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Validated All-in-One™ qPCR Primer for CAPN1(NM_001198868.2) Search again
Product ID:
HQP150821
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
CANP, CANP1, CANPL1, SPG76, muCANP, muCL
Gene Description:
calpain 1
Target Gene Accession:
NM_001198868.2(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
The calpains, calcium-activated neutral proteases, are nonlysosomal, intracellular cysteine proteases. The mammalian calpains include ubiquitous, stomach-specific, and muscle-specific proteins. The ubiquitous enzymes consist of heterodimers with distinct large, catalytic subunits associated with a common small, regulatory subunit. This gene encodes the large subunit of the ubiquitous enzyme, calpain 1. [provided by RefSeq].
Gene References into function
- Calpain (mu-calpain) is a signal transducer and activator of transcription (STAT) 3 and STAT5 protease.
- cleaves SNAP-23 in activated platelets
- investigates whether E-cadherin is a substrate for calpain and whether calpain-dependent proteolysis was associated with prostate cancer progression
- calpastatin and calpain-1 represent critical proximal elements in a cascade of pro-apoptotic events leading to Bax, mitochondria, and caspase-3 activation
- mu-calpain and m-calpain expression may be compromised in the anterior vaginal wall of women with uterovaginal prolapse
- platelet FXIII and calpain have roles in regulating integrin alpha(IIb)beta3 adhesive function
- calpain I and II, calpastatin, and the regulatory subunit localize to the cytosolic surface of the endoplasmic reticulum and Golgi apparatus membranes
- nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone-induced cell migration and invasion may occur, at least in part, through a novel mechanism involving phosphorylation of calpains that leads to their activation and secretion
- Epidermal growth factor activates m-calpain, which causes apoptosis of HaCaT keratinocytes
- Both precursor and mature forms of recombinant AIF were cleaved near the amino terminus by calpain I in vitro
- Mu-calpain is activated in human endometrial cells during hypoxia and that subsequent cleavage of the integrin beta3 cytoplasmic domain may give some adverse effects to the function of human endometrium
- mu-calpain, is a potential candidate for alpha-secretase in the regulated Alzheimer's beta-amyloid precursor protein alpha-processing
- These observations indicate that calpain is activated and reacts with alpha-fodrin as a substrate at the sarcolemma, and plays a key role in modulating sarcolemmal proteins to adapt to the specific conditions in each myopathy
- Immunohistochemistry of fixed, permeabilized oocytes exhibit localization of calpain mu isoform to the cortical region of the oocyte, as well as the cytosol.
- calpains may play a physiological role in the regulation of p73 protein stability
- the time- and concentration-dependent changes in [Ca2+]i that occurred during concentric exercise fall near but below the level necessary to cause autolysis of calpains in vivo
- The activation of calcineurin by calpain I in the brain of patients with Alzheimer's disease is reported.
- a novel role for PKCiota as a nicotine-activated, physiological calpain kinase that directly phosphorylates and activates calpains.
- beside its known effect on general muscle protein degradation, calpain contributes to Duchenne muscular dystrophy pathology by specifically degrading the compensatory protein utrophin
- Knockdown of mu-calpain decreased the proteolytic products of filamin and talin suggesting that their proteolysis could be one of the key mechanisms by which mu-calpain regulates cell migration.
- In vitro membrane binding of mu-calpain is due to the exposed hydrophobic surface of the active conformation and does not reduce the Ca2+ requirement for activation.
- Acyl coenzyme A-binding protein has a role in augmenting bid-induced mitochondrial damage and cell death by activating mu-calpain
- phosphorylation of Thr(138) predominantly defines the susceptibility of p35 to calpain-dependent cleavage and dephosphorylation of this site is a critical determinant of Cdk5-p25-induced cell death associated with neurodegeneration
- We have solved the structures of human calpain 1 and calpain 9 protease cores ; both structures have clear implications for the function of non-catalytic domains of full-length calpains in the calcium-mediated activation of the enzyme.
- Results suggest that calpains are involved in hypoxia-induced necrotic cell death, and that the inhibition of calpain switches hypoxia-induced cell death to apoptotic cell death without affecting cell viability.
- association between mu- and m-calpain, the specific inhibitor calpastatin, and axonal injury in post mortem brain tissue from patients who died from severe malaria
- Nitric oxide-induced motility in osteoclasts requires regulated Ca(2+) release, which activates mu-calpain. This occurs via the Ins(1,4,5)P(3)R1.
- These findings pinpoint calpain-1 as a regulator of Frizzled-7 turnover at the plasma membrane and reveal a link between Frizzled-7 cleavage and its activity.
- Taken together, these results suggested calpain involvement in Th1/Th2 dysregulation in MS patients.
- In patients with Alzheimer disease, over-activation of calpain because of calcium dysregulation causes increased degradation and thus decreased activity of PKA, which, in turn, contributes to down-regulation of CREB and impaired cognition and memory.
- Calpain emerges as a central player in E7-mediated degradation of Rb
- both calpain 1 and calpain 2 are essential for the replication of EV1 RNA.
- calpain 1 N-terminus is a mitochondrial targeting sequence
- platelets from patients with type 2 diabetes mellitus, were found to have enhanced tyrosine nitration and inactivation of the sarcoplasmic endoplasmic reticulum Ca2+-ATPase (SERCA-2), elevated platelet [Ca2+]i, and activation of mu-calpain.
- Protein adducts of iso[4]levuglandin E2 (iso[4]LGE2), a highly reactive product of free radical-induced lipid oxidation, accumulate in human glaucomatous trabecular meshwork (TM) but not in controls.
- The activity of calpain in human peripheral blood lymphocytes, was estimated by assessing the levels of limited proteolysis of calpastatin.
- The above suggests that cleavage of DAT by calpain may significantly modify dopamine homeostasis under pathological or physiological conditions.
- genetically determined IL-1alpha levels may modulate transcription of calpain and calpastatin.
- These results demonstrate calpain involvement in proteasome inhibitor-induced AR breakdown, and suggest that AR degradation is intrinsic to the induction of apoptosis in prostate cancer cells.
- Proof of concept that the calpastatin-based reagents may be useful to selectively detect the active conformation of calpain.
- These results provide novel insights into the mechanism of AIF release during cell death.
- degradation of human cTnT is mediated by calpain and not by caspases or proteasome