Analytical Data
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Gene name
HSPA14
- Application
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Alternative Names
HSPA14；HSP60；HSP70L1；Heat shock 70 kDa Protein 14
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q0VDF9
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Expression Region
1-509aa
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AA Sequence
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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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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
Related Products
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.
