Analytical Data
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Gene name
HSPA12B
- Application
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Alternative Names
C20orf60
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Species
Human
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Source
E. coli
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Tag
N-terminalHisTag
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96MM6
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Expression Region
1~217aa
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AA Sequence
MLAVPEMGLQGLYIGSSPERSPVPSPPGSPRTQESCGIAPLTPSQSPKPEVRAP QQASFSVVVAIDFGTTSSGYAFSFASDPEAIHMMRKWEGGDPGVAHQKTPTCLL LTPEGAFHSFGYTARDYYHDLDPEEARDWLYFEKFKMKIHSATDLTLKTQLEAV NGKTMPALEVFAHALRFFREHALQELREQSPSLPEKDTVRWVLTVPAIWKQPAK Q
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Molecular Weight
27.8kDa
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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
Identification
Protein Description
HSPA12B, a member of the heat shock protein 70 (HSP70) family, plays a vital role in cellular stress responses, protein folding, and degradation pathways. Research into HSPA12B has recently garnered attention due to its involvement in various physiological and pathological processes, including tumorigenesis, neurodegenerative diseases, and stress resistance. Unlike its well-studied counterparts, such as HSPA1A and HSPA4, the specific functions and mechanisms of HSPA12B remain poorly understood, highlighting the need for in-depth analysis of this protein. Initial studies suggest that HSPA12B may facilitate cellular protection by mediating the refolding of misfolded proteins and promoting apoptosis in stressed cells. Furthermore, its expression patterns in different tissues and under various stress conditions provide insight into its potential roles in health and disease. Understanding HSPA12B's function could pave the way for innovative therapeutic strategies targeting its pathways, particularly in conditions characterized by protein misfolding or cellular stress. Consequently, the investigation of HSPA12B recombinant protein provides a valuable tool for elucidating its mechanistic roles and potential applications in biomedical research.
