Analytical Data
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基因名
B3GNT2
- Application
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别名
B3GNT2；B3GALT7；B3GNT1；N-acetyllactosaminide beta-1.3-N-acetylglucosaminyltransferase 2
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9NY97
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表达区间
29-397aa
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氨基酸序列
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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分子量
71 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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.
