Analytical Data
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Gene name
b3GALT2
- Application
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Alternative Names
b3GALT2；Beta-1.3-galactosyltransferase 2
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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
O43825
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Expression Region
1-422aa
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AA Sequence
MLQWRRRHCCFAKMTWNAKRSLFRTHLIGVLSLVFLFAMFLFFNHHDWLPGRAGFKENPVTYTFRGFRSTKSETNHSSLRNIWKETVPQTLRPQTATNSNNTDLSPQGVTGLENTLSANGSIYNEKGTGHPNSYHFKYIINEPEKCQEKSPFLILLIAAEPGQIEARRAIRQTWGNESLAPGIQITRIFLLGLSIKLNGYLQRAILEESRQYHDIIQQEYLDTYYNLTIKTLMGMNWVATYCPHIPYVMKTDSDMFVNTEYLINKLLKPDLPPRHNYFTGYLMRGYAPNRNKDSKWYMPPDLYPSERYPVFCSGTGYVFSGDLAEKIFKVSLGIRRLHLEDVYVGICLAKLRIDPVPPPNEFVFNHWRVSYSSCKYSHLITSHQFQPSELIKYWNHLQQNKHNACANAAKEKAGRYRHRKLH
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Molecular Weight
49.2 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
B3GALT2, or Beta-1,3-galactosyltransferase 2, is an enzyme that plays a crucial role in glycosylation, specifically in the synthesis of carbohydrate structures known as glycosaminoglycans. This enzyme is involved in the transfer of galactose to other sugars, thereby contributing to the formation of vital glycan structures that are essential for various biological processes, including cell signaling, adhesion, and inflammation. Deficiencies or mutations in the B3GALT2 gene have been linked to several congenital disorders, including spondylodysplastic dysplasia, which underscores the importance of studying this protein. Understanding B3GALT2's structure, function, and activity can provide insights into its role in disease mechanisms and may open avenues for therapeutic interventions. Recent advances in recombinant protein technologies have enabled researchers to produce and purify B3GALT2 for detailed functional assays, structural analyses, and potential drug development. By exploring the enzyme’s substrate specificity and catalytic mechanisms, researchers aim to elucidate its biological significance and to investigate its potential as a target for disease treatment, resulting in a growing interest in B3GALT2 within the fields of biochemistry and molecular biology.
