Analytical Data
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Gene name
HSPC152
- Application
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Alternative Names
ADGRF3; GPR113; PGR23; UNQ9196/PRO34000Adhesion G-protein coupled receptor F3; G-protein coupled receptor 113; G-protein coupled receptor PGR23
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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
Q9UI30
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Expression Region
1-125aa
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AA Sequence
MKLLTHNLLSSHVRGVGSRGFPLRLQATEVRICPVEFNPNFVARMIPKVEWSAFLEAADNLRLIQVPKGPVEGYEENEEFLRTMHHLLLEVEVIEGTLQCPESGRMFPISRGIPNMLLSEEETES
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Molecular Weight
30.2 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
Protein Description
HSPC152, also known as "heat shock protein family C member 152," is a protein that has garnered attention in biomedical research due to its potential roles in various physiological and pathological processes. Identified as a member of the heat shock protein family, HSPC152 is believed to be involved in cellular responses to stress, particularly during inflammation and immune responses. Its expression levels have been implicated in several diseases, including cancer, where it may influence tumor progression and immune evasion. The study of HSPC152 is crucial for understanding its functional mechanisms in cellular stress responses, and it may serve as a valuable biomarker for disease progression. Moreover, its potential involvement in modulating immune responses positions HSPC152 as a significant target for therapeutic interventions. Overall, ongoing research into HSPC152's structure, function, and interactions will deepen our understanding of its biological importance and could unveil novel strategies for treating diseases linked to dysregulation of heat shock proteins.
