supplemented with 10% fetal bovine serum (Thermo Fisher Scientific #A5256801) and 1% antibiotic/antimycotic solution (Capricorn Scientific #AAS-B). All cell lines used in this study were routinely tested for mycoplasma contamination and were confirmed to be mycoplasma-free. CRISPR/Cas9 genome editing The A549 MMP7 KO clone was generated using low-passage cells. Prior to ribonucleoprotein transfection, 20,000 cells were plated in each well of a 48-well plate and incubated overnight to allow attachment. in vitro guide RNA was generated with the HighYield T7 sgRNA synthesis kit (Jena Bioscience #RNT-105), followed by incubation with DNase I-XT (New England Biolabs #M0570) and quick CIP (New England Biolabs #M0525) to remove DNA and 5’ phosphorylation respectively. RNA was purified using the Monarch spin RNA cleanup kit (New England Biolabs #T2040) and 125 ng of guide RNA (target sequence: TCAAAGGCTTTAAACATGTG) was combined with 625 ng of spCas9. Ribonucleoprotein transfection was then performed using the Lipofectamine CRISPRMAX Cas9 transfection reagent (Thermo Fisher Scientific #CMAX000008) according to the manufacturer’s protocol. The culture medium was replaced the following day, and single-cell isolation was performed on day three. Single cells were plated into 96-well plates and clonally expanded. Antibody screening by western blot A549 WT and MMP7 KO cells were washed three times in Hanks’ balanced salt solution (HBSS) (Capricorn Scientific #HBSS-2A) and serum deprived for 48-hours in DMEM media without phenol red (Thermo Fisher Scientific #21063029) supplemented with 1% antibiotic/antimycotic solution. Culture medium was then collected and centrifuged for 500 × g, for 10 minutes at 4°C to eliminate cells and larger contaminants, then for 4500 × g, for 10 minutes at 4°C to eliminate smaller contaminants. Conditioned medium was then concentrated by centrifugation at 4000 × g for 30 minutes at 4°C using Amicon Ultra 15 mL centrifugal filters with a 3 kDa molecular weight cut off (Sigma Aldrich #UFC900396). Culture media was then supplemented with 1× protease inhibitor cocktail (Cell Signaling Technology #7012). For lysate preparation, A549 WT and MMP7 KO cells were washed three times in phosphate buffered saline (PBS) (Thermo Fisher Scientific #70011044) and lysed in RIPA buffer containing 1× of protease inhibitor cocktail, sodium orthovanadate and phenylmethylsulfonyl fluoride (Santa Cruz Biotechnology #sc-24948). Lysates were sonicated (40% amplitude for 5 seconds) three times and incubated for 30 minutes on ice prior to centrifugation at 20,000 × g for 1 hour at 4°C. Protein concentration was confirmed using the Pierce BCA protein assay (Thermo Fisher Scientific #23225) and 30 μg of protein was used for both protein lysates and concentrated cell culture medium. Samples were combined with Laemmli sample buffer (Bio-Rad #1610747) containing 2-mercaptoethanol (final concentration 355 mM) (Sigma Aldrich #M7522) before being heated at 65°C for 10 minutes. Samples were then loaded in precast 4-20% WedgeWell Tris-Glycine Plus midi gels (Thermo Fisher Scientific #WTG42020BOX) alongside Prime-Step prestained broad range protein ladder (BioLegend #773302). SDS-PAGE was then performed in SureLock Tandem Midi Gel tanks (Thermo Fisher Scientific #STM1001) and run at 200V for 1 hour with Tris/Glycine/SDS buffer (Bio-Rad #1610772). Proteins were then transferred to 0.2μm supported nitrocellulose membranes (Cytiva #10600015) using a Criterion blotter with plate electrodes (Bio-Rad #17004070) run at 85V for 45 minutes. Proteins on the blot were then visualised with Ponceau S staining (Thermo Fisher Scientific #161470250) which was scanned to show alongside individual western blots. Blots were blocked with 5% milk for 1 hour except for antibody 71031 which was blocked in 5% BSA in Tris-buffered saline containing 1% Tween 20 (TBST) (Thermo Fisher Scientific #J77500.K2). Primary antibodies were then incubated overnight at 4°C in 5% milk TBST with gentle shaking. Following three ten-minute washes with TBST, horseradish peroxidase (HRP) conjugated secondary antibodies were incubated at a dilution of 1/10000 (0.1 μg/mL) in TBST with 5% milk for 1 hour at room temperature followed by three ten-minute washes with TBST. Membranes were then incubated with either Pierce ECL (Thermo Fisher Scientific #32106) for 1 minute or Clarity Western ECL substrate (Bio-Rad #1705061) for 5 minutes prior to detection with the ImageQuant LAS 4000. Antibody screening by immunoprecipitation Antibody-bead conjugates were prepared by adding 2 μg of antibody to 1 mL of Pierce IP Lysis Buffer (25 mM Tris-HCl pH 7.4, 150 mM NaCl, 1 mM EDTA, 1% NP-40 and 5% glycerol) (Thermo Fisher Scientific #87788) in a microcentrifuge tube, together with 30 μL of protein A (for rabbit antibodies) or protein G (for mouse antibodies) (Thermo Fisher Scientific #10002D and #10004D respectively). Tubes were rocked for 1 hour at 4°C followed by two washes to remove unbound antibody. Culture media from A549 WT were collected as described in the western section above. 0.5 mL aliquots at 1 mg/mL of culture medium were incubated with an antibody-bead conjugate for 18 hours at 4°C. The unbound fractions were collected, and beads were subsequently washed three times with 1.0 mL of IP buffer and processed for SDS-PAGE and western blot on precast midi 4-20% Tris-Glycine polyacrylamide gels. Data availability Underlying data Zenodo: Dataset for the MMP7 antibody screening study contains the underlying data included in a study which characterized ten commercially available antibodies against Matrix metallopeptidase 7 (MMP7) by immunoblot (Western blot) and immunoprecipitation, using a knockout based validation. https://doi.org/10.5281/zenodo.17925527 . Data are available under the terms of the Creative Commons Attribution 4.0 International license (CC-BY 4.0). Acknowledgments This is a summary of independent research funded by both the NC3Rs and MRC and carried out at the National Institute for Health and Care Research (NIHR) Leicester Biomedical Research Centre (BRC). The views expressed are those of the author(s) and not necessarily those of the NC3Rs, the MRC, the NIHR or the Department of Health and Social Care. We gratefully acknowledge the support of Dr. Carl Laflamme and Dr. Riham Ayoubi, whose technical expertise were invaluable to this work. References 1. Liao H, Da C, Liao B, et al. : Roles of matrix metalloproteinase-7 (MMP-7) in cancer. Clin. Biochem. 2021 Jun; 92 : 9–18. PubMed Abstract | Publisher Full Text 2. Jaffar J, Wong M, Fishbein G, et al. : Matrix metalloproteinase-7 is increased in lung bases but not apices in idiopathic pulmonary fibrosis. ERJ Open Res. 2022 Oct 24; 8 (4): 00191–02022. Publisher Full Text 3. Zuo F, Kaminski N, Eugui E, et al. : Gene expression analysis reveals matrilysin as a key regulator of pulmonary fibrosis in mice and humans. Proc. Natl. Acad. Sci. USA. 2002 Apr 30; 99 (9): 6292–6297. PubMed Abstract | Publisher Full Text 4. Bauer Y, White E, Bernard S, et al. : MMP-7 is a predictive biomarker of disease progression in patients with idiopathic pulmonary fibrosis. ERJ Open Res. 2017 Mar 22; 3 (1): 00074–02016. Publisher Full Text 5. Ayoubi R, Ryan J, Bolivar SG, et al. : A consensus platform for antibody characterization. Nat. Protoc. 2024 Dec 17. 6. Ayoubi R, Ryan J, Biddle MS, et al. : Scaling of an antibody validation procedure enables quantification of antibody performance in major research applications. elife. 2023 Nov 5; 12 . Publisher Full Text 7. Biddle MS, Virk HS: YCharOS open antibody characterisation data: Lessons learned and progress made. F1000Res. 2023 Oct 16; 12 . Publisher Full Text 8. Biddle MS, Alende C, Fotouhi M, et al. : A guide to selecting high-performing antibodies for Synaptotagmin-1 (Uniprot ID P21579) for use in western blot, immunoprecipitation, immunofluorescence and flow cytometry. F1000Res. 2024 Jul 19; 13 : 817–817. Publisher Full Text 9. Alshalfie W, Biddle M, Fotouhi M, et al. : The identification of high-performing antibodies for FUS (Uniprot ID: P35637) for use in western blot, immunoprecipitation, immunofluorescence and flow cytometry. F1000Res. 2024 Sep 24; 12 : 376–376. Publisher Full Text 10. Bandrowski A, Pairish M, Eckmann P, et al. : The Antibody Registry: ten years of registering antibodies. Nucleic Acids Res. 2023 Jan 6; 51 (D1): D358–D367. PubMed Abstract | Publisher Full Text 11. Bairoch A: The Cellosaurus, a Cell-Line Knowledge Resource. J. Biomol. Tech. 2018 May 10; 29 (2): 25–38. PubMed Abstract | Publisher Full Text Comments on this article Comments (0) Version 1 VERSION 1 PUBLISHED 19 Jan 2026 ADD YOUR COMMENT Comment Author details Author details 1 University of Leicester College of Life Sciences, Leicester, England, UK 2 Institute for Precision Health, University of Leicester, Leicester, England, UK Michael Biddle Roles: Conceptualization, Data Curation, Formal Analysis, Funding Acquisition, Investigation, Methodology, Project