Recombinant Human Integrin alpha V beta 6 Protein, CF

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Recombinant Human Integrin alpha V beta 6 Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
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
N-terminal Sequence
Phe31 ( alpha V subunit) & Gly22 ( beta 6 subunit)
Structure / Form
Noncovalently-linked heterodimer
Predicted Molecular Mass
110.5 kDa ( alpha V subunit), 78.6 kDa ( beta 6 subunit)
145 kDa and 115 kDa, reducing conditions

Product Datasheets

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


Formulation Lyophilized from a 0.2 μm filtered solution in Tris, NaCl and CaCl2.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: 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.
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Background: Integrin alpha V beta 6

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.
Entrez Gene IDs
3685 (Human)
Alternate Names
CD51; Integrin alpha V beta 6; integrin subunit alpha V; ITGAV; MSK8; VNRA; VTNR

Citations for Recombinant Human Integrin alpha V beta 6 Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

8 Citations: Showing 1 - 8
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  1. Ulcerative colitis is characterized by a plasmablast-skewed humoral response associated with disease activity
    Authors: 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
    Nature Medicine, 2022;0(0):.
    Species: Human
    Sample Types: Cell Culture Supernates
    Applications: Bioassay
  2. Measurement of Serum IgG Anti-Integrin alphavbeta6 Autoantibodies Is a Promising Tool in the Diagnosis of Ulcerative Colitis
    Authors: N Rydell, H Ekoff, PM Hellström, R Movérare
    Journal of Clinical Medicine, 2022;11(7):.
    Species: Human
    Sample Types: Serum
    Applications: ELISA Capture
  3. Receptor binding domain of SARS-CoV-2 is a functional alphav-integrin agonist
    Authors: EG Norris, XS Pan, DC Hocking
    bioRxiv : the preprint server for biology, 2022;0(0):.
    Species: N/A
    Sample Types: Recombinant Protein
    Applications: Surface Plasmon Resonance (SPR
  4. The RGD-binding integrins alphavbeta6 and alphavbeta8 are receptors for mouse adenovirus-1 and -3 infection
    Authors: M Bieri, R Hendrickx, M Bauer, B Yu, T Jetzer, B Dreier, PRE Mittl, J Sobek, A Plückthun, UF Greber, S Hemmi
    PloS Pathogens, 2021;17(12):e1010083.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. Truncated Bovine Integrin Alpha-v/Beta-6 as a Universal Capture Ligand for FMD Diagnosis
    PLoS ONE, 2016;11(8):e0160696.
    Species: Virus
    Sample Types: Protein
    Applications: Bioassay
  6. 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.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: ELISA Developmet
  7. Oxidation-induced structural changes of ceruloplasmin foster NGR motif deamidation that promotes integrin binding and signaling.
    Authors: Barbariga, Marco, Curnis, Flavio, Spitaleri, Andrea, Andolfo, Annapaol, Zucchelli, Chiara, Lazzaro, Massimo, Magnani, Giuseppe, Musco, Giovanna, Corti, Angelo, Alessio, Massimo
    J Biol Chem, 2014;289(6):3736-48.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  8. Critical role of flanking residues in NGR-to-isoDGR transition and CD13/integrin receptor switching.
    Authors: 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
    J. Biol. Chem., 2010;285(12):9114-23.
    Species: Human
    Sample Types: Peptide
    Applications: Binding Assay


  1. What is the amino acid sequence of the acidic and basic tails?

    • Acidic and basic tails are added to the protein to help facilitate optimal activity. While we generally include sequence information on the product datasheet, the sequences of these tails are considered confidential information.

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Recombinant Human Integrin alpha V beta 6 Protein, CF
By Anonymous on 12/04/2020
Application: Cell migration/motility

Recombinant Human Integrin alpha V beta 6 Protein, CF
By Anonymous on 10/26/2020
Application: Binding assay/Protein-protein interaction