Analytical Data
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基因名
CHST5
- Application
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别名
CHST5Carbohydrate sulfotransferase 5; EC 2.8.2.-; Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 4-alpha; GST4-alpha; Intestinal N-acetylglucosamine-6-O-sulfotransferase; I-GlcNAc6ST
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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
Q9GZS9
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表达区间
1-411aa
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氨基酸序列
MGMRARVPKVAHSTRRPPAARMWLPRFSSKTVTVLLLAQTTCLLLFIISRPGPSSPAGGEDRVHVLVLSSWRSGSSFLGQLFSQHPDVFYLMEPAWHVWTTLSQGSAATLHMAVRDLMRSIFLCDMDVFDAYMPQSRNLSAFFNWATSRALCSPPACSAFPRGTISKQDVCKTLCTRQPFSLAREACRSYSHVVLKEVRFFNLQVLYPLLSDPALNLRIVHLVRDPRAVLRSREAAGPILARDNGIVLGTNGKWVEADPHLRLIREVCRSHVRIAEAATLKPPPFLRGRYRLVRFEDLAREPLAEIRALYAFTGLTLTPQLEAWIHNITHGSGIGKPIEAFHTSSRNARNVSQAWRHALPFTKILRVQEVCAGALQLLGYRPVYSADQQRDLTLDLVLPRGPDHFSWASPD
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分子量
46.1 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
CHST5, or carbohydrate (chondroitin 4) sulfotransferase 5, is an important enzyme that plays a significant role in the biosynthesis of sulfated glycosaminoglycans, specifically chondroitin sulfate. This molecule has been implicated in various biological processes, including cell signaling, tissue development, and repair. Dysregulation of CHST5 has been associated with several pathological conditions, including cancer, where altered glycosaminoglycan sulfation patterns can influence tumor progression and metastasis. Given its critical role in modifying extracellular matrices and cellular interactions, CHST5 has garnered interest as a potential therapeutic target. The study and production of recombinant CHST5 protein provide valuable insights into its enzymatic mechanisms and functions. Utilizing recombinant DNA technology, researchers can produce purified CHST5 to investigate its biochemical properties, substrate specificity, and interactions with other cellular components. Understanding CHST5's functional characteristics not only contributes to the broader field of glycoscience but also paves the way for novel therapeutic approaches targeting sulfation pathways in various diseases, including cancer and other disorders characterized by altered glycosaminoglycan metabolism. The analysis of CHST5 recombinant protein also facilitates the exploration of its role in cell biology, potentially identifying new avenues for intervention in diseases where glycosaminoglycan sulfation is disrupted. Thus, the research surrounding CHST5 is crucial for advancing our understanding of glycosaminoglycan biosynthesis and its implications for health and disease.