Administration, Resources, Supervision, Validation, Visualization, Writing – Original Draft Preparation, Writing – Review & Editing Jemma Cooper Roles: Data Curation, Formal Analysis, Investigation, Methodology, Validation, Writing – Review & Editing Carolyn Jones Roles: Investigation, Methodology, Project Administration, Writing – Review & Editing Katie Dixon Roles: Data Curation, Writing – Original Draft Preparation, Writing – Review & Editing Harvinder Virk Roles: Conceptualization, Funding Acquisition, Project Administration, Resources, Supervision, Writing – Review & Editing Competing interests For this project, the authors developed partnerships with leading antibody manufacturers and KO cell line providers. The partners provide antibodies and KO cell lines to this project at no cost. These partners include: Abcam, ABCD antibodies, ABclonal, Addgene, Aviva Systems Biology, BioTechne, Cell Signaling Technology, Developmental Studies Hybridoma Bank, GeneTex, Horizon Discovery, Institute for Protein Innovation, MilliporeSigma, Proteintech, Synaptic Systems, Thermo Fisher Scientific. Grant information This work was supported by a grant from the National Centre for the Replacement, Refinement and Reduction of Animals in Research (NC3Rs) and MRC (NC3Rs Ref: NC/NAM0019/1, MRC UKRI076) alongside support from the Leicester Institute for Precision Health. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. Article Versions (1) version 1 Published: 19 Jan 2026, 15:74 https://doi.org/10.12688/f1000research.175973.1 Copyright © 2026 Biddle M et al . This is an open access article distributed under the terms of the Creative Commons Attribution License , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Download Export To Sciwheel Bibtex EndNote ProCite Ref. Manager (RIS) Sente metrics Views Downloads F1000Research - - PubMed Central info_outline Data from PMC are received and updated monthly. - - Citations open_in_new 0 open_in_new 0 open_in_new SEE MORE DETAILS CITE how to cite this article Biddle M, Cooper J, Jones C et al. A guide to selecting high-performing antibodies for MMP7 (UniProt ID: P09237) for use in western blot and immunoprecipitation [version 1; peer review: 2 approved] . F1000Research 2026, 15 :74 ( https://doi.org/10.12688/f1000research.175973.1 ) NOTE: If applicable, it is important to ensure the information in square brackets after the title is included in all citations of this article. COPY CITATION DETAILS track receive updates on this article Track an article to receive email alerts on any updates to this article. TRACK THIS ARTICLE Share Open Peer Review Current Reviewer Status: ? Key to Reviewer Statuses VIEW HIDE Approved The paper is scientifically sound in its current form and only minor, if any, improvements are suggested Approved with reservations A number of small changes, sometimes more significant revisions are required to address specific details and improve the papers academic merit. Not approved Fundamental flaws in the paper seriously undermine the findings and conclusions Version 1 VERSION 1 PUBLISHED 19 Jan 2026 Views 0 Cite How to cite this report: Tiede C. Reviewer Report For: A guide to selecting high-performing antibodies for MMP7 (UniProt ID: P09237) for use in western blot and immunoprecipitation [version 1; peer review: 2 approved] . F1000Research 2026, 15 :74 ( https://doi.org/10.5256/f1000research.193998.r451625 ) The direct URL for this report is: https://f1000research.com/articles/15-74/v1#referee-response-451625 NOTE: it is important to ensure the information in square brackets after the title is included in this citation. Close Copy Citation Details Reviewer Report 27 Feb 2026 Christian Tiede , University of Leeds, Leeds, England, UK Approved VIEWS 0 https://doi.org/10.5256/f1000research.193998.r451625 In this data note, the authors systematically compare the performance and specificity of ten commercially available anti-MMP7 antibodies using Western blot and immunoprecipitation assays. Because intracellular MMP7 levels are low, immunofluorescence staining could not be performed. The study reveals ... Continue reading READ ALL In this data note, the authors systematically compare the performance and specificity of ten commercially available anti-MMP7 antibodies using Western blot and immunoprecipitation assays. Because intracellular MMP7 levels are low, immunofluorescence staining could not be performed. The study reveals substantial differences among the antibodies in their