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.
Source
Chinese Hamster Ovary cell line, CHO-derived human Integrin alpha V beta 6 protein
Human Integrin alpha V (Phe31-Val992) Accession # NP_002201.1
His-Pro
GGGSGGGS
Acidic Tail
Human Integrin beta 6 (Gly22-Asn707) Accession # P18564
<1.0 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
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.
SDS-PAGE
118-144 kDa and 93-113 kDa, reducing conditions
Publications
Read Publications using 3817-AV in the following applications:
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.
Buffer
Lyophilized from a 0.2 μm filtered solution in Tris, NaCl and CaCl2.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
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
ITGAV
MSK8
VNRA
VTNR
Background
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).
Hynes, R.O. (2002) Cell 110:673.
Sheppard, D. (2004) Curr. Opin. Cell Biol. 16:552.
Bandyopadhyay, A. and S. Raghavan (2009) Curr. Drug Targets 10:645.
Suzuki, S. et al. (1987) J. Biol. Chem. 262:14080.
Sheppard, D. et al. (1990) J. Biol. Chem. 265:11502.
Dixit, R.B. et al. (1996) J. Biol. Chem. 271:25976.
Munger, J.S. et al. (1999) Cell 96:319.
Fontana, L. et al. (2005) FASEB J. 19:1798.
Jenkins, R.G. et al. (2006) J. Clin. Invest. 116:1606.
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