Analytical Data
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基因名
VWA3B
- Application
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别名
VWA3B; von Willebrand factor A domain-containing Protein 3B; VWA domain-containing Protein 3B
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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
Q502W6
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表达区间
1-624 aa
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氨基酸序列
MEKSGPSSTISEQQLQRQEGWINTKTDLAEQSLISSEKWLQLHGLKSNKLTLKQILSQIGFPHCEDYVASLGRPVASRYADGLFPQLYRAEDGRVYNLTAKSELIYQFVEHLTQAVESYKQRMDWLTSKSRQIFGVILEQCVTIVLDFGGILEGELDLCREALTMVLQEQVAHITEFNIIRVSQEPVKWQENATPVTEQSIATAISWVEKLTVELTVSEAGRLDALLEAGRDKTIESIYYFVVGDVPEESKELLLQRALEIPCPVYTVSFNARGEGTIAFLKDLSAKTHSRFHAFAERTECVEFPAFSTKDGDNVMTWNSRKLKGKLPPGAGVREDVFLVWQEMEEACSTLAQIQRLVAEPPKPDVATVDCESETTSVEIASNPEDTWDSKTWLQKYGLKAQKLSLYDVLADCSFRHADGVVDIKAKPENESVQTSAETNKKTVHAKYCSRFVHAPWKDGSLVHVNITKEKCKWYSERIHTALARIRRRIKWLQDGSQSLFGRLHNDCIYILIDTSHSMKSKLDLVKDKIIQFIQEQLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAQSWIRDIKIGSSTNTLSALKTAFADKETQAIYLLTDGRPDQGTSSHLLLTAAV
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分子量
97 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
The research on the recombinant VWA3B protein has gained significant attention due to its potential role in various biological processes and disease mechanisms. VWA3B, a member of the von Willebrand factor A (VWA) domain-containing protein family, is implicated in cell adhesion, extracellular matrix interactions, and modulation of signaling pathways. Studies have indicated that VWA3B may be involved in cancer progression, immune response, and neurodegenerative diseases, highlighting its significance in health and disease. Advances in biotechnology have enabled the production of recombinant VWA3B, which allows for detailed structural and functional analyses. By generating this protein in vitro, researchers aim to elucidate its biological functions, interactions with other molecules, and potential as a therapeutic target. Understanding the mechanisms by which VWA3B influences cellular behavior could pave the way for novel treatment strategies for conditions influenced by its activity. Thus, the exploration of recombinant VWA3B not only contributes to fundamental biological knowledge but also has implications for developing targeted therapies and diagnostics in various medical fields.
