Human beta-1,4‑Galactosyltransferase 1/B4GalT1 Antibody
Human beta-1,4‑Galactosyltransferase 1/B4GalT1 Antibody Summary
Gly44-Ser398
Accession # P15291
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: beta-1,4-Galactosyltransferase 1/B4GalT1
beta 4GalT1 is one of seven beta 1,4 galactosyltransferases that transfer galactose in a beta 1,4 linkage to acceptor sugars including GlcNAc, and Glc, and Xyl. By sequence similarity, the beta 4GalTs form four groups: beta 4GalT1 and beta 4GalT2, beta 4GalT3 and beta 4GalT4, beta 4GalT5 and beta 4GalT6, and beta 4GalT7 (1). beta 4GalT1 is unique among the seven enzymes because it can be expressed either as membrane associated form or secreted form (2). The secreted form is restricted to lactating mammary tissues where the enzyme forms a heterodimer with alpha -lactalbumin to catalyze the synthesis of lactose (3). The membrane form can reside either in the Golgi apparatus, where it adds galactose to N-acetylglucosamine residues, or on cell surface, where it functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix (4). The two enzymatic forms result from alternate transcription initiation sites and post-translational processing (5). Defects in beta 4GalT1 are the cause of congenital disorder of glycosylation type 2D (CDG2D) (6).
- Amado, M. et al. (1999) Biochim. Biophys. Acta. 1473:35.
- Yamaguchi, N and Fukuda, M.N. (1995) J. Biol. Chem. 270:12170.
- Appert, H.E. et al. (1986) Biochem. Biophys. Res. Commun. 138:224.
- Lopez, L.C. et al. (1991) J. Biol. Chem. 266:15984.
- Mengle-Gaw, L. et al. (1991) Biochem. Biophys. Res. Commun. 176:1269.
- Hansske, B. et al. (2002) J. Clin. Invest. 109:725.
Product Datasheets
Citations for Human beta-1,4‑Galactosyltransferase 1/B4GalT1 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Shedding of N-acetylglucosaminyltransferase-V is regulated by maturity of cellular N-glycan
Authors: Tetsuya Hirata, Misaki Takata, Yuko Tokoro, Miyako Nakano, Yasuhiko Kizuka
Communications Biology
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N-terminome analyses underscore the prevalence of SPPL3-mediated intramembrane proteolysis among Golgi-resident enzymes and its role in Golgi enzyme secretion
Authors: Laura Hobohm, Tomas Koudelka, Fenja H. Bahr, Jule Truberg, Sebastian Kapell, Sarah-Sophie Schacht et al.
Cellular and Molecular Life Sciences
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Modeling Glycan Processing Reveals Golgi-Enzyme Homeostasis upon Trafficking Defects and Cellular Differentiation
Authors: P Fisher, H Spencer, J Thomas-Oat, AJ Wood, D Ungar
Cell Rep, 2019-04-23;27(4):1231-1243.e6.
Species: Human
Sample Types: Cell Lysates
Applications: Western Blot -
Membrane detachment is not essential for COG complex function
Authors: LK Climer, ID Pokrovskay, JB Blackburn, VV Lupashin
Mol. Biol. Cell, 2018-03-30;0(0):.
Species: Human
Sample Types: Cell Lysates
Applications: Western Blot -
Shedding of glycan-modifying enzymes by signal peptide peptidase-like 3 (SPPL3) regulates cellular N-glycosylation.
Authors: Voss M, Kunzel U, Higel F, Kuhn P, Colombo A, Fukumori A, Haug-Kroper M, Klier B, Grammer G, Seidl A, Schroder B, Obst R, Steiner H, Lichtenthaler S, Haass C, Fluhrer R
EMBO J, 2014-10-29;33(24):2890-905.
Species: Human, Mouse
Sample Types: Cell Lysates
Applications: Western Blot
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