Caspase6 Antibody (Rabbit mAb) [L13G8]

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:1000 IP1:50 IHC1:1000 IF1:500

Application
WB, IP, IHC, IF

Reactivity
Mouse, Rat, Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
33 kDa 11 kDa,33 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Positive Control	Mouse brain tissue; Rat brain tissue; Human colon tissue; Jurkat cells; NIH/3T3 cells (staurosporine, 1 uM, 4 h); C6 cells; PC-12 cells; HAP1 cells; MCF7 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
Caspase6 Antibody (Rabbit mAb) [L13G8] detects endogenous levels of total Caspase6 protein.

Clone
L13G8

Synonym(s)
MCH2, CASP6, Caspase-6, CASP-6, CSP-6, Apoptotic protease Mch-2

Background
Caspase-6 belongs to the cysteine-dependent aspartate-specific protease family and is classified as an executioner caspase, though it operates through mechanisms that distinguish it from the other executioners, caspase-3 and caspase-7. Within the intrinsic apoptotic hierarchy, caspase-9 directly activates caspase-3 and caspase-7, and active caspase-3 subsequently processes caspase-6, positioning caspase-6 downstream in the proteolytic cascade rather than as a primary effector activated in parallel with the other executioners. Once activated, caspase-6 localizes to the nucleus and cleaves the nuclear intermediate filament proteins lamin A and lamin C, and gene disruption experiments in chicken DT40 cells demonstrate that this cleavage is specifically required for chromatin condensation and apoptotic body formation, since nuclei incubated in caspase-6-deficient apoptotic extracts fail to condense chromatin properly, a defect that is reversed by reintroducing caspase-6 and reproduced pharmacologically using the caspase-6-selective inhibitor z-VEID-fmk. This establishes lamin A and lamin C as caspase-6-specific substrates whose proteolysis drives nuclear envelope disassembly and nuclear shrinkage during the execution phase of apoptosis, a mechanistic role distinct from the DNA fragmentation functions carried out by caspase-3 and caspase-7. Beyond this canonical apoptotic role, caspase-6 acts as an essential mediator of innate immune signaling and programmed cell death during influenza A virus infection, where it interacts directly with RIPK3 and enhances RIPK3 binding to the viral sensor ZBP1 through a RIP homotypic interaction motif-dependent mechanism, promoting assembly of the ZBP1-associated multiprotein platform that coordinates pyroptosis, apoptosis, and necroptosis, a combined cell death program termed PANoptosis. This function operates independently of caspase-6's proteolytic activity, since caspase-6 deficiency impairs both PANoptosis and NLRP3 inflammasome activation following viral infection without requiring its catalytic cysteine, distinguishing this scaffolding role from the protease-dependent cleavage of lamin A during classical apoptosis. Caspase-6 additionally promotes the differentiation of alternatively activated macrophages during infection, extending its influence into innate immune cell polarization beyond direct cell death control. Caspase-6 activation is implicated in axonal degeneration and has been associated with Alzheimer's disease pathology through neuronal substrate cleavage, and its dual protease-dependent and protease-independent functions across apoptotic execution, viral innate immunity, and inflammasome-linked cell death programs make it a distinctive target among the executioner caspases for researchers studying nuclear disassembly mechanisms, antiviral host defense, and PANoptosis biology.

Background

Caspase-6 belongs to the cysteine-dependent aspartate-specific protease family and is classified as an executioner caspase, though it operates through mechanisms that distinguish it from the other executioners, caspase-3 and caspase-7. Within the intrinsic apoptotic hierarchy, caspase-9 directly activates caspase-3 and caspase-7, and active caspase-3 subsequently processes caspase-6, positioning caspase-6 downstream in the proteolytic cascade rather than as a primary effector activated in parallel with the other executioners. Once activated, caspase-6 localizes to the nucleus and cleaves the nuclear intermediate filament proteins lamin A and lamin C, and gene disruption experiments in chicken DT40 cells demonstrate that this cleavage is specifically required for chromatin condensation and apoptotic body formation, since nuclei incubated in caspase-6-deficient apoptotic extracts fail to condense chromatin properly, a defect that is reversed by reintroducing caspase-6 and reproduced pharmacologically using the caspase-6-selective inhibitor z-VEID-fmk. This establishes lamin A and lamin C as caspase-6-specific substrates whose proteolysis drives nuclear envelope disassembly and nuclear shrinkage during the execution phase of apoptosis, a mechanistic role distinct from the DNA fragmentation functions carried out by caspase-3 and caspase-7. Beyond this canonical apoptotic role, caspase-6 acts as an essential mediator of innate immune signaling and programmed cell death during influenza A virus infection, where it interacts directly with RIPK3 and enhances RIPK3 binding to the viral sensor ZBP1 through a RIP homotypic interaction motif-dependent mechanism, promoting assembly of the ZBP1-associated multiprotein platform that coordinates pyroptosis, apoptosis, and necroptosis, a combined cell death program termed PANoptosis. This function operates independently of caspase-6's proteolytic activity, since caspase-6 deficiency impairs both PANoptosis and NLRP3 inflammasome activation following viral infection without requiring its catalytic cysteine, distinguishing this scaffolding role from the protease-dependent cleavage of lamin A during classical apoptosis. Caspase-6 additionally promotes the differentiation of alternatively activated macrophages during infection, extending its influence into innate immune cell polarization beyond direct cell death control. Caspase-6 activation is implicated in axonal degeneration and has been associated with Alzheimer's disease pathology through neuronal substrate cleavage, and its dual protease-dependent and protease-independent functions across apoptotic execution, viral innate immunity, and inflammasome-linked cell death programs make it a distinctive target among the executioner caspases for researchers studying nuclear disassembly mechanisms, antiviral host defense, and PANoptosis biology.

References
https://pubmed.ncbi.nlm.nih.gov/11953316/ https://pubmed.ncbi.nlm.nih.gov/32298652/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%