Recombinant Human Integrin alpha V beta 6 Protein, CF


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Product Details

Reactivity HuSpecies Glossary
Applications Binding Activity

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Recombinant Human Integrin alpha V beta 6 Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized Recombinant Human Integrin  alpha V beta 6 at 2.0 µg/mL can bind Recombinant Human LAP TGF‑ beta 1 (Catalog # 246-LP) with an apparent Kd <0.1 nM.
Chinese Hamster Ovary cell line, CHO-derived human Integrin alpha V beta 6 protein
Human Integrin alpha V
Accession # NP_002201.1
His-Pro GGGSGGGS Acidic Tail
Human Integrin beta 6
Accession # P18564
His-His-Pro GGGSGGGS Basic Tail
N-terminus C-terminus
Accession #
N-terminal Sequence
Phe31 ( alpha V subunit) & Gly22 ( beta 6 subunit)
Structure / Form
Noncovalently-linked heterodimer
Protein/Peptide Type
Recombinant Proteins
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.


  • Binding Activity
Theoretical MW
110.5 kDa ( alpha V subunit), 78.6 kDa ( beta 6 subunit).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
145 kDa and 115 kDa, reducing conditions
Read Publications using
3817-AV in the following applications:

Packaging, Storage & Formulations

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in Tris, NaCl and CaCl2.
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Integrin alpha V beta 6 Protein, CF

  • CD51
  • Integrin alpha V beta 6
  • integrin subunit alpha V
  • MSK8
  • VNRA
  • VTNR


Integrin alpha V beta 6 is one of five alpha V integrins and the sole beta 6 integrin (1, 2). The non-covalent heterodimer of 170 kDa alpha V/CD51 and 95 kDa beta 6 integrin subunits is expressed exclusively on subsets of epithelial cells, especially during development, after injury or inflammation, or on many carcinomas (2-5). The ligand interaction site of alpha V beta 6 is in the N-terminal head region formed by an interaction of the beta 6 vWFA domain with the alpha V beta-propeller structure (2). The alpha V subunit contains domains termed thigh, calf, and calf-2 with a divalent cation-binding site found at a position equivalent to the “knee”. The 962 aa human alpha V ECD (4), which is cleaved at aa 890 but remains associated, shares 92-95% aa sequence identity with mouse and bovine alpha V, while the 685 aa human beta 6 ECD (5) shares 90-93% aa sequence identity with mouse, rat, bovine, ovine, and porcine beta 6. Each subunit has a transmembrane sequence and a short cytoplasmic tail connected to the cytoskeleton. The beta 6 C-terminal 11 amino acid (aa) cytoplasmic sequence transduces a signal, enhancing proliferation and inducing MMP-9 expression (6). Either “inside-out” signaling or Mg2+ or Mn2+ binding unfolds and activates the integrin (1). Active alpha V beta 6 binds matrix proteins fibronectin and tenascin C (2). It also binds the TGF-beta latency‑associated peptide (LAP) and activates TGF-beta 1 or TGF-beta 3 from large latent complexes (7). This activation requires interaction with LTBP-1 and fibronectin, and is enhanced by PAR-1 (8, 9). Deletion of beta 6 ablates tonic inhibition of alveolar macrophages by TGF-beta , inhibits intestinal regulatory T cell production, and predisposes mice to inflammatory reactions in the skin, lungs, and intestines where irritations and microbial challenges are frequent (10-12). High alpha V beta 6 expression in carcinomas may contribute to progression through its effects on TGF-beta and MMP activity (3). The foot-and-mouth disease virus and several other viruses can use alpha V beta 6 as a receptor, and soluble alpha V beta 6 may block virus infectivity in vitro (13, 14).
  1. Hynes, R.O. (2002) Cell 110:673.
  2. Sheppard, D. (2004) Curr. Opin. Cell Biol. 16:552.
  3. Bandyopadhyay, A. and S. Raghavan (2009) Curr. Drug Targets 10:645.
  4. Suzuki, S. et al. (1987) J. Biol. Chem. 262:14080.
  5. Sheppard, D. et al. (1990) J. Biol. Chem. 265:11502.
  6. Dixit, R.B. et al. (1996) J. Biol. Chem. 271:25976.
  7. Munger, J.S. et al. (1999) Cell 96:319.
  8. Fontana, L. et al. (2005) FASEB J. 19:1798.
  9. Jenkins, R.G. et al. (2006) J. Clin. Invest. 116:1606.
  10. Huang, X.Z. et al. (1996) J. Cell Biol. 133:921.
  11. Morris, D.G. et al. (2003) Nature 422:169.
  12. Chen, X. et al. (2011) J. Leukoc. Biol. 90:751.
  13. Berryman, S. et al. (2005) J. Virol. 79:8519.
  14. Heikkila, O. et al. (2009) J. Gen. Virol. 90:197.

