Monoclonal Anti-Bin1 antibody produced in mouse

Monoclonal Anti-Bin1 (SH3P9, Amphiphysin II, amphl) (mouse IgG2b isotype) is derived from the 99D hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a recombinant polypeptide, containing amino acids 189-398 of human Bin1. Bin1 [Box-dependent myc-interacting protein-1, also known as SH3P9, amphiphysin II and amphl (amphiphysin-like)] is a novel protein that has features of a tumor suppressor. The human BIN1 gene has been mapped to chromosome 2q14. In human and rodent cells it appears as a short-lived (half-life of approx. 2 hrs) monomeric phosphoprotein (approx. 70 kDa). Bin1 molecule appears in different isoforms or conformations, and the localization varies between normal and tumor cells. In normal cells, Bin1 is predominantly nucleoplasmic, but is also present in a subnuclear compartment. In a panel of tumor cells that express Bin1, the predominant localization of the molecule is in the subnuclear compartment.

recombinant polypeptide containing amino acids 189-398 of human Bin1.

Monoclonal Anti-Bin1 antibody produced in mouse has been used in:

• western blotting
• enzyme linked immunosorbent assay (ELISA)
• immunoprecipitation
• immunocytochemistry
• immunohistochemistry
• flow cytometry

Box-dependent myc-interacting protein-1 (Bin1) interacts with and inhibits the oncogenic activity of the myc oncoprotein that has a major role in many human cancers. The loss of Bin1 may contribute to growth deregulation in cancer cells in carcinoma of the breast, colon, lung, cervix, prostate and liver. In bin1 locus mid-2q region that is deleted in approx. 42% of metastatic prostate cancers, and at the syntenic murine locus, in >90% of radiation-induced myeloid leukemias. In addition to the role of Bin1 in controlling neoplastic cell growth and cell cycle by the inhibition of transformation by both myc and the adenovirus E1A protein. Deficits in expression are functionally significant, because ectopic Bin1 can inhibit the growth of tumor cells that lack endogenous expression. Bin1 has also been found to be highly expressed in murine skeletal muscle; overexpression of Bin1 promotes myotube formation and upregulation of myosin heavy chain, while interference with Bin1 expression significantly impairs these processes.

The antibody reacts specifically with a 33-residue segment of the myc-binding domain (MBD, amino acids 323-356) of the human Bin1 molecule. It does not react with the Bin1-related 45 kDa polypeptide.

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