Recombinant Human B4GALT1 protein, GST-tagged
Cat.No. : | B4GALT1-028H |
Product Overview : | Human B4GALT1 partial ORF ( NP_001488, 44 a.a. - 153 a.a.) recombinant protein with GST-tag at N-terminal. |
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Description : | This gene is one of seven beta-1,4-galactosyltransferase (beta4GalT) genes. They encode type II membrane-bound glycoproteins that appear to have exclusive specificity for the donor substrate UDP-galactose; all transfer galactose in a beta1,4 linkage to similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a distinct function in the biosynthesis of different glycoconjugates and saccharide structures. As type II membrane proteins, 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. This gene is unique among the beta4GalT genes because it encodes an enzyme that participates both in glycoconjugate and lactose biosynthesis. For the first activity, the enzyme adds galactose to N-acetylglucosamine residues that are either monosaccharides or the nonreducing ends of glycoprotein carbohydrate chains. The second activity is restricted to lactating mammary tissues where the enzyme forms a heterodimer with alpha-lactalbumin to catalyze UDP-galactose + D-glucose <=> UDP + lactose. The two enzymatic forms result from alternate transcription initiation sites and post-translational processing. Two transcripts, which differ only at the 5 end, with approximate lengths of 4.1 kb and 3.9 kb encode the same protein. The longer transcript encodes the type II membrane-bound, trans-Golgi resident protein involved in glycoconjugate biosynthesis. The shorter transcript encodes a protein which is cleaved to form the soluble lactose synthase. [provided by RefSeq] |
Source : | Wheat Germ |
Species : | Human |
Tag : | GST |
Form : | 50 mM Tris-HCI, 10 mM reduced Glutathione, pH=8.0 in the elution buffer. |
Molecular Mass : | 37.84 kDa |
AA Sequence : | GRDLSRLPQLVGVSTPLQGGSNSAA AIGQSSGELRTGGARPPPPLGASSQ PRPGGDSSPVVDSGPGPASNLTSVP VPHTTALSLPACPEESPLLVGPMLI EFNMPVDLEL |
Notes : | Best use within three months from the date of receipt of this protein. |
Storage : | Store at -80 centigrade. Aliquot to avoid repeated freezing and thawing. |
Gene Name : | B4GALT1 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1 [ Homo sapiens ] |
Official Symbol : | B4GALT1 |
Synonyms : | B4GALT1; UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1; GGTB2; beta-1,4-galactosyltransferase 1; beta4Gal T1; lactose synthase; beta-1,4-GalTase 1; glycoprotein-4-beta-galactosyltransferase 2; UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1; UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1; GT1; GTB; CDG2D; B4GAL-T1; beta4Gal-T1; MGC50983; DKFZp686N19253; |
Gene ID : | 2683 |
mRNA Refseq : | NM_001497 |
Protein Refseq : | NP_001488 |
MIM : | 137060 |
UniProt ID : | P15291 |
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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Customer Reviews (3)
Write a reviewQuick shipping, excellent quality.
High quality, excellent performance.
Reliable, good for research.
Q&As (7)
Ask a questionIt synthesizes lactosylceramide, a building block for complex glycosphingolipids in glycoprotein and glycolipid synthesis.
B4GALT1 is crucial for glycosylation, attaching galactose to proteins and lipids.
B4GALT1 is widely expressed but has higher activity in the liver, kidney, and intestine.
Therapeutic strategies include targeting B4GALT1 to modulate its activity in cancer and other diseases.
Altered B4GALT1 expression is linked to cancer, influencing tumor growth and metastasis.
Genetic mutations in B4GALT1 are associated with some rare metabolic disorders.
It modulates immune responses by altering glycosylation patterns on immune cells.
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