Analytical Data
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Gene name
B4GALT1
- Application
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Alternative Names
B4GALT1；GGTB2；Beta-1.4-galactosyltransferase 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P15291-1
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Expression Region
44-398aa
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AA Sequence
GRDLSRLPQL VGVSTPLQGG SNSAAAIGQS SGELRTGGAR PPPPLGASSQ PRPGGDSSPV VDSGPGPASN LTSVPVPHTT ALSLPACPEE SPLLVGPMLI EFNMPVDLEL VAKQNPNVKM GGRYAPRDCV SPHKVAIIIP FRNRQEHLKY WLYYLHPVLQ RQQLDYGIYV INQAGDTIFN RAKLLNVGFQ EALKDYDYTC FVFSDVDLIP MNDHNAYRCF SQPRHISVAM DKFGFSLPYV QYFGGVSALS KQQFLTINGF PNNYWGWGGE DDDIFNRLVF RGMSISRPNA VVGRCRMIRH SRDKKNEPNP QRFDRIAHTK ETMLSDGLNS LTYQVLDVQR YPLYTQITVD IGTPS
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Molecular Weight
42 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
B4GALT1, also known as β-1,4-galactosyltransferase 1, plays a critical role in glycosylation processes, particularly in the biosynthesis of complex carbohydrates and glycoconjugates. This enzyme is involved in the transfer of galactose from UDP-galactose to various substrates, contributing to glycan structures that are essential for proper cellular functions, including cell adhesion, signaling, and immune response. Dysregulation of B4GALT1 has been implicated in several pathological conditions, including cancer progression, where altered glycosylation patterns can influence tumor growth and metastasis. The production of recombinant B4GALT1 has become a focal point in biochemical research, allowing scientists to study its enzymatic activity, substrate specificity, and interaction with various glycoproteins. By using techniques such as molecular cloning and expression in suitable host systems, researchers aim to produce active forms of the protein for structural and functional analyses. Understanding B4GALT1's role in glycosylation pathways could provide insights into therapeutic targets and strategies for diseases linked to glycan abnormalities. Through these investigations, the potential implications of B4GALT1 in both basic research and clinical applications are becoming increasingly apparent, highlighting the importance of this enzyme in the field of glycobiology.
