Integrin alpha V Protein, Human (P. pastoris, His)

Integrin α V beta 5 proteins, specifically the α-V (ITGAV) subunit, are multifunctional receptors for ligands such as vitronectin and fibronectin and recognize RGD sequences. ITGAV: ITGB3 binds fractalkine and acts as a coreceptor in CX3CR1-dependent signaling. Integrin alpha V Protein, Human (P. pastoris, His) is the recombinant human-derived Integrin alpha V , Human (P. pastoris, His) protein, expressed by P. pastoris, with C-6*His labeled tag.

The Integrin alpha V beta 5 protein, specifically the alpha-V (ITGAV) integrin subunit, serves as a versatile receptor for a range of ligands, including vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, and vWF. Recognizing the sequence R-G-D in various ligands, ITGAV:ITGB3 binds to fractalkine, acting as a coreceptor in CX3CR1-dependent fractalkine signaling. Additionally, it forms essential binding interactions with NRG1, FGF1, FGF2, IGF1, IGF2, IL1B, PLA2G2A, fibrillin-1 (FBN1), and CD40LG, contributing to diverse signaling pathways. Notably, the ITGAV:ITGB3 or ITGAV:ITGB6 complex acts as a receptor for transforming growth factor beta-1 (TGF-beta-1), mediating its release from regulatory Latency-associated peptide (LAP) and playing a crucial role in TGF-beta-1 activation. Furthermore, ITGAV:ITGB5 functions as a receptor for Adenovirus type C during microbial infection. The integrative and multifunctional nature of Integrin alpha V beta 5 underscores its pivotal role in mediating diverse cellular responses and signaling cascades.

Human

P. pastoris

C-6*His

P06756 (D891-T1048)

3685

Partial

DLALSEGDIHTLGCGVAQCLKIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVTTNVTWGIQPAPMPVPVWVIILAVLAGLLLLAVLVFVMYRMGFFKRVRPPQEEQEREQLQPHENGEGNSET

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.