Analytical Data
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基因名
HSPA14
- Application
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别名
HSPA14；HSP60；HSP70L1；Heat shock 70 kDa Protein 14
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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
Q0VDF9
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表达区间
1-509aa
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氨基酸序列
MAAIGVHLGC TSACVAVYKD GRAGVVANDA GDRVTPAVVA YSENEEIVGL AAKQSRIRNI SNTVMKVKQI LGRSSSDPQA QKYIAESKCL VIEKNGKLRY EIDTGEETKF VNPEDVARLI FSKMKETAHS VLGSDANDVV ITVPFDFGEK QKNALGEAAR AAGFNVLRLI HEPSAALLAY GIGQDSPTGK SNILVFKLGG TSLSLSVMEV NSGIYRVLST NTDDNIGGAH FTETLAQYLA SEFQRSFKHD VRGNARAMMK LTNSAEVAKH SLSTLGSANC FLDSLYEGQD FDCNVSRARF ELLCSPLFNK CIEAIRGLLD QNGFTADDIN KVVLCGGSSR IPKLQQLIKD LFPAVELLNS IPPDEVIPIG AAIEAGILIG KENLLVEDSL MIECSARDIL VKGVDESGAS RFTVLFPSGT PLPARRQHTL QAPGSISSVC LELYESDGKN SAKEETKFAQ VVLQDLDKKE NGLRDILAVL TMKRDGSLHV TCTDQETGKC EAISIEIAS
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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
HSPA14, a member of the heat shock protein 70 (HSP70) family, plays a crucial role in protein folding, trafficking, and degradation, thereby ensuring cellular homeostasis under stress conditions. This protein is particularly implicated in the regulation of various cellular processes, including apoptosis and stress response mechanisms. Its expression is often upregulated in response to thermal, oxidative, and other stressors, highlighting its potential protective role in cells. Research into HSPA14 has gained momentum due to its involvement in several diseases, including cancer, neurodegenerative disorders, and metabolic syndromes, where its dysregulation may contribute to pathophysiological conditions. Understanding the molecular mechanisms of HSPA14, including its interactions with client proteins and chaperone activity, is critical for elucidating its functional roles in health and disease. Recent studies have focused on the recombinant expression and characterization of HSPA14, aiming to provide insights into its biochemical properties and therapeutic potential. This research is essential for developing targeted strategies that could modulate HSPA14 activity, potentially offering novel approaches for treating diseases associated with cellular stress and misfolded proteins.