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Publications for Integrin alpha V beta 6 (3817-AV)(8)

We have publications tested in 3 confirmed species: Human, N/A, Virus.

We have publications tested in 5 applications: Binding Assay, Bioassay, ELISA Capture, ELISA Developmet, Surface Plasmon Resonance (SPR.

Filter By Application
Binding Assay
ELISA Capture
ELISA Developmet
Surface Plasmon Resonance (SPR
All Applications
Filter By Species
All Species
Showing Publications 1 - 8 of 8.
Publications using 3817-AV Applications Species
EG Norris, XS Pan, DC Hocking Receptor binding domain of SARS-CoV-2 is a functional alphav-integrin agonist bioRxiv : the preprint server for biology, 2022;0(0):. 2022 [PMID: 35441172] (Surface Plasmon Resonance (SPR, N/A) Surface Plasmon Resonance (SPR N/A
N Rydell, H Ekoff, PM Hellström, R Movérare Measurement of Serum IgG Anti-Integrin alphavbeta6 Autoantibodies Is a Promising Tool in the Diagnosis of Ulcerative Colitis Journal of Clinical Medicine, 2022;11(7):. 2022 [PMID: 35407486] (ELISA Capture, Human) ELISA Capture Human
M Uzzan, JC Martin, L Mesin, AE Livanos, T Castro-Dop, R Huang, F Petralia, G Magri, S Kumar, Q Zhao, AK Rosenstein, M Tokuyama, K Sharma, R Ungaro, R Kosoy, D Jha, J Fischer, H Singh, ME Keir, N Ramamoorth, WEO Gorman, BL Cohen, A Rahman, F Cossarini, A Seki, L Leyre, ST Vaquero, S Gurunathan, EK Grasset, B Losic, M Dubinsky, AJ Greenstein, Z Gottlieb, P Legnani, J George, H Irizar, A Stojmirovi, C Brodmerkel, A Kasarkis, BE Sands, G Furtado, SA Lira, ZK Tuong, HM Ko, A Cerutti, CO Elson, MR Clatworthy, M Merad, M Suárez-Far, C Argmann, JA Hackney, GD Victora, GJ Randolph, E Kenigsberg, JF Colombel, S Mehandru Ulcerative colitis is characterized by a plasmablast-skewed humoral response associated with disease activity Nature Medicine, 2022;0(0):. 2022 [PMID: 35190725] (Bioassay, Human) Bioassay Human
M Bieri, R Hendrickx, M Bauer, B Yu, T Jetzer, B Dreier, PRE Mittl, J Sobek, A Plückthun, UF Greber, S Hemmi The RGD-binding integrins alphavbeta6 and alphavbeta8 are receptors for mouse adenovirus-1 and -3 infection PloS Pathogens, 2021;17(12):e1010083. 2021 [PMID: 34910784] (Bioassay, Human) Bioassay Human
Systematic site-directed mutagenesis of the Helicobacter pylori CagL protein of the Cag type IV secretion system identifies novel functional domains Sci Rep, 2016;6(0):38101. 2016 [PMID: 27922023] (ELISA Developmet, Human) ELISA Developmet Human
Truncated Bovine Integrin Alpha-v/Beta-6 as a Universal Capture Ligand for FMD Diagnosis PLoS ONE, 2016;11(8):e0160696. 2016 [PMID: 27494135] (Bioassay, Virus) Bioassay Virus
Barbariga , Marco, Curnis , Flavio, Spitaleri , Andrea, Andolfo , Annapaol, Zucchelli , Chiara, Lazzaro , Massimo, Magnani , Giuseppe, Musco , Giovanna, Corti , Angelo, Alessio , Massimo Oxidation-induced structural changes of ceruloplasmin foster NGR motif deamidation that promotes integrin binding and signaling. J Biol Chem, 2014;289(6):3736-48. 2014 [PMID: 24366863] (Bioassay, Human) Bioassay Human
Curnis F, Cattaneo A, Longhi R, Sacchi A, Gasparri AM, Pastorino F, Di Matteo P, Traversari C, Bachi A, Ponzoni M, Rizzardi GP, Corti A Critical role of flanking residues in NGR-to-isoDGR transition and CD13/integrin receptor switching. J. Biol. Chem., 2010;285(12):9114-23. 2010 [PMID: 20064928] (Binding Assay, Human) Binding Assay Human

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