B4GALT1 Antibody
(Synonyms: GGTB2, B4GALT1, Beta4Gal-T1, b4Gal-T1, Lactose synthase A protein, N-acetyllactosamine synthase, Nal synthase)B4GALT1 Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to B4GALT1.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% sodium azide.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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|---|---|---|
| Dilution Ratio | 1:1000-2000 | 1:100-200 |
Product Details
B4GALT1 Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to B4GALT1.
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Host Rabbit
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Clonality Polyclonal
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 43 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 43 kDa
Synthetic peptide corresponding to the C-term region of human B4GALT1.
Endogenous
affinity purified.
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% sodium azide.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
B4GALT1 is a Galactosyltransferase acting in the Golgi stacks. Catalyzes the transfer of galactose (Gal) from UDP-alpha-D-galactose in beta(1->4) linkage to the non-reducing terminal N-acetylglucosamine (GlcNAc) moieties of glycolipids and complex-type N-linked glycans. Adds one Gal residue to both GlcNAc beta(1->2)-linked to the alpha(1->3) and alpha(1->6) mannose antennae of complex-type N-glycans, enabling the formation of mono- and di-galactosylated glycoforms. Galactosylates complex-type N-glycans attached on the fragment crystallizable (Fc) of immunoglobulin-gamma isotypes (IgGs), a prerequisite for antibody glycan sialylation and related anti-inflammatory effector functions. Can also transfer a Gal residue to free GlcNAc to form N-acetyllactosamine. With LALBA/alpha-lactalbumin forms the lactose synthase complex responsible for production of large amounts of lactose in the lactating mammary gland. Interaction with LALBA alters the sugar substrate specificity of the catalytic domain, enabling high affinity binding of glucose and its transformation to lactose[1][2][3][4][5][6].
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Subcellular Localization
Golgi apparatus, Golgi stack membrane
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Expression
Tissue_Specificity: Ubiquitously expressed, but at very low levels in fetal and adult brain. -
Isoforms & Post-Translational Modification
B4GALT1 has 2 isoforms, P15291-1: amino acid length is 398, molecular weight is 43920 Da (predicted); P15291-2: amino acid length is 385, molecular weight is 42538 Da (predicted).The soluble form derives from the membrane forms by proteolytic processing
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Subunit
Homodimer; and heterodimer with LALBA/alpha-lactalbumin to form lactose synthase.
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SwissProt ID
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Synonyms
GGTB2, B4GALT1, Beta4Gal-T1, b4Gal-T1, Lactose synthase A protein, N-acetyllactosamine synthase, Nal synthase
Documentation
[1]. Ramasamy V, et al. Oligosaccharide preferences of beta1,4-galactosyltransferase-I: crystal structures of Met340His mutant of human beta1,4-galactosyltransferase-I with a pentasaccharide and trisaccharides of the N-glycan moiety. J Mol Biol. 2005 Oct 14;353(1):53-67. [Content Brief]
[2]. Dekkers G, et al. Multi-level glyco-engineering techniques to generate IgG with defined Fc-glycans. Sci Rep. 2016 Nov 22;6:36964. [Content Brief]
[3]. Benedetti E, et al. Network inference from glycoproteomics data reveals new reactions in the IgG glycosylation pathway. Nat Commun. 2017 Nov 14;8(1):1483. [Content Brief]
[4]. Jaroentomeechai T, et al. A universal glycoenzyme biosynthesis pipeline that enables efficient cell-free remodeling of glycans. Nat Commun. 2022 Oct 24;13(1):6325. [Content Brief]
[5]. Ma W, et al. Divergent Enzymatic Assembly of a Comprehensive 64-Membered IgG N-Glycan Library for Functional Glycomics. Adv Sci (Weinh). 2023 Oct;10(30):e2303832. [Content Brief]
[6]. Makrydaki E, et al. Immobilized enzyme cascade for targeted glycosylation. Nat Chem Biol. 2024 Jun;20(6):732-741. [Content Brief]
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