Analytical Data
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Gene name
HSPA9
- Application
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Alternative Names
Heat shock 70kDa protein 9, Mortalin, GRP75, mot-2, HSPA9B, PBP74, CSA
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Species
Human
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Source
E. coli
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Tag
N-6His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P38646
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Expression Region
1-679aa
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Molecular Weight
75 kDa
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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
HSPA9, also known as Heat Shock Protein Family A Member 9 or Mortalin, is a member of the HSP70 family of proteins that play a crucial role in cellular stress response and protein homeostasis. Research indicates that HSPA9 is involved in various cellular processes, including mitochondrial function, apoptosis, and cellular signaling pathways. Its expression is often upregulated in response to stress conditions, making it a key player in protecting cells from damage. Given its involvement in oncogenic processes and its association with several diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases, HSPA9 has gained attention as a potential biomarker and therapeutic target. Studies have demonstrated that HSPA9 can influence tumor progression and resistance to therapies, highlighting the necessity for detailed investigations into its functional mechanisms. The development of recombinant HSPA9 proteins allows for in-depth studies on its structural and functional properties, facilitating the understanding of its role in various biological contexts. The exploration of HSPA9 as a therapeutic target is particularly promising due to its dual roles in promoting cell survival in stressed environments and its potential involvement in disease pathology. This research has significant implications for the development of novel therapeutic strategies aimed at modulating HSPA9 activity in disease contexts, ultimately influencing treatment approaches in oncology and other related fields. Understanding the molecular mechanisms regulated by HSPA9 can provide insights into stress-response pathways, potentially leading to advancements in targeted therapies and improved patient outcomes in conditions where cellular stress plays a critical role.