ability to detect MMP7 in both Western blot and immunoprecipitation applications. This work is particularly valuable because it not only identifies reliable primary anti-MMP7 antibodies but also provides practical guidance for selecting appropriate secondary antibodies for immunoprecipitation. As a result, the findings will benefit not only the MMP7 research community but also researchers working with similar detection methods. For completeness, it is recommended that the authors include the dilution information for each primary anti-MMP7 antibody in the Methods section rather than in the captions of Figures 1 and 2. Is the rationale for creating the dataset(s) clearly described? Yes Are the protocols appropriate and is the work technically sound? Yes Are sufficient details of methods and materials provided to allow replication by others? Yes Are the datasets clearly presented in a useable and accessible format? Yes Competing Interests: No competing interests were disclosed. Reviewer Expertise: phage display, protein engineering, antibody alternative scaffolds. I confirm that I have read this submission and believe that I have an appropriate level of expertise to confirm that it is of an acceptable scientific standard. Close READ LESS CITE CITE HOW TO CITE THIS REPORT Tiede C. Reviewer Report For: A guide to selecting high-performing antibodies for MMP7 (UniProt ID: P09237) for use in western blot and immunoprecipitation [version 1; peer review: 2 approved] . F1000Research 2026, 15 :74 ( https://doi.org/10.5256/f1000research.193998.r451625 ) The direct URL for this report is: https://f1000research.com/articles/15-74/v1#referee-response-451625 NOTE: it is important to ensure the information in square brackets after the title is included in all citations of this article. COPY CITATION DETAILS Report a concern Respond or Comment COMMENT ON THIS REPORT Views 0 Cite How to cite this report: Shao J. Reviewer Report For: A guide to selecting high-performing antibodies for MMP7 (UniProt ID: P09237) for use in western blot and immunoprecipitation [version 1; peer review: 2 approved] . F1000Research 2026, 15 :74 ( https://doi.org/10.5256/f1000research.193998.r451624 ) The direct URL for this report is: https://f1000research.com/articles/15-74/v1#referee-response-451624 NOTE: it is important to ensure the information in square brackets after the title is included in this citation. Close Copy Citation Details Reviewer Report 30 Jan 2026 Jieya Shao , Washington University in St Louis, St. Louis, USA Approved VIEWS 0 https://doi.org/10.5256/f1000research.193998.r451624 In this article the authors systematically compared the performance and specificity of ten commercially available anti-MMP7 antibodies using two standard experimentais approaches (Western blot and immunoprecipitation). The authors could not perform immunofluorescence staining due to the fact that the target ... Continue reading READ ALL In this article the authors systematically compared the performance and specificity of ten commercially available anti-MMP7 antibodies using two standard experimentais approaches (Western blot and immunoprecipitation). The authors could not perform immunofluorescence staining due to the fact that the target MMP7 is a secreted protein and its intracellular level is too low in most cell lines. This study is part of a large collaborative initiative to characterize commercial antibodies for different human proteins and offer unbiased guidance to researchers who can select the best antibodies for their specific experimental objectives based on their own interpretations. As a Data Note, this paper successfully achieved its goal with rigorously collected and clearly presented high-quality data, and the results are useful for the research community. The authors are encouraged to capitalize “Western blot” in the text. Also, in the Methods section, under CRISPR/Cas9 genome editing, the first word (In vitro) should be capitalized. Is the rationale for creating the dataset(s) clearly described? Yes Are the protocols appropriate and is the work technically sound? Yes Are sufficient details of methods and materials provided to allow replication by others? Yes Are the datasets clearly presented in a useable and accessible format? Yes Competing Interests: No competing interests were disclosed. Reviewer Expertise: Genome integrity, DNA replication stress, cancer biology I confirm that I have read this submission and believe that I have an appropriate level of