Analytical Data
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Gene name
b3GALT5
- Application
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Alternative Names
b3GALT5；Beta-1.3-galactosyltransferase 5
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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
P59052
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Expression Region
1-145aa
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AA Sequence
MRRLRHREVR GPVLGHTATG GPQNGTSGCT TAPQQRPPPG TQGMLEQYLN RGGQKSHGLC WLLCFVSQGQ NQDVISAELW CRIHVQAHWG CWQNSAVWGC RNEVLVSLLA VGQGLPSASG GRLPSLVHGP SHPDSQHPRE VPLAL
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Molecular Weight
15.7 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
B3GALT5 is a member of the beta-1,3-galactosyltransferase family, which plays a critical role in glycan biosynthesis, specifically in the formation of the carbohydrate moiety on glycoproteins and glycolipids. This enzyme catalyzes the transfer of galactose from UDP-galactose to nascent polypeptide chains, facilitating the synthesis of glycosaminoglycans and glycoproteins essential for various biological processes, including cell adhesion, signaling, and immune responses. Abnormal expression or mutations in the B3GALT5 gene have been implicated in various pathologies, including development disorders and cancers, which has intensified research into its functional mechanisms and therapeutic potential. Recent studies have focused on the recombinant expression of B3GALT5 to investigate its enzymatic activity and substrate specificity, aiming to elucidate its role in cellular processes and disease states. Understanding the structure-function relationship of B3GALT5 through recombinant protein studies could pave the way for novel therapeutic strategies targeting glycosylation pathways in disease.
