Analytical Data
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Gene name
HSPC163
- Application
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Alternative Names
CNIH4; HSPC163; Protein cornichon homolog 4; CNIH-4; Cornichon family AMPA receptor auxiliary protein 4
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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
Q9P003
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Expression Region
1-139aa
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AA Sequence
MEAVVFVFSLLDCCALIFLSVYFIITLSDLECDYINARSCCSKLNKWVIPELIGHTIVTVLLLMSLHWFIFLLNLPVATWNIYRYIMVPSGNMGVFDPTEIHNRGQLKSHMKEAMIKLGFHLLCFFMYLYSMILALIND
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Molecular Weight
41.03 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
HSPC163, also known as Heat Shock Protein Family C Member 1, is a member of the heat shock protein family, which plays a crucial role in cellular stress responses and protein folding. Recent studies have highlighted its potential involvement in various biological processes, including cell proliferation, differentiation, and apoptosis. Given its expression in multiple tissues and its suggested role in cancer development and progression, HSPC163 has become a focus of research in the context of tumor biology. Scientists have sought to elucidate the molecular mechanisms underlying HSPC163's functions, as well as its interactions with other proteins and signaling pathways. The reconstitution of HSPC163 as a recombinant protein offers valuable insights into its structural and functional properties, facilitating the development of targeted therapies for diseases associated with stress responses and dysregulated protein homeostasis. The investigation of HSPC163 aims to advance our understanding of its biological significance and therapeutic potential, particularly in the context of cancer and other pathological conditions where cellular stress plays a pivotal role.
