Recombinant Mouse Cold-Inducible Rna-Binding Protein (CIRBP) Protein (His)

Name: Recombinant Mouse Cold-Inducible Rna-Binding Protein (CIRBP) Protein (His)
Brand: Beta LifeScience
SKU: BLC-02833P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Cirbp.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Cold-Inducible Rna-Binding Protein (CIRBP) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P60824
Target Symbol	CIRBP
Synonyms	Cirbp; CirpCold-inducible RNA-binding protein; A18 hnRNP; Glycine-rich RNA-binding protein CIRP
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MASDEGKLFVGGLSFDTNEQALEQVFSKYGQISEVVVVKDRETQRSRGFGFVTFENIDDAKDAMMAMNGKSVDGRQIRVDQAGKSSDNRSRGYRGGSAGGRGFFRGGRSRGRGFSRGGGDRGYGGGRFESRSGGYGGSRDYYASRSQGGSYGYRSSGGSYRDSYDSYATHNE
Expression Range	1-172aa
Protein Length	Full Length
Mol. Weight	22.6 kDa
Research Area	Cell Biology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Cold-inducible mRNA binding protein that plays a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. Promotes assembly of stress granules (SGs), when overexpressed. Seems to play an essential role in cold-induced suppression of cell proliferation. Acts as a translational repressor. Acts as a translational activator. Binds specifically to the 3'-untranslated regions (3'-UTRs) of stress-responsive transcripts RPA2 and TXN.
Subcellular Location	Nucleus, nucleoplasm. Cytoplasm.
Database References	KEGG: mmu:12696 STRING: 10090.ENSMUSP00000101004 UniGene: PMID: 28128330 Study demonstrates CIRP-induced endothelial cell (EC)pyroptosis in the lungs of C57BL/6 mice for the first time. CIRP stimulates the assembly and activation of Nlrp3 inflammasome in EC accompanied with caspase-1 activation, IL-1beta release and induction of proinflammatory cell death pyroptosis. PMID: 27217302 tissue damage induced NADPH oxidase activation and increased the release of reactive oxygen species via cold-inducible RNA-binding protein (CIRP)-TLR4-MyD88 signaling. PMID: 28492546 temperature-dependent accumulation of Cirbp mRNA is controlled primarily by the regulation of splicing efficiency, defined as the fraction of Cirbp pre-mRNA processed into mature mRNA PMID: 27633015 this paper shows that cold air stimulation induced MUC5AC expression in wild-type mice but not in CIRP-/-) mice. PMID: 27423012 state. These data collectively suggest that a deficiency in CIRP accelerates the wound healing process PMID: 26743936 These results can provide new insights into the molecular mechanisms of Cirp function. PMID: 25597958 Findings suggest that CIRP could exert protective effects against oxidative stress, and that it might be a novel neuroprotective agent PMID: 25498861 targeting CIRP offers potential therapeutic implications in the treatment of hepatic I/R injury. PMID: 25186836 Cirp appears to play a critical carcinogenic function and its expression might be a useful biomarker for hepatocellular carcinomas risk prediction. PMID: 25611373 Cirp promotes the development of intestinal inflammation and colorectal tumors through regulating apoptosis and production of TNFalpha and IL23 in inflammatory cells. PMID: 25187386 alcohol exposure activates microglia to produce and secrete CIRP PMID: 24223948 Extracellular CIRP is a detrimental factor in stimulating inflammation to cause neuronal damage in cerebral ischemia PMID: 24613680 Down-regulated CIRP is involved in testicular injury after testicular torsion/detorsion. PMID: 24094970 Depletion of Cirbp is found to increase the susceptibility of cells to the TNF-mediated inhibition of high amplitude expression of clock genes and modulates the TNF-induced cytokine response. PMID: 24337574 In animal models of hemorrhage and sepsis, CIRP is upregulated in the heart and liver and released into the circulation. In macrophages under hypoxic stress, CIRP translocates from the nucleus to the cytosol and is released. PMID: 24097189 Moderate hypothermia resulted in significant up-regulation of both RBM3 and CIRP mRNA in murine organotypic hippocampal slice cultures PMID: 23415676 we discovered that downregulation of CIRP resulted in increased germ cell apoptosis, possibly via the activation of the p44/p42, p38 and SAPK/JNK MAPK pathways PMID: 23001445 mRNAs binding with CIRP in testis were mostly associated with translation regulator activity, antioxidant activity, envelope and reproduction, including important mRNAs related to male infertility. PMID: 22819822 CIRP confers robustness to circadian oscillators through regulation of CLOCK expression. PMID: 22923437 Cirp functions to fine-tune the proliferation of undifferentiated spermatogonia by interacting with Dyrk1b. PMID: 22711815 These data suggest that mild hypothermia protects cells from TNF-alpha-induced apoptosis, at least partly, via induction of Cirp, and that Cirp protects cells by activating the ERK pathway. PMID: 16569452 These findings further reveal the diversity of mechanisms by which CIRP is regulated by environmental stresses and provide new insights into CIRP cytoplasmic function. PMID: 17967451 CIRP enhanced extracellular signal-regulated kinase 1 and 2 (ERK1/2) phosphorylation, and treatment with an MEK inhibitor decreased the proliferation caused by CIRP. PMID: 19158277 Overexpression of CIRP may reduce testicular damage induced by cryptorchidism by down-regulating the levels of p53 and Fas. PMID: 19331798

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.