Analytical Data
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Gene name
HSPC111
- Application
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Alternative Names
CGI 117; HBV pre S2 trans regulated protein 3; HBV pre-S2 trans-regulated protein 3; HSPC185; Hypothetical protein HSPC111; NOP16; NOP16 Gene; NOP16 nucleolar protein homolog ; NOP16 nucleolar protein homolog (yeast); NOP16_HUMAN
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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
Q9Y3C1
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Expression Region
1-178aa
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AA Sequence
MPKAKGKTRRQKFGYSVNRKRLNRNARRKAAPRIECSHIRHAWDHAKSVRQNLAEMGLAVDPNRAVPLRKRKVKAMEVDIEERPKELVRKPYVLNDLEAEASLPEKKGNTLSRDLIDYVRYMVENHGEDYKAMARDEKNYYQDTPKQIRSKINVYKRFYPAEWQDFLDSLQKRKMEVE
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Molecular Weight
45.32 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
HSPC111, also known as Heat Shock Protein Candidate 111, has garnered attention in the field of molecular biology and biomedicine due to its involvement in cellular stress responses and its potential implications in various diseases. Heat shock proteins (HSPs) play crucial roles in protein folding, protecting cells from stress-induced damage, and facilitating recovery from physiological insults. The HSPC111 protein is categorized within the larger family of HSPs and is believed to participate in crucial cellular processes, including protein stabilization and degradation. Recent studies have suggested that alterations in the expression or function of HSPC111 may be linked to pathological conditions such as cancer, neurodegenerative diseases, and autoimmune disorders. Therefore, understanding the functional mechanisms of HSPC111 at a molecular level is essential for uncovering its role in health and disease. Additionally, the development of recombinant HSPC111 proteins for experimental purposes holds promise for therapeutic innovations, including the design of targeted treatments and vaccine development. The ongoing research into HSPC111 aims to elucidate its structure-function relationships, regulatory mechanisms, and potential as a biomarker for disease progression, enhancing our overall knowledge of HSPs in cellular biology and their applications in medical research.
