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抗Human CAPNL1 抗体:
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Human Polyclonal CAPNL1 Primary Antibody for IHC (p), WB - ABIN3043467
Chen, Tang, Gao, Xu, Jiang, Cao, Fu, Sun, Liu, Shi: Fibrosis, adipogenesis, and muscle atrophy in congenital muscular torticollis. in Medicine 2014
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Human Polyclonal CAPNL1 Primary Antibody for ICC, IHC (fro) - ABIN3044292
Mo, Chen, Li, Zheng, Ke, Deng, Li, Jiang, Wu, Wang, Wang, Yang, Cao: Suppression of NHE1 by small interfering RNA inhibits HIF-1?-induced angiogenesis in vitro via modulation of calpain activity. in Microvascular research 2011
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Unexpected role of the L-domain of calpastatin during the autoproteolytic activation of human erythrocyte calpain.
Studies indicate that reactive oxygen and nitrogen species (RONS) and calpain play important roles in the development of airway and pulmonary vascular remodeling in COPD.
Calpain-1 was significantly expressed in Triple-negative breast cancer tissues varying from low to high with a significant correlation to lymph node status but not with the other clinicopathological variables, suggesting its role as a prognostic factor
These findings suggest that calpain and AR-V7 may serve as important biomarkers in the treatment of castration-resistant prostate cancer , and targeting calpain and AR-V7 may provide a new approach in overcoming docetaxel-resistance.
Rare homozygous and compound-heterozygous nonsense, missense, frameshift, and splice-site mutations in CAPN1 were identified in all hereditary spastic paraplegia affected individuals, and sequencing in additional family members confirmed the segregation of these mutations with the disease.
the cleavage of myoferlin, yielding a membrane-associated dual C2 domain 'mini-myoferlin', is reported.
mutations in CAPN1 are an additional cause of ataxia in mammals, including humans.
Calpain-1 expression is associated with poor relapse-free survival in breast cancer patients treated with trastuzumab.
Regulation of platelet-activating factor-mediated PTP1B activation by a Janus kinase 2/ calpain pathway has been reported.
HRNR deimination improves its cross-linking by TGases and its proteolytic processing by calpain-1.
calpains and calpastatin in patients with idiopathic pulmonary arterial hypertension (PAH) and mice with hypoxic or spontaneous (SM22-5HTT(+) strain) PH, were investigated.
calpain and protein kinase Calpha abnormal release promotes a constitutive release of matrix metalloproteinase 9 in peripheral blood mononuclear cells from cystic fibrosis patients
Endoplasmic reticulum stress may be associated with apoptosis of LECs, resulting in cataract formation in diabetic patients.
our findings suggest that the gene/protein expression of both CAPN1 and CAPN2, as well as the ERK1 and ERK2 genes and related proteins, could be molecular factors associated with more invasive tumor behavior in squamous cell laryngeal cancer.
This study demonstrated that Upregulation of calpain activity precedes tau phosphorylation and loss of synaptic proteins in Alzheimer's disease brain.
the calpain-dependent cleavage of Nav1.6 channels expressed in human embryonic kidney (HEK) 293 cells caused the upregulation of I(NaP)
Increased mu-Calpain Activity in Blasts of Common B-Precursor Childhood Acute Lymphoblastic Leukemia Correlates with Their Lower Susceptibility to Apoptosis.
Data indicate that calpain is responsible for processing translation termination factor eRF3 into its IAP-binding isoform p-eRF3.
NOS stimulation via PI3K, calpain proteases, and SIRT1-dependent deacetylation downstream from VEGFR2 activation contributes to these vasodilator responses.
Junctophilin-2 is cleaved by calpain at multiple sites, resulting in dysfunctional junctophilin-2 truncations.
Calpain-1 deficiency impairs mGluR-dependent LTD and fear memory extinction.
calpain contributes to the regulation of new gene expression that is necessary for these memory processes as a regulator of Ca(2+)-signal transduction pathway.
the present study suggested that ephrinB/EphB signaling contributes to spinal nociceptive processing via the actions of calpain1 and caspase3.
Authors provide the first evidence that calpain-1 regulates platelet hyperactivity in sickle mice.
A total of 55 genes were differentially expressed in micro-calpain knockout mice.
calpains inhibition plays crucial roles in vascular restenosis by preventing neointimal hyperplasia at the early stage via suppression of the MMP2/TGF-beta1 pathway.
indicate that calpain-1 and calpain-2 play opposite roles in high increased intraocular pressure-induced ischemic injury
Results strengthen the roles of both calpain-1 and PHLPP1 in synaptic plasticity and learning and memory, and illustrate the complexities of the interactions between multiple pathways participating in synaptic plasticity.
Genetic ablation of calpain-1 ameliorates chronic pain behavior in sickle cell mice.
Our results indicate that calpain mediates cytokine-induced collagen-I synthesis and proliferation of ASMCs via the mTORC2/Akt signalling pathway, thereby regulating airway smooth muscle remodelling in asthma.
Results indicate that calpain-1 and calpain-2 are differentially activated in hippocampus following seizure activity, with calpain-1 activation being limited to a small population of interneurons, and possibly triggering neuroprotective events, while calpain-2 is widely activated in pyramidal neurons of CA1 and CA3, and triggers neurodegenerative cascades.
