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Dog (Canine) Polyclonal Caspase 6 Primary Antibody for ICC, IHC (fro) - ABIN252116
Berta, Park, Xu, Xie, Liu, Lü, Liu, Ji: Extracellular caspase-6 drives murine inflammatory pain via microglial TNF-α secretion. in The Journal of clinical investigation 2014
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Human Polyclonal Caspase 6 Primary Antibody for IHC, WB - ABIN223017
Nikolaev, McLaughlin, OLeary, Tessier-Lavigne: APP binds DR6 to trigger axon pruning and neuron death via distinct caspases. in Nature 2009
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Human Polyclonal Caspase 6 Primary Antibody for IHC, ELISA - ABIN1536082
Yashiro, Qiu, Hasegawa, Zhang, Matsuzaki, Hirakawa: An EGFR inhibitor enhances the efficacy of SN38, an active metabolite of irinotecan, in SN38-refractory gastric carcinoma cells. in British journal of cancer 2011
Dog (Canine) Polyclonal Caspase 6 Primary Antibody for IHC (p), IP - ABIN537397
Krajewska, Rosenthal, Mikolajczyk, Stennicke, Wiesenthal, Mai, Naito, Salvesen, Reed, Fiskum, Krajewski: Early processing of Bid and caspase-6, -8, -10, -14 in the canine brain during cardiac arrest and resuscitation. in Experimental neurology 2004
Human Polyclonal Caspase 6 Primary Antibody for WB - ABIN222958
Vohra, Sasaki, Miller, Chang, DiAntonio, Milbrandt: Amyloid precursor protein cleavage-dependent and -independent axonal degeneration programs share a common nicotinamide mononucleotide adenylyltransferase 1-sensitive pathway. in The Journal of neuroscience : the official journal of the Society for Neuroscience 2010
Human Polyclonal Caspase 6 Primary Antibody for ICC, ELISA - ABIN1002015
Wolf, Green: Suicidal tendencies: apoptotic cell death by caspase family proteinases. in The Journal of biological chemistry 1999
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Human Polyclonal Caspase 6 Primary Antibody for ICC, ELISA - ABIN1002016
Fernandes-Alnemri, Litwack, Alnemri: Mch2, a new member of the apoptotic Ced-3/Ice cysteine protease gene family. in Cancer research 1995
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Caspase-6 is posttranslationally palmitoylated by the palmitoyl acyltransferase HIP14 (show ZDHHC17 Antibodies) and that the palmitoylation of Caspase-6 inhibits its activation.
The bactericidal activity of caspase-6-/- macrophages was impaired compared to wild type cells. Caspase-6-/- mice showed higher expression of the IL-1b (show IL1B Antibodies) gene, known to be detrimental in murine melioidosis. Expression of the IL-10 (show IL10 Antibodies) gene was also increased in caspase-6-/- mice as early as 6 hours after infection. Treatment with exogenous IL-10 (show IL10 Antibodies) rendered mice more susceptible against B. pseudomallei challenge
caspase-6 could regulate breast cancer cell invasion by modulating MMP-2 (show MMP2 Antibodies) and MMP-9 (show MMP9 Antibodies) expression in 4T1 tumor-associated macrophages
Casp6 is unlikely to be involved in colitis-associated tumors.
p53 (show TP53 Antibodies) activity is an important upstream regulator of caspase-6 activity in muscle tissue.
TNFalpha (show TNF Antibodies)-induced RIP1 (show RALBP1 Antibodies)-independent caspase-6 activation was involved in regulating the relationship between autophagy and necroptosis.
CASP6 released from axonal terminals regulates microglial TNF-alpha (show TNF Antibodies) secretion, synaptic plasticity, and inflammatory pain.
both Caspase-3 (show CASP3 Antibodies) and Caspase-6 are implicated in axon degeneration that occurs as a part of normal development.
Casp6-/- neurons are protected against excitotoxicity, nerve growth factor deprivation and myelin-induced axonal degeneration. Furthermore, Casp6-deficient mice show an age-dependent increase in cortical and striatal volume.
This study demonistrated that elimination of caspase-6 protein and activity in the BACHD mouse model does not prevent the production of a 586 aa Htt (show HTT Antibodies) proteolytic fragment in the brain.
The prodomain region was found to be intrinsically disordered independent of the activation state of caspase-6; however, its complete removal resulted in the protection of the adjacent 26-32 region, suggesting that this region may play a regulatory role. The molecular details of caspase-6 dynamics in solution provide a comprehensive scaffold for strategic design of therapeutic approaches for neurodegenerative disorders.
SMSr is a novel and specific substrate of caspase-6, a non-conventional effector caspase (show CASP3 Antibodies) implicated in Huntington's and Alzheimer's diseases.
Results support the possibility that the Casp6 activity in the anterior olfactory nucleus of the olfactory bulb reflects degeneration in the entorhinal cortex and suggest that Casp6 activity in the olfactory bulb could represent degeneration associated with cognitive decline and early Alzheimer disease.
These data suggest that caspase-6 deactivating mutations may contribute to multifactorial carcinogenic transformations.
Caspase-6 undergoes helix-strand transition upon substrate binding. Caspase-6 shows distinctive conformational dynamics in its 130's region Local pKa Values of Key Amino Acid Residues within the 130's Region Vary between the Unliganded (Helical) and the VEID-bound (Strand) States of Caspase-6 .
Following specific binding to and internalization into HER2 (show ERBB2 Antibodies)-overexpressing tumor cells, the e23sFv-Fdt-casp6 protein induced tumor cell apoptosis and inhibited the proliferation of HER2 (show ERBB2 Antibodies)-overexpressing A172 and U251MG cells in vitro, but not in U87MG cells with undetectable HER2 (show ERBB2 Antibodies)
Results identified novel members of the CASP6 interactome and demonstrate that a number of them are involved in key signaling pathways observed in neurodegenerative diseases.
The ability of sox11 (show SOX11 Antibodies) to reduce effector caspase (show CASP3 Antibodies) activity was also reflected in its capacity to reduce cell death following toxic insult. Interestingly, other sox (show PIPOX Antibodies) proteins also had the ability to reduce caspase-6 activity but to a lesser extent than sox11 (show SOX11 Antibodies)
Caspase-6 plays a role in activating caspase-3 (show CASP3 Antibodies) in Tau truncation.
unmodified STAT1 (show STAT1 Antibodies) is cleaved at multiple sites by caspase-3 (show CASP3 Antibodies) and caspase-6 in malignant undifferentiated hematopoietic cells
This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein is processed by caspases 7, 8 and 10, and is thought to function as a downstream enzyme in the caspase activation cascade. Alternative splicing of this gene results in two transcript variants that encode different isoforms.
, caspase 6, apoptosis-related cysteine protease
, caspase 6
, apoptotic protease Mch-2
, apoptotic protease MCH-2