Analytical Data
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Gene name
HSPC105
- Application
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Alternative Names
SDR42E1; HSPC105; Short-chain dehydrogenase/reductase family 42E member 1
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8WUS8
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Expression Region
1-383aa
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AA Sequence
MDPKRSQKESVLITGGSGYFGFRLGCALNQNGVHVILFDISSPAQTIPEGIKFIQGDIRHLSDVEKAFQDADVTCVFHIASYGMSGREQLNRNLIKEVNVRGTDNILQVCQRRRVPRLVYTSTFNVIFGGQVIRNGDESLPYLPLHLHPDHYSRTKSIAEQKVLEANATPLDRGDGVLRTCALRPAGIYGPGEQRHLPRIVSYIEKGLFKFVYGDPRSLVEFVHVDNLVQAHILASEALRADKGHIASGQPYFISDGRPVNNFEFFRPLVEGLGYTFPSTRLPLTLVYCFAFLTEMVHFILGRLYNFQPFLTRTEVYKTGVTHYFSLEKAKKELGYKAQPFDLQEAVEWFKAHGHGRSSGSRDSECFVWDGLLVFLLIIAVLM
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Molecular Weight
69.6 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
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Protein Description
HSPC105, also known as heat shock protein family C member 1, is an essential protein involved in cellular stress responses, particularly in the context of heat shock and other forms of environmental stress. Its expression is significantly upregulated in various tissues during stress conditions, suggesting a protective role in cell survival and maintenance of protein homeostasis. Research on HSPC105 has revealed its potential implications in cancer biology, as it may influence tumor growth and the body's response to therapy. Furthermore, studies indicate that HSPC105 may play a role in the regulation of immune responses and inflammation. The understanding of HSPC105's structure and function is crucial, as it may serve as a therapeutic target or biomarker for various diseases. Recent advances in recombinant protein technology have facilitated the production and purification of HSPC105, allowing for in-depth characterization of its biological functions and interactions at the molecular level. Additionally, investigations into HSPC105's role in different cellular pathways have opened avenues for exploring its potential applications in regenerative medicine and cancer therapeutics. Given the protein's vital functions and its regulatory mechanisms, further research on HSPC105 is expected to shed light on its broader implications in health and disease. Overall, the study of HSPC105 and its recombinant forms continues to be a promising field for understanding stress response mechanisms and developing novel therapeutic strategies.