Here we show the combined loss of glial glutamate transporters GLT1 and GLAST in spinal cord caused motor neuronal death and hindlimb paralysis.
These results suggested that Streptococcus pneuomoniae PLY induces the influx of calcium in Streptococcus pneumoniae-infected macrophages, followed by calpain activation and subsequent IL-1alpha maturation and secretion.
High calpain expression is associated with brain injury.
the expression of the full-length 60-kDa calcineurin protein is down-regulated due to over-activated calpain that cleaves calcineurin to form a 45-kDa fragment.
Attenuation of atherosclerotic lesions/inflammation in ApoE KO mice by simvastatin might be associated with the downregulation of CD36 and calpain-1.
Leukocyte calpain-1/calpain-2 deficiency reduces angiotensin II-induced inflammation and atherosclerosis but not abdominal Aortic aneurysms in mice.
TnT3 regulates transcription of Cacna1s, the gene encoding Cav1.1. Knocking down TnT3 in vivo downregulated Cav1.1.
CAPN1 HM535412:g.157T > C showed effect on meat redness.
The decreased expression of calpain 1A mRNA during development is highly correlated with muscle protein accumulation in neonatal Sus scrofa.
Right ventricular (RV) dysfunction from acute RV pressure overload is, in part, due to activation of calpain, and calpain inhibition would therefore attenuate RV dysfunction.
catalytic site amino acid residues 105-133 contained a disulfide bond between Cys(108) and Cys(115)
Association of polymorphisms with breed characteristics indicated that the mutations in CAPN1 detected by P4, P6 primers and that resulting in the change of Hinf 1 recognition site may be related to lean meat percentage.
The activities of Calpain and PLA2 on the muscle tissue of the bladders were analyzed.
Most heifer reproductive traits were not significantly affected by CAST and CAPN1 markers that are widely used to improve beef tenderness by selection and breeders should not be concerned with how these markers affect reproduction and other heifer traits with the possible exception of CAPN1 effects on calving date.
study is the first report on genetic variant g.-1256 A>C in the promoter region of CAPN1 gene association with the semen quality of Chinese Holstein bulls by influencing its expression
These results suggest an important role of genetics in meat color variation for cattle raised under the tropic conditions.
This work is supportive of the importance of CAPN1 and CAST for mean tenderness in beef.
Suppression of CANP1 resulted in the activation of caspase and heat-shock-protein systems which might in turn regulate apoptosis through the caspase-dependent cell death pathway. [CANP1]
bovine CAPN-CAST interaction were well reflected in the geometry between the pharmacophore features and its shape constraints identified using our modeled bovine CAPN1/CAST4 complex structures
This work confirms the importance of CAPN1 and CAST for tenderness in beef, provides a new effect of CAST on beef tenderness, and questions the utility of GHR as a selection marker for beef quality.
It was found that the marker c.3379G > A in the CAPN1 gene influences the Ca content in the meat of this Nelore population, with the rare genotype associated with less Ca content.
m- and micro-calpain immunosignals in the cytoplasm both along the Z disk/I band regions and in the form of intracellular stores.
Association of polymorphisms in calpain 1, (mu/I) large subunit, calpastatin, and cathepsin D genes with meat quality traits in double-muscled Piemontese cattle.
Relationships of the calpain system with meat tenderness and carcass traits were examined for 94 purebred Angus bulls.
The association of polymorphisms in calpastatin and mu-calpain genes with meat tenderness in 3 French beef breeds is reported.
A new insertion/deletion (InDel) polymorphism, consisting of a change of seven nucleotides for only one nucleotide (TCTGGGT --> C) within intron 17 of the CAPN1 gene, is reported.
mu-calpain (CAPN1S) has a role in the proteolysis process and the meat tenderness of young cattle
CAPN1 4751 affected all meat traits and CAPN1 316 showed association with tenderness and color.
The mu-calpain gene marker improved beef tenderness without affecting other objective meat quality traits in heterozygous cattle compared with homozygotes for the unfavorable allele.
The present study indicated that calpain-system gene markers are suitable for use in marker-assisted selection to improve meat tenderness in Brahman cattle without negative effects on other production and carcass characteristics.
Single-nucleotide polymorphisms (SNPs) in the calpain (CAPN) and calpastatin (CAST) genes, described from Bos primigenius taurus, were examined to see if they were polymorphic in Nellore cattle.
Reduced eNOS protein levels were accompanied by an increase in intracellular Ca(2+), augmented production of reactive oxygen species (ROS) and induction of Ca(2+)-dependent calpain activity.
investigation of calpain 1 binding with alpha-actinin; propose that calpain 1 interacts in a resting state with cytoskeletal targets
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. Several transcript variants encoding two different isoforms have been found for this gene.
, calcium-activated neutral proteinase 1
, calpain mu-type
, calpain, large polypeptide L1
, calpain-1 catalytic subunit
, calpain-1 large subunit
, cell proliferation-inducing gene 30 protein
, cell proliferation-inducing protein 30
, calpain 1, large subunit
, micromolar calcium-activated neutral protease 1
, micromolar calcium activated neutral protease 1
, mu-calpain large subunit