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Bcl-W / BCL2L2 Antibody, Rabbit PAb, Antigen Affinity Purified

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    Human BCL-W Antibody Product Information
    Immunogen:Recombinant Human Bcl-W / BCL2L2 protein (Catalog#10059-H08E)
    Clone ID:
    Ig Type:Rabbit IgG
    Concentration:
    Formulation:0.2 μm filtered solution in PBS with 5% trehalose
    Preparation:Produced in rabbits immunized with purified, recombinant Human Bcl-W / BCL2L2 (rh Bcl-W / BCL2L2; Catalog#10059-H08E; Q92843-1; Met 1-Thr 172). Bcl-W / BCL2L2 specific IgG was purified by Human Bcl-W / BCL2L2 affinity chromatography.
    Other BCL-W Antibody Products
    Bcl-W/BCL2L2 Background

    Beta1,4-Galactosyltransferase-I (B4GALT1), one of seven beta1,4-galactosyltransferases, is an enzyme commonly found in the trans-Golgi complex that adds galactose to oligosaccharides. They have an N-terminal hydrophobic signal sequence that directs the protein to the Golgi apparatus and which then remains uncleaved to function as a transmembrane anchor. By sequence similarity, the beta4GalTs form four groups: beta4GalT1 and beta4GalT2, beta4GalT3 and beta4GalT4, beta4GalT5 and beta4GalT6, and beta4GalT7. B4GALT1 gene directs production of B4GALT1 protein using either of two transcription start sites. The product of the smaller transcript serves the traditional biosynthetic role in the Golgi. This form also complexes with α-lactalbumin, a mammary-specific protein, to form lactose synthase. In addition to a biosynthetic role, the protein translated from the longer transcript appears on the plasma membranes of some cells where it serves as a signalling receptor in cell-matrix interactions such as sperm-egg binding.

    Human Bcl-W/BCL2L2 References
  • Hennet T. (2002) The galactosyltransferase family. Cellular and Molecular Life Sciences. 59(7): 1081-95.
  • Landers EA, et al. (2009) Porcine 1, 4-Galactosyltransferase-I Sequence and Expression. Reproduction in Domestic Animals. 44(2): 228-34.
  • Amado M, et al. (2000) Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim Biophys Acta. 1473 (1): 35-53.
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