Analytical Data
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基因名
B3GALNT2
- Application
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别名
3 N acetylgalactosaminyltransferase II MGC39558; Beta 3 GalNAc T2; Beta-1
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种属
Human
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表达系统
E. coli
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标签
GST-tag at N-terminal
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q8NCR0
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表达区间
1-500aa
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氨基酸序列
MRNWLVLLCPCVLGAALHLWLRLRSPPPACASGAGPADQLALFPQWKSTHYDVVVGVLSARNNHELRNVIRSTWMRHLLQHPTLSQRVLVKFIIGAHGCEVPVEDREDPYSCKLLNITNPVLNQEIEAFSLSEDTSSGLPEDRVVSVSFRVLYPIVITSLGVFYDANDVGFQRNITVKLYQAEQEEALFIARFSPPSCGVQVNKLWYKPVEQFILPESFEGTIVWESQDLHGLVSRNLHKVTVNDGGGVLRVITAGEGALPHEFLEGVEGVAGGFIYTIQEGDALLHNLHSRPQRLIDHIRNLHEEDALLKEESSIYDDIVFVDVVDTYRNVPAKLLNFYRWTVETTSFNLLLKTDDDCYIDLEAVFNRIVQKNLDGPNFWWGNFRLNWAVDRTGKWQELEYPSPAYPAFACGSGYVISKDIVKWLASNSGRLKTYQGEDVSMGIWMAAIGPKRYQDSLWLCEKTCETGMLSSPQYSPWELTELWKLKERCGDPCRCQAR
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分子量
83.1 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
B3GALNT2, also known as Beta-1,3-N-acetylgalactosaminyltransferase 2, is an essential enzyme involved in the biosynthesis of glycosphingolipids and glycoproteins. It specifically catalyzes the transfer of N-acetylgalactosamine (GalNAc) to terminal galactose residues, playing a crucial role in the formation of various glycan structures that are critical for cellular interactions and signaling. Research on B3GALNT2 has gained momentum due to its association with several pathological conditions, including cancer progression and neurodegenerative diseases. Alterations in B3GALNT2 activity can lead to abnormal glycosylation patterns, which have been implicated in tumor metastasis and immune response modulation. Moreover, the enzyme’s involvement in the synthesis of complex carbohydrates makes it a potential target for therapeutic interventions. Understanding the structure-function relationship of B3GALNT2 through recombinant protein studies can illuminate its biochemical pathways and offer insights into its role in disease mechanisms. Recent advances in recombinant DNA technology have enabled the generation of B3GALNT2 proteins for functional assays, providing a platform for drug discovery and the development of glycan-based therapies. The ongoing research aims to elucidate the regulatory mechanisms governing B3GALNT2 expression and the functional consequences of its modification, contributing to the broader understanding of glycosylation's impact on health and disease.
