关键信息
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基因名
GALNACT-2
- 应用
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别名
4-N-acetylgalactosaminyltransferase 2; Beta4GalNAcT-2; CGAT2_HUMAN; CHGN2; Chondroitin beta-1; Chondroitin sulfate N-acetylgalactosaminyltransferase 2; Csgalnact2; DKFZp686H13226; FLJ43310; GALNACT 2; GalNAcT-2; GALNACT2; MGC40204; PRO0082
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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
Q8N6G5
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表达区间
1-542aa
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氨基酸序列
MPRRGLILHTRTHWLLLGLALLCSLVLFMYLLECAPQTDGNASLPGVVGENYGKEYYQALLQEQEEHYQTRATSLKRQIAQLKQELQEMSEKMRSLQERRNVGANGIGYQSNKEQAPSDLLEFLHSQIDKAEVSIGAKLPSEYGVIPFESFTLMKVFQLEMGLTRHPEEKPVRKDKRDELVEVIEAGLEVINNPDEDDEQEDEEGPLGEKLIFNENDFVEGYYRTERDKGTQYELFFKKADLTEYRHVTLFRPFGPLMKVKSEMIDITRSIINIIVPLAERTEAFVQFMQNFRDVCIHQDKKIHLTVVYFGKEGLSKVKSILESVTSESNFHNYTLVSLNEEFNRGRGLNVGARAWDKGEVLMFFCDVDIYFSAEFLNSCRLNAEPGKKVFYPVVFSLYNPAIVYANQEVPPPVEQQLVHKKDSGFWRDFGFGMTCQYRSDFLTIGGFDMEVKGWGGEDVHLYRKYLHGDLIVIRTPVPGLFHLWHEKRCADELTPEQYRMCIQSKAMNEAPHSHLGMLVFREEIETHLHKQAYRTNSEAVG
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分子量
85.36 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.
质检流程
相关产品
背景信息
GALNACT-2, a member of the galactosamine N-acetyltransferase family, plays a crucial role in carbohydrate metabolism and cellular interactions by mediating the transfer of acetamido groups to specific substrates. Its involvement in glycosylation processes makes it significant in various biological functions, including cell signaling, immune response, and development. Recent studies have suggested that GALNACT-2 may also be implicated in the pathogenesis of certain diseases, including cancer and neurological disorders, where altered glycosylation patterns can influence tumor progression and the neuronal environment. Research focusing on GALNACT-2 aims to unravel its precise biological functions, regulatory mechanisms, and potential as a therapeutic target. Innovations in recombinant protein technologies have enabled the production and functional characterization of GALNACT-2, allowing scientists to explore its enzymatic properties and interactions with other biomolecules. Understanding GALNACT-2's structure-function relationship will be vital for developing targeted therapies and diagnostic tools. As research progresses, GALNACT-2 is emerging as a promising focus for studies in carbohydrate biochemistry and its associated medical applications.
