Analytical Data
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基因名
htpG
- Application
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别名
htpG；Chaperone Protein HtpG
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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
P0A6Z3
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表达区间
1-624aa
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氨基酸序列
MKGQETRGFQSEVKQLLHLMIHSLYSNKEIFLRELISNASDAADKLRFRALSNPDLYEGDGELRVRVSFDKDKRTLTISDNGVGMTRDEVIDHLGTIAKSGTKSFLESLGSDQAKDSQLIGQFGVGFYSAFIVADKVTVRTRAAGEKPENGVFWESAGEGEYTVADITKEDRGTEITLHLREGEDEFLDDWRVRSIISKYSDHIALPVEIEKREEKDGETVISWEKINKAQALWTRNKSEITDEEYKEFYKHIAHDFNDPLTWSHNRVEGKQEYTSLLYIPSQAPWDMWNRDHKHGLKLYVQRVFIMDDAEQFMPNYLRFVRGLIDSSDLPLNVSREILQDSTVTRNLRNALTKRVLQMLEKLAKDDAEKYQTFWQQFGLVLKEGPAEDFANQEAIAKLLRFASTHTDSSAQTVSLEDYVSRMKEGQEKIYYITADSYAAAKSSPHLELLRKKGIEVLLLSDRIDEWMMNYLTEFDGKPFQSVSKVDESLEKLADEVDESAKEAEKALTPFIDRVKALLGERVKDVRLTHRLTDTPAIVSTDADEMSTQMAKLFAAAGQKVPEVKYIFELNPDHVLVKRAADTEDEAKFSEWVELLLDQALLAERGTLEDPNLFIRRMNQLLVS
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分子量
71.4 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
HtpG, or heat shock protein 70 (Hsp70) family member, is a highly conserved molecular chaperone found in various organisms, playing a critical role in protein folding, protection against stress, and maintaining cellular homeostasis. Its importance is underscored by its involvement in essential biological processes, such as protein assembly and degradation. In recent years, research on HtpG recombinant protein has gained momentum due to its potential implications in understanding stress responses and its role in various diseases, including cancer and neurodegenerative disorders. By generating recombinant HtpG proteins, researchers aim to delve deeper into the mechanisms of chaperone action, elucidate its interactions with client proteins, and explore its prospective therapeutic applications. Moreover, HtpG is also of interest in vaccine development and biotechnology, given its immunogenic properties and ability to stabilize other proteins. The study of HtpG not only enhances our understanding of cellular stress responses but also opens avenues for novel therapeutic strategies that exploit its chaperoning capabilities. As such, continued research into HtpG recombinant protein presents significant opportunities for advancements in both basic biology and translational science.
