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Mouse Anti-B4GALT1 Recombinant Antibody (CBYY-0092) (CBMAB-0092-YY)

This product is mouse antibody that recognizes B4GALT1. The antibody CBYY-0092 can be used for immunoassay techniques such as: ICC, WB
See all B4GALT1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBYY-0092
Antibody Isotype
IgG1
Application
ELISA

Basic Information

Immunogen
Recombinant Human B4GALT1 protein.
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.4
Preservative
None
Concentration
Batch dependent
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Beta-1,4-Galactosyltransferase 1
Introduction
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 forMouse a heterodimer with alpha-lactalbumin to catalyze UDP-galactose + D-glucose <=> UDP + lactose. The two enzymatic forMouse 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.
Entrez Gene ID
2683
UniProt ID
P15291
Alternative Names
Beta-1,4-Galactosyltransferase 1; UDP-Galactose:Beta-N-Acetylglucosamine Beta-1,4-Galactosyltransferase 1; UDP-Gal:BetaGlcNAc Beta 1,4- Galactosyltransferase, Polypeptide 1; UDP-Gal:Beta-GlcNAc Beta-1,4-Galactosyltransferase 1; Beta-1,4-GalTase 1; Beta4Gal-T1; B4GAL-T1; GGTB2;
Function
Beta-1,4-galactosyltransferase 1: The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.
Processed beta-1,4-galactosyltransferase 1: The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix.
Biological Process
Acute inflammatory response Source: Ensembl
Angiogenesis involved in wound healing Source: Ensembl
Binding of sperm to zona pellucida Source: Reactome
Cell adhesion Source: Ensembl
Development of secondary sexual characteristics Source: Ensembl
Epithelial cell development Source: Ensembl
Extracellular matrix organization Source: Ensembl
Galactose metabolic process Source: Ensembl
Glycosylation Source: GO_Central
Keratan sulfate biosynthetic process Source: Reactome
Lactose biosynthetic process Source: Reactome
Leukocyte migration Source: Ensembl
Negative regulation of cell population proliferation Source: Ensembl
neutrophil degranulation Source: Reactome
Oligosaccharide biosynthetic process Source: UniProtKB
Penetration of zona pellucida Source: Ensembl
Positive regulation of apoptotic process Source: Ensembl
Positive regulation of epithelial cell proliferation involved in wound healing Source: Ensembl
Protein N-linked glycosylation Source: UniProtKB
Regulation of acrosome reaction Source: Ensembl
Cellular Location
Isoform Long: Cell membrane; Golgi stack membrane; Cell surface; Filopodium. Found in trans cisternae of Golgi but is mainly localized at the plasma membrane (PubMed:1714903). B4GALT1 cell surface expression is regulated by UBE2Q1 (By similarity).
Isoform Short: Golgi stack membrane. Found in trans cisternae of Golgi.
Processed beta-1,4-galactosyltransferase 1: Secreted. Soluble form found in body fluids.
Involvement in disease
Congenital disorder of glycosylation 2D (CDG2D): A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.
Topology
Cytoplasmic: 1-24 aa
Helical: 25-44 aa
Lumenal: 45-398 aa
PTM
The soluble form derives from the membrane forms by proteolytic processing.

Chen, Y., Su, L., Huang, C., Wu, S., Qiu, X., Zhao, X., ... & Wong, P. P. (2021). Galactosyltransferase B4GALT1 confers chemoresistance in pancreatic ductal adenocarcinomas by upregulating N-linked glycosylation of CDK11p110. Cancer Letters, 500, 228-243.

Di Buduo, C. A., Giannini, S., Abbonante, V., Rosti, V., Hoffmeister, K. M., & Balduini, A. (2021). Increased B4GALT1 expression is associated with platelet surface galactosylation and thrombopoietin plasma levels in MPNs. Blood, 137(15), 2085-2089.

Wiertelak, W., Sosicka, P., Olczak, M., & Maszczak-Seneczko, D. (2020). Analysis of homologous and heterologous interactions between UDP-galactose transporter and beta-1, 4-galactosyltransferase 1 using NanoBiT. Analytical biochemistry, 593, 113599.

Valsalan, J., Sadan, T., Venkatachalapathy, T., Anilkumar, K., & Aravindakshan, T. V. (2020). Identification of novel single-nucleotide polymorphism at exon1 and 2 region of B4GALT1 gene and its association with milk production traits in crossbred cattle of Kerala, India. Animal Biotechnology, 1-9.

Montasser, M. E., Van Hout, C. V., McFarland, R., Rosenberg, A., Callaway, M., Shen, B., ... & Shuldiner, A. R. (2019). Genetic and functional evidence relates a missense variant in B4GALT1 to lower LDL-C and fibrinogen. bioRxiv, 721704.

Nilius, V., Killer, M. C., Timmesfeld, N., Schmitt, M., Moll, R., Lorch, A., ... & Brendel, C. (2018). High β-1, 4-Galactosyltransferase-I expression in peripheral T-lymphocytes is associated with a low risk of relapse in germ-cell cancer patients receiving high-dose chemotherapy with autologous stem cell reinfusion. Oncoimmunology, 7(5), e1423169.

Chen, P. D., Chang, A. A., Wu, Y. M., & Huang, M. C. (2018). Silencing of B4GALT1 inversely regulates malignant phenotypes of hepatocellular carcinoma cells.

Cipriano, V. T. F., Miranda-Furtado, C. L., Mioranza, A. A., de Paz, C. C. P., Vila, R. A., Ramos, E. S., & Lôbo, R. B. (2018). B4GALT1, LHR, FSHR and IGF2 polymorphisms and scrotal circumference in Nellore bulls. Revista Brasileira de Reprodução Animal, 42(2), 70-75.

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For research use only. Not intended for any clinical use.

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