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Human Caspase 6 Protein expressed in Escherichia coli (E. coli) - ABIN2487275
Basu, Lu, Sun, Moor, Akkaraju, Huang: Proteolytic activation of protein kinase C-epsilon by caspase-mediated processing and transduction of antiapoptotic signals. in The Journal of biological chemistry 2002
Show all 8 references for ABIN2487275
caspase-6 could regulate breast cancer cell invasion by modulating MMP-2 (show MMP2 Proteins) and MMP-9 (show MMP9 Proteins) expression in 4T1 tumor-associated macrophages
Casp6 is unlikely to be involved in colitis-associated tumors.
p53 (show TP53 Proteins) activity is an important upstream regulator of caspase-6 activity in muscle tissue.
TNFalpha (show TNF Proteins)-induced RIP1 (show RALBP1 Proteins)-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 Proteins) secretion, synaptic plasticity, and inflammatory pain.
both Caspase-3 (show CASP3 Proteins) 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 Proteins) proteolytic fragment in the brain.
Neutrophil/macrophage contact activates CASP-6, producing interleukin-1 receptor-associated kinase-M (show IRAK3 Proteins) (IRAK-M (show IRAK3 Proteins)) cleavage and de-repression of alveolar macrophages; CASP-6 deletion protects mice from death caused by bacterial peritonitis.
Lamin A/C (show LMNA Proteins) and caspase-6 could be valuable tools in the knowledge of oocyte in vitro destiny
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 Proteins)-overexpressing tumor cells, the e23sFv-Fdt-casp6 protein induced tumor cell apoptosis and inhibited the proliferation of HER2 (show ERBB2 Proteins)-overexpressing A172 and U251MG cells in vitro, but not in U87MG cells with undetectable HER2 (show ERBB2 Proteins)
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 Proteins) to reduce effector caspase (show CASP3 Proteins) activity was also reflected in its capacity to reduce cell death following toxic insult. Interestingly, other sox (show PIPOX Proteins) proteins also had the ability to reduce caspase-6 activity but to a lesser extent than sox11 (show SOX11 Proteins)
Caspase-6 plays a role in activating caspase-3 (show CASP3 Proteins) in Tau truncation.
unmodified STAT1 (show STAT1 Proteins) is cleaved at multiple sites by caspase-3 (show CASP3 Proteins) and caspase-6 in malignant undifferentiated hematopoietic cells
p53 (show TP53 Proteins) activity is an important upstream regulator of caspase-6 activity in Huntington's disease.
In this study, the crystal structure of a full-length CASP6 zymogen mutant, proCASP6H121A, was solved.
Caspase-6 is likely important in most tissues during early development but is less involved in adult tissues
axon regeneration promoted by suppression of CASP2 (show CASP2 Proteins) and CASP6 is CNTF (show CNTF Proteins)-dependent and mediated through the JAK (show JAK3 Proteins)/STAT (show STAT1 Proteins) signalling pathway
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