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Merck
CN

218799

Caspase-6, Human, Recombinant, E. coli

Caspase-6, Human, Recombinant is expressed as a single polypeptide in E. coli. Fused at the N- and C- termini to a His•Tag sequence. Undergoes spontaneous autoprocessing to yield the active enzyme.

别名:

Mch2

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关于此项目

NACRES:
NA.77
UNSPSC Code:
12352202
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产品名称

Caspase-6, Human, Recombinant, E. coli, Caspase-6, Human, Recombinant is expressed as a single polypeptide in E. coli. Fused at the N- and C- termini to a His•Tag sequence. Undergoes spontaneous autoprocessing to yield the active enzyme.

recombinant

expressed in E. coli

assay

≥95% (SDS-PAGE)

form

lyophilized

specific activity

≥6000 units/mg protein

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
avoid repeated freeze/thaw cycles

shipped in

wet ice

storage temp.

−70°C

Quality Level

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Other Notes

One unit is defined as the amount of enzyme that will cleave 1 nmol Ac-VEID-pNA (Cat. No. 218762) per h at 37°C, pH 7.2.
LeBlanc, A., et al. 1999. J. Biol. Chem.274, 23426.
Stennicke, H.R., and Salvesen, G.S. 1997. J. Biol. Chem.272, 25719.

Preparation Note

Following reconstitution, aliquot and freeze (-70°C). Stock solutions are stable for up to 3 months at -70°C.
Reconstitute to 1 unit/µl in PBS, 15% glycerol.

Disclaimer

Toxicity: Standard Handling (A)

General description

M.W. 11,000 and 18,000 (heterodimer).
Recombinant, human caspase-6 fused at the N- and C- termini to a His•Tag sequence and expressed in E. coli as a single polypeptide. Subsequently undergoes spontaneous autoprocessing to yield the active enzyme. Useful for the study of enzyme regulation and kinetics, cleavage of target substrates, and inhibitor screening. MW: 11000 and 18000.

存储类别

11 - Combustible Solids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Chunyan Wang et al.
Neuroscience letters, 721, 134802-134802 (2020-02-06)
Neuroinflammation in the spinal cord is a pathological event in remifentanil-induced hyperalgesia (RIH), but its underlying molecular mechanisms remain unclear. Recent studies recapitulate the significance of the intracellular protease caspase-6 in the release of inflammatory mediators and synaptic plasticity in

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