β-1,4-Gal-T1 Antibody [C2J8] | Primary Antibodies

Application: Reactivity: Human

Usage Information

Dilution
WB1:100-1:1000 IP1:100-1:200 IF1:50-1:500

Application
WB, IP, IHC, IF, ELISA

Reactivity
Human

Source
Mouse Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
44 kDa

Datasheet & SDS

Biological Description

Specificity
β-1,4-Gal-T1 Antibody [C2J8] detects endogenous levels of total β-1,4-Gal-T1 protein.

Clone
C2J8

Synonym(s)
Beta-1,4-galactosyltransferase 1, Beta-1,4-GalTase 1; Beta4Gal-T1; b4Gal-T1, B4GALT1, GGTB2

Background
β-1,4-Galactosyltransferase 1 (β-1,4-Gal-T1/B4GALT1) is a type II Golgi-resident glycosyltransferase of the β4GalT family that uses UDP-galactose to add β1,4-linked galactose onto terminal N-acetylglucosamine, glucose, or xylose residues, providing a key late elongation step in N-glycan processing and broader glycoconjugate biosynthesis, while uniquely also participating in lactose production in lactating mammary epithelium. The enzyme is synthesized as a type II membrane glycoprotein with an N‑terminal cytosolic tail, a single transmembrane anchor that serves as an uncleaved signal for Golgi targeting, a short luminal stem, and a C‑terminal catalytic domain that binds UDP‑galactose and positions acceptor sugars in a metal‑dependent active site to form Galβ1‑4GlcNAc (N‑acetyllactosamine) and related disaccharide units. B4GALT1 recognizes terminal GlcNAc in complex and hybrid N‑glycans and extends these termini with β1,4‑galactose, generating N‑acetyllactosamine repeats that are further modified by sialyltransferases nd fucosyltransferases into diverse antigenic and adhesion‑related epitopes, thereby controlling the composition of glycoprotein and glycolipid surfaces that mediate cell–cell and cell–matrix interactions. In the Golgi, the transmembrane domain and homodimerization of B4GALT1 contribute to its retention in trans‑Golgi cisternae, where it works in an ordered sequence with other glycosyltransferases, and its localization and activity are sensitive to perturbations in intra‑Golgi trafficking complexes, such as COG, which when disrupted cause mislocalization and hypogalactosylation of N‑glycans. The same gene also generates a shorter transcript that is cleaved to a soluble form that pairs with α‑lactalbumin in the mammary gland to form lactose synthase; binding of α‑lactalbumin remodels the sugar‑binding pocket, shifts the acceptor preference from GlcNAc to glucose, and converts the broad glycosyltransferase into a lactose synthase that transfers galactose from UDP‑Gal to glucose as the final step in lactose biosynthesis during lactation. Genetic defects in B4GALT1 underlie congenital disorder of glycosylation type 2D, characterized by undergalactosylated N‑glycans, multi‑system involvement, and coagulopathy, and glomerular upregulation and altered activity of B4GALT1 have been associated with IgA nephropathy, highlighting the importance of its galactosylation function in both systemic glycoprotein maturation and organ‑specific pathology.

Background

β-1,4-Galactosyltransferase 1 (β-1,4-Gal-T1/B4GALT1) is a type II Golgi-resident glycosyltransferase of the β4GalT family that uses UDP-galactose to add β1,4-linked galactose onto terminal N-acetylglucosamine, glucose, or xylose residues, providing a key late elongation step in N-glycan processing and broader glycoconjugate biosynthesis, while uniquely also participating in lactose production in lactating mammary epithelium. The enzyme is synthesized as a type II membrane glycoprotein with an N‑terminal cytosolic tail, a single transmembrane anchor that serves as an uncleaved signal for Golgi targeting, a short luminal stem, and a C‑terminal catalytic domain that binds UDP‑galactose and positions acceptor sugars in a metal‑dependent active site to form Galβ1‑4GlcNAc (N‑acetyllactosamine) and related disaccharide units. B4GALT1 recognizes terminal GlcNAc in complex and hybrid N‑glycans and extends these termini with β1,4‑galactose, generating N‑acetyllactosamine repeats that are further modified by sialyltransferases nd fucosyltransferases into diverse antigenic and adhesion‑related epitopes, thereby controlling the composition of glycoprotein and glycolipid surfaces that mediate cell–cell and cell–matrix interactions. In the Golgi, the transmembrane domain and homodimerization of B4GALT1 contribute to its retention in trans‑Golgi cisternae, where it works in an ordered sequence with other glycosyltransferases, and its localization and activity are sensitive to perturbations in intra‑Golgi trafficking complexes, such as COG, which when disrupted cause mislocalization and hypogalactosylation of N‑glycans. The same gene also generates a shorter transcript that is cleaved to a soluble form that pairs with α‑lactalbumin in the mammary gland to form lactose synthase; binding of α‑lactalbumin remodels the sugar‑binding pocket, shifts the acceptor preference from GlcNAc to glucose, and converts the broad glycosyltransferase into a lactose synthase that transfers galactose from UDP‑Gal to glucose as the final step in lactose biosynthesis during lactation. Genetic defects in B4GALT1 underlie congenital disorder of glycosylation type 2D, characterized by undergalactosylated N‑glycans, multi‑system involvement, and coagulopathy, and glomerular upregulation and altered activity of B4GALT1 have been associated with IgA nephropathy, highlighting the importance of its galactosylation function in both systemic glycoprotein maturation and organ‑specific pathology.

References
https://pubmed.ncbi.nlm.nih.gov/18393823/ https://pubmed.ncbi.nlm.nih.gov/15465321/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%