Analytical Data
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Gene name
HSPA9
- Application
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Alternative Names
CSA; GRP75; HSPA9B; MOT; MOT2; MTHSP75; PBP74; Mot-2; Stress-70 Protein,Mitochondrial; Mortalin,Perinuclear; 75 kDa glucose-regulated protein; Peptide-binding protein 74
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Species
Human
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Source
E. coli
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Tag
N-His
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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
Ser65~Ala311
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Molecular Weight
31kDa
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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
HSPA9, also known as heat shock protein 70 homolog 9, is a member of the Hsp70 family of proteins that play pivotal roles in cellular protection, protein folding, and stress response mechanisms. Research into HSPA9 has garnered attention due to its involvement in various cellular processes, including apoptosis, mitosis, and the maintenance of mitochondrial function. Its expression is often upregulated in response to cellular stress, highlighting its potential as a biomarker for stress-related diseases. Notably, HSPA9 has also been implicated in several pathological conditions, including cancer, neurodegenerative diseases, and metabolic disorders, where its dysregulation can lead to disease progression. The study of HSPA9 recombinant proteins is crucial for elucidating its biological functions and interactions within cells. Utilizing recombinant technology allows researchers to produce high quantities of HSPA9 for biochemical assays, structural studies, and functional analyses. These studies are essential for understanding the molecular mechanisms by which HSPA9 operates, potentially leading to novel therapeutic strategies targeting HSPA9-related pathways in various diseases. Additionally, the exploration of HSPA9's role in mitochondrial integrity and cellular signaling may provide insights into its contributions to aging and longevity. As research advances, HSPA9 continues to emerge as an exciting target for further investigation, promising to unveil new dimensions of cellular biology and disease modulation.
