Analytical Data
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Gene name
CIRBP
- Application
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Alternative Names
CIRP; A18HNRNP; Glycine-Rich RNA Binding Protein
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Species
Mouse
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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
P60824
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Expression Region
Met1~Glu172
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Molecular Weight
22kDa
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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
CIRBP (Cold-Inducible RNA-Binding Protein) is a crucial protein involved in cellular response to stressors such as low temperatures and oxidative stress. It plays a significant role in the regulation of gene expression by binding to specific RNA targets, influencing their stability and translation. Studies have shown that CIRBP is linked to various biological processes, including cell proliferation, differentiation, and apoptosis. The protein's expression is upregulated in response to cold shock, enabling cells to survive adverse conditions by promoting the synthesis of protective proteins. Given its implications in stress response mechanisms, CIRBP has garnered interest in the field of cancer research, where its expression levels can impact tumor growth and survival. Additionally, abnormalities in its function have been associated with various pathological conditions, including neurodegenerative diseases and inflammation. As a result, the recombinant expression and purification of CIRBP have become important for understanding its biochemical properties and potential therapeutic applications. Researchers are exploring the protein's structure and function through advanced techniques, contributing to our understanding of cellular stress responses and opening new avenues for targeted drug development. By generating recombinant CIRBP, scientists aim to elucidate its role in RNA metabolism and explore its potential as a biomarker or therapeutic target in diseases characterized by dysregulated cellular stress responses.
