Description
Human Integrin alpha V beta 8 (ITGAV&ITGB8) Heterodimer Protein, His Tag&Tag Free | IT8-H52W4-100ug| Gentaur Distribution US, UK & Europe
Integrin alpha V beta 8 (ITGAV & ITGB8 or ITGAVB8) is expressed in yolk sac, placenta, brain perivascular astrocytes, Schwann cells, renal glomerular mesangial cells and pulmonary epithelial cells. Unlike other alpha V integrins, ITGAVB8 does not appear to assume different activation states, and the cytoplasmic tail does not connect to the cytoskeleton. It binds ligands containing an RGD motif, including vitronectin, fibrin and the latency associated peptide (LAP) of the latent TGF-beta complex. High affinity binding of alpha V beta 8 to LAP allows proteolytic cleavage by MT1-MMP, which releases active TGF-beta. This mechanism differs from that of alpha V beta 6, the other alpha V integrin which can activate TGF-beta from latency through non-proteolytic mechanisms. Downstream effects of TGF-beta activation include control of cell growth and associated vascularization.
Source: Human ITGAV&ITGB8 Heterodimer Protein, His Tag&Tag Free (IT8-H52W4) is expressed from human 293 cells (HEK293). It contains AA Phe 31 - Val 992 (ITGAV) & Glu 43 - Arg 684 (ITGB8) (Accession # NP_002201.1 (ITGAV) & NP_002205.1 (ITGB8) ).
Format: Powder.
Tag: C-10×His | Native.
Expression System: HEK293.
Expression Region: Phe 31 - Val 992 (ITGAV) & Glu 43 - Arg 684 (ITGB8).
Conjugate: Unconjugated.
Molecular Weight: 112.9 kDa (ITGAV) & 76.5 kDa (ITGB8).
Characteristics: Human ITGAV&ITGB8 Heterodimer Protein, His Tag&Tag Free, produced by co-expression of ITGAV and ITGB8, has a calculated MW of 112.9 kDa (ITGAV) and 76.5 kDa (ITGB8). Subunit ITGAV is fused with polyhistidine tag at the C-terminus and followed by a acidic tail and subunit ITGB8 contains no tag but a basic tail at the C-terminus. The non-reducing (NR) protein migrates as 130-150 kDa (ITGAV) and 80-90 kDa (ITGB8) respectively due to glycosylation.
Purity: 95%.
Buffer: 50 mM Tris, 100 mM NaCl, pH8.0.
Storage Conditions: -20℃.
Shipping Conditions: RT
