Anti-Supervillin antibody produced in rabbit

Supervillin is an F-actin-binding protein originally isolated from bovine neutrophils. It has two isoforms of reported 205/250 kDa. The longer isoform named archvillin is muscle specific. Supervillin is a tightly bound peripheral membrane protein that is concentrated at sites of epithelial cell-cell adhesion. The COOH-terminus of supervillin is homologous to villin/gelsolin. The NH2-terminus contains functional nuclear localization sequences and F-actin and myosin II binding domains. Supervillin is found in many cells of several species, but is most abundant in muscle, bone marrow, thyroid gland and salivary gland.

synthetic peptide corresponding to amino acid residues 900-918 of human supervillin with C-terminal added cysteine, conjugated to KLH. The corresponding sequence differs by two amino acids in mouse.

Anti-Supervillin antibody produced in rabbit has been used in:

• immunoblotting
• chromatin immunoprecipitation (ChIP)
• immunofluorescence

Supervillin participates in cell-cell adhesion, motility regulation and information transfer between cell compartments. It has been suggested that supervillin may mediate actin and myosin II filament organization at cholesterol-rich membrane domains. Supervillin has been identified as a transcriptional activator of the androgen receptor. Increased levels of supervillin are found in many carcinoma cell lines, including HeLa S3 cervical carcinoma, SW480 adenocarcinoma and A549 lung carcinoma cells.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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