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.
- Anti-Human B4GALT1/GGTB2 Antibody, Cat No:11220-R001
- Anti-Human Rabbit Polyclonal Antibody, Cat No:11220-RP01
- Anti-Human B4GALT1/GGTB2 Antibody, Cat No:11220-RP02
- Anti-Human B4GALT1/GGTB2 Antibody, Cat No:10059-RP02
Bcl-W/BCL2L2 ELISA Pair sets
Bcl-W/BCL2L2 cDNA Clones
B4GALT1, B4GAL-T1, GGTB2, beta4Gal-T1, DKFZp686N19253, GT1, GTB, MGC50983 [Homo sapiens]
B4GALT1, Ggtb2, Ggtb, B-1,4-GalT, RP23-135L5.6, AA407245, GalT [Mus musculus]
Entrez Gene summary for Bcl-W/BCL2L2:
This gene encodes a member of the BCL-2 protein family. The proteins of this family form hetero- or homodimers and act as anti- and pro-apoptotic regulators. Expression of this gene in cells has been shown to contribute to reduced cell apoptosis under cytotoxic conditions. Studies of the related gene in mice indicated a role in the survival of NGF- and BDNF-dependent neurons. Mutation and knockout studies of the mouse gene demonstrated an essential role in adult spermatogenesis. Alternative splicing results in multiple transcript variants. Read-through transcription also exists between this gene and the neighboring downstream PABPN1 (poly(A) binding protein, nuclear 1) gene.
OMIM - description for Bcl-W/BCL2L2:
Using degenerate PCR, Gibson et al. (1996) cloned human BCLW, a novel homolog of BCL2 (151430), a prototypic mammalian regulator of cell death. Several other homologs of BCL2 are known, including BCLX (600039), BAX (600040), and BAK (600516). The BCLW gene encodes a 193-amino acid polypeptide. Gibson et al. (1996) also isolated the mouse Bclw gene; its amino acid sequence is 99% identical to that of the human gene. Mouse Bclw is expressed as a 3.7-kb mRNA in a variety of tissues, with highest expression in brain, colon, and salivary gland. In mouse hematopoietic cell lines, Bclw is expressed in myeloid cells and to a lesser extent in lymphoid cells. Like Bcl2, expressed Bclw promoted cell survival under a variety of cytotoxic conditions.
Wikipedia summary for Bcl-W/BCL2L2:
Bcl-2-like protein 2 is a protein that in humans is encoded by the BCL2L2 gene.This gene encodes a pro-survival (anti-apoptotic) member of the bcl-2 protein family. The proteins of this family form hetero- or homodimers and act as anti- and pro-apoptotic regulators. Expression of this gene in cells has been shown to contribute to reduced cell apoptosis under cytotoxic conditions. Studies of the related gene in mice indicated a role in the survival of NGF- and BDNF-dependent neurons. Mutation and knockout studies of the mouse gene demonstrated an essential role in adult spermatogenesis.Relative to its Bcl-2 counterparts there is considerably less data on this particular protein however much effort is being made to further understand its cellular roles. Located on chromosome 14q11 it appears to be redundant in most tissues apart from specific examples. It was originally discovered by Leonie Gibson, Suzanne Cory and colleagues at the Walter and Eliza Hall Institute of Medical Research, who called it Bcl-w..
Recommended name: Bcl-2-like protein 2 Short name=Bcl2-L-2
The BH4 motif seems to be involved in the anti-apoptotic function. The BH1 and BH2 motifs form a hydrophobic groove which acts as a docking site for the BH3 domain of some pro-apoptotic proteins. The C-terminal residues of BCL2L2 fold into the BH3-binding cleft and modulate pro-survival activity by regulating ligand access. When BH3 domain-containing proteins bind, they displace the C-terminus, allowing its insertion into the membrane and neutralizing the pro-survival activity of BCL2L2.
Belongs to the Bcl-2 family.
|Subcellular location:||Mitochondrion membrane; Peripheral membrane protein. Note: Loosely associated with the mitochondrial membrane in healthy cells. During apoptosis, tightly bound to the membrane.|
Expressed (at protein level) in a wide range of tissues with highest levels in brain, spinal cord, testis, pancreas, heart, spleen and mammary glands. Moderate levels found in thymus, ovary and small intestine. Not detected in salivary gland, muscle or liver. Also expressed in cell lines of myeloid, fibroblast and epithelial origin. Not detected in most lymphoid cell lines.
General information above from UniProt
Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX.
- Bcl-W/BCL2L2 promotes cell survival
- Bcl-W/BCL2L2 mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX