Analytical Data
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Gene name
HSPA13
- Application
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Alternative Names
HSPA13;STCH;Heat shock 70 kDa Protein 13
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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
P48723
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Expression Region
23-471aa
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AA Sequence
QQYLPLPTPKVIGIDLGTTYCSVGVFFPGTGKVKVIPDENGHISIPSMVSFTDNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAEELEAEIGRYPFKVLNKNGMVEFSVTSNETITVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAANLAGLKILRVINEPTAAAMAYGLHKADVFHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLYKQIYQTYGFVPSRKEEIHRLRQAVEMVKLNLTLHQSAQLSVLLTVEEQDRKEPHSSDTELPKDKLSSADDHRVNSGFGRGLSDKKSGESQVLFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNTSVDPDLAVVTGVAIQAGIDGGSWPLQVSALEIPNKHLQKTNFN
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Molecular Weight
76.6kDa
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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
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Protein Description
HSPA13, a member of the heat shock protein 70 (HSP70) family, plays a crucial role in cellular stress response and protein homeostasis. Its involvement in various cellular processes such as protein folding, repair, and degradation highlights its significance in maintaining cellular function. Research has shown that HSPA13 may be implicated in several diseases, including neurodegenerative disorders and certain cancers, where its expression and activity can be altered. Understanding the mechanisms through which HSPA13 functions can provide insight into its potential as a therapeutic target. The study of recombinant HSPA13 protein is essential for elucidating its structural and functional properties, as well as its interactions with client proteins. By producing HSPA13 in a recombinant form, researchers can investigate its role in normal physiology and disease states, which may lead to the development of novel strategies for disease intervention. Additionally, exploring the regulation of HSPA13 expression and its chaperone activity may contribute to a deeper understanding of protein misfolding diseases, paving the way for innovative treatments that harness the capabilities of molecular chaperones. Overall, research on HSPA13 recombinant protein not only enhances our understanding of cellular stress responses but also opens avenues for therapeutic exploration in conditions where protein homeostasis is disrupted.
