Analytical Data
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Gene name
B3GNT2
- Application
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Alternative Names
B3GNT2；B3GALT7；B3GNT1；N-acetyllactosaminide beta-1.3-N-acetylglucosaminyltransferase 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
Q9NY97
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Expression Region
29-397aa
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AA Sequence
KSSSQEKNGK GEVIIPKEKF WKISTPPEAY WNREQEKLNR QYNPILSMLT NQTGEAGRLS NISHLNYCEP DLRVTSVVTG FNNLPDRFKD FLLYLRCRNY SLLIDQPDKC AKKPFLLLAI KSLTPHFARR QAIRESWGQE SNAGNQTVVR VFLLGQTPPE DNHPDLSDML KFESEKHQDI LMWNYRDTFF NLSLKEVLFL RWVSTSCPDT EFVFKGDDDV FVNTHHILNY LNSLSKTKAK DLFIGDVIHN AGPHRDKKLK YYIPEVVYSG LYPPYAGGGG FLYSGHLALR LYHITDQVHL YPIDDVYTGM CLQKLGLVPE KHKGFRTFDI EEKNKNNICS YVDLMLVHSR KPQEMIDIWS
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Molecular Weight
71 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
Related Products
Protein Description
B3GNT2, a member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, plays a crucial role in the biosynthesis of glycoproteins and glycosphingolipids through the addition of N-acetylgalactosamine (GalNAc) to serine or threonine residues on target proteins. The study of B3GNT2 has gained significant interest due to its involvement in various physiological and pathological processes, including cell signaling, differentiation, and immune responses. Dysregulation of glycosylation, particularly through enzymes like B3GNT2, has been implicated in diseases such as cancer, where altered glycan structures can influence tumor progression and metastasis. Understanding the functional mechanisms of B3GNT2 and its role in specific cellular pathways may offer insights into therapeutic targets for diseases characterized by aberrant glycosylation. Moreover, the development of recombinant B3GNT2 proteins facilitates structural and functional studies, aiding in the elucidation of the enzyme's substrate specificity and kinetic properties. As a result, this research is vital for advancing our knowledge of glycosylation processes and their implications in health and disease.
