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抗Rat (Rattus) Caspase 2 抗体:
抗Mouse (Murine) Caspase 2 抗体:
抗Human Caspase 2 抗体:
Human Polyclonal Caspase 2 Primary Antibody for WB - ABIN3043696
Jiang, Li, Zhou, Wang, Zhang, Wang: Colistin-induced apoptosis in PC12 cells: involvement of the mitochondrial apoptotic and death receptor pathways. in International journal of molecular medicine 2014
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Human Polyclonal Caspase 2 Primary Antibody for IP, ELISA - ABIN540283
Troy, Shelanski: Caspase-2 redux. in Cell death and differentiation 2003
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Human Polyclonal Caspase 2 Primary Antibody for IHC, WB - ABIN222882
Basu, Adkins, Basu: Down-regulation of caspase-2 by rottlerin via protein kinase C-delta-independent pathway. in Cancer research 2008
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Human Polyclonal Caspase 2 Primary Antibody for IHC (fro), WB - ABIN550327
Kuida, Lippke, Ku, Harding, Livingston, Su, Flavell: Altered cytokine export and apoptosis in mice deficient in interleukin-1 beta converting enzyme. in Science (New York, N.Y.) 1995
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Polyclonal Caspase 2 Primary Antibody for IHC (p), WB - ABIN540568
Bergeron, Perez, Macdonald, Shi, Sun, Jurisicova, Varmuza, Latham, Flaws, Salter, Hara, Moskowitz, Li, Greenberg, Tilly, Yuan: Defects in regulation of apoptosis in caspase-2-deficient mice. in Genes & development 1998
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caspase-2 has a role as an initiator caspase in lipoapoptosis
tail regression at metamorphosis implicates an apoptotic pathway inducible by T(3) hormone in an organ autonomous manner and involving the cell death executioners BH3 interacting domain death agonist and Caspases-2 and -8
Caspase-2 phosphorylated at S135 binds 14-3-3zeta, thus preventing C2 dephosphorylation.
The data demonstrate that cell death is prevented during mitosis through the inhibitory phosphorylation of caspase-2 and suggest that under conditions of mitotic arrest, cdk1-cyclin B1 activity must be overcome for apoptosis to occur.
A novel function for caspase-2 in myocyte differentiation and myogenesis.
Casp2(-/-) mice, which are more susceptible to genomic instability, are limited in their ability to respond to DNA damage and thus carry more damaged cells resulting in accelerated tumourigenesis.
BECN1/Beclin 1 binding to viral phosphoprotein (P) induced an incomplete autophagy via activating the pathways CASP2-AMPK-AKT-MTOR and CASP2-AMPK-MAPK by decreasing CASP2.
We further generated Casp2(C320S) mutant mice to demonstrate that caspase-2 catalytic activity is essential for its function in limiting aneuploidy. Our results provide direct evidence that the apoptotic activity of caspase-2 is necessary for deleting cells with mitotic aberrations to limit aneuploidy
These results provide the first evidence of caspase-2 in regulating haematopoietic stem cell and progenitor differentiation, as well as aneuploidy, in vivo.
Study describes a novel pathological process in which caspase-2 cleavage of tau at Asp314 impairs cognitive and synaptic function in animal and cellular models of tauopathies by promoting the missorting of tau to dendritic spines.
Caspase-2 deficiency protected mice from diet-induced obesity, metabolic syndrome and nonalcoholic fatty liver disease.
The tumor-modulatory effects of Caspase-2 and Pidd1 do not require the scaffold protein Raidd
Data show that indoles can effectively suppress acute hepatic inflammation caused by staphylococcal enterotoxin B (SEB) maybe mediated by decreased expression of miR-31 and caspase-2-dependent apoptosis in T cells.
Data indicate that the nucleotide-binding domain and leucine-rich repeat containing (NLRP3)-caspase-2 axis drives general endoplasmic reticulum (ER) stress-induced inflammasome activation.
these studies elucidate a Caspase-2-p53 signaling network that impacts lung tumorigenesis and chemotherapy response in vivo.
data strongly suggest that caspase-2 deficiency leads to increased cellular stress largely because these mice fail to respond to oxidative stress by upregulating their antioxidant defense mechanism
These results demonstrate an important role for caspase-2 in regulating proteome and metabolome remodelling during ageing.
Caspase-2 is not a suppressor in MYCN-induced neuroblastoma and suggest a tissue and context-specific role for caspase-2 in tumorigenesis.
our data point to a critical and novel role for caspase-2 in maintaining bone homeostasis by modulating ROS levels and osteoclast apoptosis during conditions of enhanced oxidative stress that occur during aging
Report the novel finding that CASP2 is an endogenous repressor of autophagy. Knockout or knockdown of CASP2 resulted in upregulation of autophagy in a variety of cell types and tissues.
