Analytical Data
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Gene name
HSPF2
- Application
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Alternative Names
DNAJC4; MCG18; HSP-F2; DnaJ(Hsp40)Homolog,Subfamily C,Member 4; DnaJ-like protein HSPF2; Multiple endocrine neoplasia type 1 candidate protein number 18
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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
Q9NNZ3
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Expression Region
Met1~His150
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Molecular Weight
21kDa
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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
HSPF2 (Heat Shock Protein Family F Member 2) is a member of the heat shock protein family, known for its role in cellular stress response mechanisms, particularly in protein folding and protection against denaturing conditions. Research on HSPF2 has gained attention due to its potential implications in various physiological and pathological processes, including cancer progression, neurodegenerative diseases, and cellular aging. The protein is primarily localized in the mitochondria, suggesting its involvement in mitochondrial function and energy metabolism. Moreover, studies have shown that HSPF2 can interact with other molecular chaperones, enhancing their functionality during stress scenarios. Characterization of HSPF2 through recombinant protein expression allows for detailed investigations into its structural and functional properties, as well as its interactions with other proteins. Understanding the role of HSPF2 through recombinant techniques can elucidate its significance in disease mechanisms and may lead to novel therapeutic strategies targeting stress response pathways. As research progresses, elucidating the molecular functions and biological significance of HSPF2 will contribute to a deeper understanding of cellular homeostasis and stress management. This knowledge could potentially pave the way for the development of HSPF2-based biomarkers or therapeutic agents, thereby addressing a range of diseases linked to cellular stress responses.