expertise to confirm that it is of an acceptable scientific standard. Close READ LESS CITE CITE HOW TO CITE THIS REPORT Shao J. Reviewer Report For: A guide to selecting high-performing antibodies for MMP7 (UniProt ID: P09237) for use in western blot and immunoprecipitation [version 1; peer review: 2 approved] . F1000Research 2026, 15 :74 ( https://doi.org/10.5256/f1000research.193998.r451624 ) The direct URL for this report is: https://f1000research.com/articles/15-74/v1#referee-response-451624 NOTE: it is important to ensure the information in square brackets after the title is included in all citations of this article. COPY CITATION DETAILS Report a concern Respond or Comment COMMENT ON THIS REPORT Comments on this article Comments (0) Version 1 VERSION 1 PUBLISHED 19 Jan 2026 ADD YOUR COMMENT Comment keyboard_arrow_left keyboard_arrow_right Open Peer Review Reviewer Status info_outline Alongside their report, reviewers assign a status to the article: Approved The paper is scientifically sound in its current form and only minor, if any, improvements are suggested Approved with reservations A number of small changes, sometimes more significant revisions are required to address specific details and improve the papers academic merit. Not approved Fundamental flaws in the paper seriously undermine the findings and conclusions Reviewer Reports Invited Reviewers 1 2 Version 1 19 Jan 26 read read Jieya Shao , Washington University in St Louis, St. Louis, USA Christian Tiede , University of Leeds, Leeds, UK Comments on this article All Comments (0) Add a comment Sign up for content alerts Sign Up You are now signed up to receive this alert Browse by related subjects keyboard_arrow_left Back to all reports Reviewer Report 0 Views copyright © 2026 Tiede C. This is an open access peer review report distributed under the terms of the Creative Commons Attribution License , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. 27 Feb 2026 | for Version 1 Christian Tiede , University of Leeds, Leeds, England, UK 0 Views copyright © 2026 Tiede C. This is an open access peer review report distributed under the terms of the Creative Commons Attribution License , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. format_quote Cite this report speaker_notes Responses (0) Approved info_outline Alongside their report, reviewers assign a status to the article: Approved The paper is scientifically sound in its current form and only minor, if any, improvements are suggested Approved with reservations A number of small changes, sometimes more significant revisions are required to address specific details and improve the papers academic merit. Not approved Fundamental flaws in the paper seriously undermine the findings and conclusions In this data note, the authors systematically compare the performance and specificity of ten commercially available anti-MMP7 antibodies using Western blot and immunoprecipitation assays. Because intracellular MMP7 levels are low, immunofluorescence staining could not be performed. The study reveals substantial differences among the antibodies in their ability to detect MMP7 in both Western blot and immunoprecipitation applications. This work is particularly valuable because it not only identifies reliable primary anti-MMP7 antibodies but also provides practical guidance for selecting appropriate secondary antibodies for immunoprecipitation. As a result, the findings will benefit not only the MMP7 research community but also researchers working with similar detection methods. For completeness, it is recommended that the authors include the dilution information for each primary anti-MMP7 antibody in the Methods section rather than in the captions of Figures 1 and 2. Is the rationale for creating the dataset(s) clearly described? Yes Are the protocols appropriate and is the work technically sound? Yes Are sufficient details of methods and materials provided to allow replication by others? Yes Are the datasets clearly presented in a useable and accessible format? Yes Competing Interests No competing interests were disclosed. Reviewer Expertise phage display, protein engineering, antibody alternative scaffolds. I confirm that I have read this submission and believe that I have an appropriate level of expertise to confirm that it is of an acceptable scientific standard. reply Respond to this report Responses (0) Tiede C. Peer Review Report For: A guide to selecting high-performing antibodies for MMP7 (UniProt ID: P09237) for use in western blot and immunoprecipitation [version 1; peer review: 2 approved] . F1000Research 2026, 15 :74 ( https://doi.org/10.5256/f1000research.193998.r451625) NOTE: it is important to ensure the information in square brackets after the title is included in this citation. The direct URL for this report is: https://f1000research.com/articles/15-74/v1#referee-response-451625 keyboard_arrow_left Back to all reports Reviewer Report 0 Views copyright © 2026 Shao J. This is an open access peer review report distributed under the terms of the Creative Commons Attribution License , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. 