Caspase-2 activation is one of the few early molecular events identified in Parkinson disease models.
The involvement of caspase 2 and iNOS-mediated apoptotic signaling in nicotine plus high fat diet-induced hepatocellular apoptosis, is reported.
Axin expression may facilitate AKI-induced caspase-2 activation followed by activation of PARP and initiation of the necrotic cell death pathway.
Data strongly argue against a critical role for caspase-2 in ER-stress-induced apoptosis.
caspase-2 negatively regulates necroptotic cell death
The authors found that tumor necrosis factor receptor-associated factor 2 (TRAF2), as well as TRAF1 and 3, directly binds to the active caspase-2 dimer.
these data identify a novel caspase-2-interacting factor, FAN, and expand the role for the enzyme in seemingly non-apoptotic cellular mechanisms.
Results suggest that TG-induced macrophage cell death is mediated via the caspase-2.
study demonstrates that apoptosis inhibitor 5 (API5/AAC11) is an endogenous and direct inhibitor of caspase-2. API5 protein directly binds to the caspase recruitment domain (CARD) of caspase-2 and impedes dimerization and activation of caspase-2.
This peptide, Ac-VDTTD-AFC, was efficiently cleaved by purified caspase-2 and auto-activating caspase-2 in mammalian cells, and exhibited better selectivity for caspase-2 relative to caspase-3 than reagents that are currently available.
There results support a special role for miR-149 in malignant glioma by targeting Caspase-2
Whole exome sequencing (WES) of an affected fetus, and subsequent Sanger sequencing of the second fetus, revealed a homozygous frameshift variant in CRADD, which encodes an adaptor protein that interacts with PIDD and caspase-2 to initiate apoptosis
This study shows that human procaspase-2 interaction with 14-3-3 zeta is governed by phosphorylation at both S139 and S164.
NPM1-dependent nucleolar PIDDosome is a key initiator of the caspase-2 activation cascade.
Sensitization of colon carcinoma cells to radiation-induced cell death and DNA-damage by HuR knockdown critically depends on caspase-2.
BCL9L dysfunction contributes to aneuploidy tolerance in both TP53-WT and mutant cells by reducing basal caspase-2 levels and preventing cleavage of MDM2 and BID.
CASP2 down-regulation had a reverse relationship with miR-383 down-regulation in regulating epithelial ovarian cancer development.
Results suggest that mutations at all three cleavage sites of caspase-2 protein neither affect the macromolecular core complex assembly, nor modify caspase-2 activity upon DNA damage. Consequently, caspase-2 activation occurs in the macromolecular complex without its dissociation.
These findings indicate that miR-125a-5p decreases after HOTAIR knockdown to promote cancer cell apoptosis by releasing caspase 2.
We have also demonstrated that these correlations are tissue specific being reduced (CASP9 and CASP10) or different (CASP2) in the liver
the initiator caspase-2 is required for robust death of ovarian cancer cells induced by FASN inhibitors
HuR sensitizes adenocarcinoma cells to the intrinsic apoptotic pathway by upregulating the translation of caspase-2.
Authors have demonstrated in vitro and in vivo that loss of function of caspase-2 allows to escape oncogenic stress induced senescence.
EtOH-induced mitochondria-mediated apoptosis is initiated by caspase-2 activation, which is regulated by CoQ10
the capacity for blastocysts to undergo further development is related to degree of group II caspase activity
Caspase-2 expression was increased two-fold in the hypoxia group. After Src kinase inhibition followed by hypoxia, caspase-2 expression was similar to normoxia levels: hypoxia results in increased expression of caspase-2 protein in the cytosolic fraction of the cerebral cortex of the newborn piglets. This increase is mediated by Src kinase.
hypoxia/re-oxygenation injury in cultured proximal tubule cells induced apoptosis by activation of caspase-2, which is required for the mitochondrial translocation of Bax.
This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Caspases mediate cellular apoptosis through the proteolytic cleavage of specific protein substrates. The encoded protein may function in stress-induced cell death pathways, cell cycle maintenance, and the suppression of tumorigenesis. Increased expression of this gene may play a role in neurodegenerative disorders including Alzheimer's disease, Huntington's disease and temporal lobe epilepsy. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
, ICH-1 protease
, protease ICH-1
, neural precursor cell expressed developmentally down-regulated protein 2
, protein phosphatase 1, regulatory subunit 57
, caspase 2, apoptosis-related cysteine peptidase (neural precursor cell expressed, developmentally down-regulated 2)
, ICH1 protease
, caspase 2, apoptosis-related cysteine protease
, cysteine protease caspase-2