Vinculin (VCL) Rabbit Polyclonal Antibody

Specifications

Product Data
Applications	WB
Recommend Dilution	WB 1:500 - 1:2000
Reactivity	Human, Mouse, Rat
Host	Rabbit
Clonality	Polyclonal
Immunogen	Recombinant protein of human VCL
Formulation	Store at -20C or -80C. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3
Concentration	lot specific
Purification	Affinity purification
Conjugation	Unconjugated
Storage Condition	Store at -20°C as received.
Gene Name	vinculin
Database Link	NP_003364 Entrez Gene 22330 MouseEntrez Gene 305679 RatEntrez Gene 7414 Human UniProt ID P18206
Background	Vinculin is a cytoskeletal protein that plays an important role in the regulation of focal adhesions and embryonic development. Three structural vinculin domains include an amino-terminal head, a short, flexible proline-rich region and a carboxy-terminal tail. In the inactive state, the head and tail domains of vinculin interact to form a closed confirmation. The open and active form of vinculin translocates to focal adhesions where it is thought to be involved in anchoring F-actin to the membrane and regulation of cell migration. Phospholipid binding to the tail domain and subsequent phosphorylation of vinculin at Ser1033 and Ser1045 by PKC-a and Tyr100 and Tyr1065 by Src kinases weakens the head-tail interaction. This change in vinculin allows the binding of a number of other proteins, including talin, a-actinin and paxillin, which disrupts the head-tail interaction and initiates the conformational change from the inactive to active state. Vinculin deficiencies are associated with a decrease in cell adhesion and an increase in cell motility, suggesting a possible role in metastatic growth. This is supported by a recently demonstrated relationship between decreased vinculin expression and increased carcinogenesis and metastasis in colorectal carcinoma.
Synonyms	CMD1W; CMH15; HEL114; MV; MVCL
Reference Data
Protein Families	Druggable Genome
Protein Pathways	Adherens junction, Focal adhesion, Leukocyte transendothelial migration, Regulation of actin cytoskeleton

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