Analytical Data
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Gene name
B3GNT7
- Application
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Alternative Names
B3GNT7；UDP-GlcNAc:betaGal beta-1.3-N-acetylglucosaminyltransferase 7
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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
Q8NFL0
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Expression Region
27-401aa
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AA Sequence
RSLTPGQFLQEPPPPTLEPQKAQKPNGQLVNPNNFWKNPKDVAAPTPMASQGPQAWDVTTTNCSANINLTHQPWFQVLEPQFRQFLFYRHCRYFPMLLNHPEKCRGDVYLLVVVKSVITQHDRREAIRQTWGRERQSAGGGRGAVRTLFLLGTASKQEERTHYQQLLAYEDRLYGDILQWGFLDTFFNLTLKEIHFLKWLDIYCPHVPFIFKGDDDVFVNPTNLLEFLADRQPQENLFVGDVLQHARPIRRKDNKYYIPGALYGKASYPPYAGGGGFLMAGSLARRLHHACDTLELYPIDDVFLGMCLEVLGVQPTAHEGFKTFGISRNRNSRMNKEPCFFRAMLVVHKLLPPELLAMWGLVHSNLTCSRKLQVL
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Molecular Weight
50.5 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
B3GNT7, or Beta-1,3-N-acetylglucosaminyltransferase 7, is a crucial enzyme involved in glycosylation processes, specifically in the synthesis of glycosaminoglycans. It plays a vital role in cell signaling, cell adhesion, and various biological processes essential for normal physiology. Dysregulation of B3GNT7 has been linked to various diseases, including cancer, where altered glycosylation patterns can influence tumor progression and metastasis. The research on B3GNT7 recombinant proteins focuses on understanding its structure-function relationships, enzymatic activity, and its biological implications. By producing recombinant B3GNT7, researchers aim to elucidate its role in glycan biosynthesis and its impact on cellular interactions. This is particularly significant in developing therapeutic strategies that can manipulate glycosylation patterns for disease intervention. Understanding B3GNT7's functional mechanisms could pave the way for new diagnostic markers and targeted therapies, enhancing our ability to address diseases associated with glycan abnormalities. The ongoing research further investigates potential applications in biotechnology and medicine, exploring how recombinant B3GNT7 can be utilized in drug development and the engineering of glycan-based therapeutics.
