C4977
Caspase 6 human
≥90% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous solution, >1,000 units/mg protein, C-terminal histidine tagged
Synonym(s):
Mch2
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About This Item
MDL number:
UNSPSC Code:
12352200
recombinant
expressed in E. coli
Assay
≥90% (SDS-PAGE)
form
buffered aqueous solution
specific activity
>1,000 units/mg protein
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... CASP6(839)
Biochem/physiol Actions
Caspases are cysteine aspartic proteases that play a central role in apoptosis. Caspase 6 (Mch2) belongs to the group of effector caspases and is localized downstream of caspase 3. It has been suggested that caspase 6 is implicated in Alzheimer′s disease.
Caspase 6 proenzyme is expressed in E. coli as a C-terminal histidine-tagged protein. It undergoes autoactivation and autoprocessing to 21 and 19 kDa proteins (large subunits), and 14 kDa protein (small subunit). Substrate specificity studies show a favorable interaction of caspase 6 with peptides containing Val in P46. Thus, Ac-VEID-pNA is used as chromogenic substrate for caspase 6.
Caspase 6 proenzyme is expressed in E. coli as a C-terminal histidine-tagged protein. It undergoes autoactivation and autoprocessing to 21 and 19 kDa proteins (large subunits), and 14 kDa protein (small subunit). Substrate specificity studies show a favorable interaction of caspase 6 with peptides containing Val in P46. Thus, Ac-VEID-pNA is used as chromogenic substrate for caspase 6.
Physical form
Solution in 10% sucrose containing 50 mM HEPES, pH 7.5, 0.5 M NaCl, 100 mM imidazole, 0.1% CHAPS, 4 mM DTT
Other Notes
One unit will cleave 1 nmole of Ac-VEID-pNA per minute at 25 °C at pH 7.4.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Repr. 1B
Storage Class Code
6.1D - Non-combustible acute toxic Cat.3 / toxic hazardous materials or hazardous materials causing chronic effects
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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E S Alnemri
Journal of cellular biochemistry, 64(1), 33-42 (1997-01-01)
So far nine human aspartate-specific cysteine proteases (ASCPs) have been identified and cloned in our lab and others. Their sequence and structural homology to the nematode Ced-3 implicated them in the cell death pathway of mammalian cells. Recent evidence suggests
Protein complexes activate distinct caspase cascades in death receptor and stress-induced apoptosis.
S B Bratton et al.
Experimental cell research, 256(1), 27-33 (2000-03-31)
Caspases play a central role in the execution phase of apoptosis and are responsible for many of the morphological features normally associated with this form of cell death. Caspases can activate one another and consequently can initiate specific caspase cascades.
A LeBlanc et al.
The Journal of biological chemistry, 274(33), 23426-23436 (1999-08-07)
Neuronal cell death, neurofibrillary tangles, and amyloid beta peptide (Abeta) deposition depict Alzheimer's disease (AD) pathology, but neuronal loss correlates best with dementia. We have shown that increased production of Abeta is a consequence of neuronal apoptosis, suggesting that apoptosis
H R Stennicke et al.
The Journal of biological chemistry, 272(41), 25719-25723 (1997-11-05)
The observation that the nematode cell death effector gene product Ced-3 is homologous to human interleukin-1beta-converting enzyme (caspase-1) has led to the discovery of at least nine other human caspases, many of which are implicated as mediators of apoptosis. Significant
T Fernandes-Alnemri et al.
Cancer research, 55(13), 2737-2742 (1995-07-01)
We have developed a PCR approach to clone new apoptotic Ced-3/Ice-like cysteine protease genes. This approach uses degenerate oligonucleotides encoding the highly conserved pentapeptides QACRG and GSWFI that are present in all known apoptotic cysteine proteases. Using this approach, we
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