30 Jan 2026 | for Version 1 Jieya Shao , Washington University in St Louis, St. Louis, USA 0 Views copyright © 2026 Shao J. This is an open access peer review report distributed under the terms of the Creative Commons Attribution License , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. format_quote Cite this report speaker_notes Responses (0) Approved info_outline Alongside their report, reviewers assign a status to the article: Approved The paper is scientifically sound in its current form and only minor, if any, improvements are suggested Approved with reservations A number of small changes, sometimes more significant revisions are required to address specific details and improve the papers academic merit. Not approved Fundamental flaws in the paper seriously undermine the findings and conclusions In this article the authors systematically compared the performance and specificity of ten commercially available anti-MMP7 antibodies using two standard experimentais approaches (Western blot and immunoprecipitation). The authors could not perform immunofluorescence staining due to the fact that the target MMP7 is a secreted protein and its intracellular level is too low in most cell lines. This study is part of a large collaborative initiative to characterize commercial antibodies for different human proteins and offer unbiased guidance to researchers who can select the best antibodies for their specific experimental objectives based on their own interpretations. As a Data Note, this paper successfully achieved its goal with rigorously collected and clearly presented high-quality data, and the results are useful for the research community. The authors are encouraged to capitalize “Western blot” in the text. Also, in the Methods section, under CRISPR/Cas9 genome editing, the first word (In vitro) should be capitalized. Is the rationale for creating the dataset(s) clearly described? Yes Are the protocols appropriate and is the work technically sound? Yes Are sufficient details of methods and materials provided to allow replication by others? Yes Are the datasets clearly presented in a useable and accessible format? Yes Competing Interests No competing interests were disclosed. Reviewer Expertise Genome integrity, DNA replication stress, cancer biology I confirm that I have read this submission and believe that I have an appropriate level of expertise to confirm that it is of an acceptable scientific standard. reply Respond to this report Responses (0) Shao J. Peer Review Report For: A guide to selecting high-performing antibodies for MMP7 (UniProt ID: P09237) for use in western blot and immunoprecipitation [version 1; peer review: 2 approved] . F1000Research 2026, 15 :74 ( https://doi.org/10.5256/f1000research.193998.r451624) NOTE: it is important to ensure the information in square brackets after the title is included in this citation. The direct URL for this report is: https://f1000research.com/articles/15-74/v1#referee-response-451624 Alongside their report, reviewers assign a status to the article: Approved - the paper is scientifically sound in its current form and only minor, if any, improvements are suggested Approved with reservations - A number of small changes, sometimes more significant revisions are required to address specific details and improve the papers academic merit. Not approved - fundamental flaws in the paper seriously undermine the findings and conclusions Adjust parameters to alter display View on desktop for interactive features Includes Interactive Elements View on desktop for interactive features Competing Interests Policy Provide sufficient details of any financial or non-financial competing interests to enable users to assess whether your comments might lead a reasonable person to question your impartiality. 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