Vinculin Protein, Human (GST)

Vinculin Protein, an actin-binding protein, is crucial for cell adhesion, morphology, and mechanosensing. It regulates E-cadherin expression and enhances mechanosensing. Vinculin forms complexes with THSD1, PTK2/FAK1, TLN1, and VCL, and interacts with APBB1IP, NRAP, CTNNB1, SYNM, SORBS1, and CTNNA1. Its interaction with CTNNA1 is necessary for localization to cell-cell junctions. Vinculin also binds to ACTN4, causing conformational changes. Vinculin Protein, Human (GST) is the recombinant human-derived Vinculin protein, expressed by E. coli, with N-GST labeled tag. The total length of Vinculin Protein, Human (GST) is 234 a.a., with molecular weight of ~53.0 kDa.

Vinculin Protein, an actin filament (F-actin)-binding protein, is extensively involved in cell-matrix adhesion and cell-cell adhesion, playing crucial roles in cell morphology, locomotion, and mechanosensing. It regulates the expression of cell-surface E-cadherin and enhances mechanosensing through the E-cadherin complex. Vinculin exhibits self-association properties and forms a complex with THSD1, PTK2/FAK1, TLN1, and VCL. It interacts with APBB1IP, NRAP, TLN1, CTNNB1, SYNM, SORBS1, and CTNNA1, and its interaction with CTNNA1 is necessary for its localization to cell-cell junctions and regulation of E-cadherin expression. Additionally, Vinculin binds to ACTN4, triggering conformational changes.

Human

E. coli

N-GST

P18206 (2P-235E)

7414  [NCBI]

PVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVE

Approximately 53.0 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.