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anti-Human CIRBP Antibodies:
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Cow (Bovine) Polyclonal CIRBP Primary Antibody for WB - ABIN2778761
Schroeder, Metzger, Miller, Rhen: A Novel Candidate Gene for Temperature-Dependent Sex Determination in the Common Snapping Turtle. in Genetics 2016
Show all 2 Pubmed References
Human Polyclonal CIRBP Primary Antibody for IHC (p), WB - ABIN653083
Chen, Ran, Xie, Xu, Zhou: Cold-inducible RNA-binding protein mediates cold air inducible airway mucin production through TLR4/NF-κB signaling pathway. in International immunopharmacology 2017
Human Polyclonal CIRBP Primary Antibody for ELISA, IHC - ABIN4298803
Zeng, Kulkarni, Inoue, Getzenberg: Down-regulating cold shock protein genes impairs cancer cell survival and enhances chemosensitivity. in Journal of cellular biochemistry 2009
XCIRP is required to maintain the expression of adhesion molecules and cell movement during embryonic development.
Cold-inducible RNA binding protein XCIRP regulates anterior neural development in Xenopus.
Cold induction of serine and arginine rich splicing factor 5 (SRSF5) is independent of cold-inducible RNA-binding protein (CIRP) and RNA-binding motif protein 3 (RBM3).
The serum and synovial concentrations of CIRP in the rheumatoid arthritis patients were increased, suggesting that CIRP mediates inflammation and is a potential marker for synovial inflammation.
This study reports that cold-inducible RNA-binding protein (CIRBP) is a newly identified key regulator in DNA double-strand break (DSB) repair.
Crystal structure of the hnRNP A18 RNA recognition motif has been reported.
cold temperature can induce an airway inflammatory response and excess mucus production via a CIRP-mediated increase in mRNA stability and protein translation
CIRP Expression Is Induced in Skin Cancer Cells and in Keratinocytes Exposed to Lower-Dose But Not Higher-Dose UVB Radiation.
In human abdominal aortic aneurysm (AAA) tissue, Cold-inducible RNA-binding protein (CIRP) exhibited a 5.6-fold and 93% increase in mRNA and protein expression, respectively. In a rat AAA model, CIRP was upregulated significantly in a time-dependent manner in the serum and AAA tissue.
We found out that the link between CIRP and Snail is mediated by ERK and p38 pathways. EMT is a critical component of carcinoma metastasis and invasion. As demonstrated in this study, the biological role of CIRP in EMT may explain why CIRP overexpression has been associated with a bad prognosis in cancer patients.
CIRP was expressed in the bronchi of human COPD patients and was involved in inflammatory factors and MUC5AC expression after cold stimulation through the ERK and NF-kappaB pathways
Low CIRP expression is associated with colon Cancer.
this study shows that CIRP expression in bronchial airway epithelial cells of patients with chronic obstructive pulmonary disease is higher than that in healthy person
We generated a transgenic mouse model overexpressing human CIRP in the mammary epithelium to ask if it plays a role in mammary gland development. Effects of CIRP overexpression on mammary gland morphology, cell proliferation, and apoptosis were studied from puberty through pregnancy, lactation and weaning
Increased synovial fluid CIRP concentrations were closely associated with the severity of knee osteoarthritis
hnRNP A18 can promote tumor growth in in vivo models by coordinating the translation of pro-survival transcripts to support the demands of proliferating cells and increase survival under cellular stress.
Clinically, CIRP overexpression is significantly correlated with Cushing's disease recurrence. CIRP appears to play a critical tumorigenesis function in Cushing's disease and its expression might be a useful biomarker for tumor recurrence.
CIRP protein regulates telomerase activity in a temperature-dependent manner by regulating the level of TERT mRNAs.
Study shows that CIRP elevated plasma concentration is significantly associated with poor prognosis among patients with sepsis. Therefore, CIRP is a potential predictor of sepsis prognosis.
The expression of CIRP in pituitary adenoma is closely related with tumor proliferation and invasion, and its significantly elevated expression level indicates post-op recurrence.
CIRP inhibits DNA damage-induced apoptosis by regulating p53 protein.CIRP suppresses p53 upregulation during apoptosis.CIRP regulates the expression of genes involved in apoptosis.
High levels of CIRP protein expression was associated with a short survival rate in oral squamous cell carcinoma patients.
CIRP induces lung endoplasmic reticulum stress and downstream responses to cause sepsis-associated acute lung injury.
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.
tissue damage induced NADPH oxidase activation and increased the release of reactive oxygen species via cold-inducible RNA-binding protein (CIRP)-TLR4-MyD88 signaling.
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
this paper shows that cold air stimulation induced MUC5AC expression in wild-type mice but not in CIRP-/-) mice.
state. These data collectively suggest that a deficiency in CIRP accelerates the wound healing process
These results can provide new insights into the molecular mechanisms of Cirp function.
Findings suggest that CIRP could exert protective effects against oxidative stress, and that it might be a novel neuroprotective agent
targeting CIRP offers potential therapeutic implications in the treatment of hepatic I/R injury.
Cirp appears to play a critical carcinogenic function and its expression might be a useful biomarker for hepatocellular carcinomas risk prediction.
Cirp promotes the development of intestinal inflammation and colorectal tumors through regulating apoptosis and production of TNFalpha and IL23 in inflammatory cells.
alcohol exposure activates microglia to produce and secrete CIRP
Extracellular CIRP is a detrimental factor in stimulating inflammation to cause neuronal damage in cerebral ischemia
Down-regulated CIRP is involved in testicular injury after testicular torsion/detorsion.
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.
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.
Moderate hypothermia resulted in significant up-regulation of both RBM3 and CIRP mRNA in murine organotypic hippocampal slice cultures
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
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.
CIRP confers robustness to circadian oscillators through regulation of CLOCK expression.
Cold-inducible mRNA binding protein. Acts cooperatively with elavl1/elrA to stabilize AU-rich element (ARE)-containing mRNAs by binding to themm and inhibiting their deadenylation. Essential for embryonic gastrulation and neural development, acting to maintain the expression of a set of adhesion molecules, and cell movement during embryogenesis. Required for pronephros development (By similarity).
cold-inducible RNA-binding protein
, Glycine-rich RNA-binding protein CIRP
, glycine-rich RNA-binding protein CIRP
, hyperosmotic glycine rich protein-like
, Cold-inducible RNA-binding protein
, cold inducible RNA binding protein
, Cold-inducible RNA-binding protein-1
, Glycine-rich RNA-binding protein CIRP-A
, cold inducible RNA-binding protein
, cold-inducible RNA-binding protein 1
, cold-inducible RNA-binding protein A
, aggrecan promoter binding protein
, A18 hnRNP
, glycine-rich RNA binding protein
, cold-inducible RNA binding protein