Human Integrin alpha 6 beta 1 Heterodimer Antibody
Human Integrin alpha 6 beta 1 Heterodimer Antibody Summary
Phe24-Ser1012(Integrin alpha 6) and Gln21-Asp728 (Integrin beta1)
Accession # NP_000201
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Integrin alpha 6 beta 1 in Human PBMC by Flow Cytometry Human PBMC were stained with (A) Rabbit Anti-Human Integrin a6 beta 1 Monoclonal Antibody (Catalog # MAB7809) or (B) Rabbit IgG control antibody (Catalog # MAB1050) followed by PE-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog # F0110) and Mouse anti-Human CD3 APC-conjugated Monoclonal Antibody (Catalog # FAB100A). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Integrin alpha 6 beta 1
Integrin alpha 6 beta 1, also called platelet glycoprotein GPIc-IIa, is a laminin binding integrin that is expressed on T cells, monocytes, endothelial cells, stem cells, and platelets (1-9). The non-covalent heterodimer is composed of ~150 kDa alpha 6/CD49f and 130 kDa beta 1/CD29 type I transmembrane glycoprotein subunits (2). While alpha 6 pairs only with beta 1 or beta 4, twelve integrins share the beta 1 subunit (1-5). The alpha 6 subunit is cleaved into extracellular heavy and transmembrane light chains (3). Alternative splicing in the human alpha 6 extracellular domain (ECD) at amino acid (aa) 216 creates X1 (ubiquitous), X2 and X1X2 isoforms, while splicing at a mouse or human cytoplasmic site creates A and B isoforms (10, 11). These forms do not appear to alter the binding specificity (4, 10, 11). The beta 1 ECD contains a vWFA domain, which participates in binding. Each subunit then has a transmembrane sequence and a short cytoplasmic tail. The dimer is folded when it is least active. Divalent cations and intracellular (inside-out) signaling convert it to its most active, extended and open conformation (1, 2). The human alpha 6 (X1) heavy chain shares 94‑95% aa identity with mouse, rat, bovine, and canine alpha 6, and the human beta 1 ECD shares 92‑96% aa sequence identity with rat, bovine, mouse, and feline beta 1. alpha 6 beta 1 shows broad specificity for adhesion to laminin isoforms (4, 10). Its expression on human and mouse pluripotent stem cells is important for attachment, expansion, and self‑renewal on LN‑511 (laminin alpha 5 beta 1 gamma 1) (6, 7). The secreted protein Netrin-4 and the laminin gamma 1 subunit form an adhesion‑activating complex with alpha 6 beta 1 on mouse neural stem cells and human lymphatic endothelial cells that promotes lymphangiogenesis (8, 9). alpha 6 beta 1 up‑regulation on cancers such as prostate, glioma, and hepatoma is reported to enhance tumorigenicity, motility, invasion and metastasis (12‑14). alpha 6 beta 1 cleavage via uPA (urokinase-type plasminogen activator) facilitates tumorigenicity in prostate cancers, and interaction of hepatoma alpha 6 beta 1 with EMMPRIN/CD147 may also enhance tumorigenicity by inducing uPA and other metalloproteinases (12, 13).
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