Caspase-5, human recombinant | 1085

Caspase-5 (also know as ICErelIII, TY) is a member of the caspase-family of cysteine proteases. Similar to other caspases, caspase-5 exists in cells as an inactive proenzyme which is matured by proteolysis to yield large and small subunits. The active caspase-5 is a heterotetramer consisting of two large and two small subunits. To date the mechanism of caspase-5 activation and roles of caspase-5 in apoptosis are poorly understood. The recombinant active human caspase-5 was expressed in E. coli. The active caspase-5 is routinely tested at for its ability to enzymatically cleave these two substrates Ac-WEHD-pNA (Cat. #1102-200) or Ac-WEHD-AFC (1101-200).

1085 | Caspase-5 human recombinant DataSheet

Biomolecule/Target: Caspase-5

Synonyms: Caspase-5

Alternates names: Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12--like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

Taglines: A cysteine protease involved in apoptosis

NCBI Gene ID #: 57264

NCBI Gene Symbol: RETN

Gene Source: Human

Accession #: Q99P87

Recombinant: Yes

Source: E. coli.

Purity by SDS-PAGEs: 98%

Assay: SDS-PAGE

Purity: N/A

Assay #2: HPLC

Endotoxin Level: N/A

Activity (Specifications/test method): > 5000 units/mg

Biological activity: Test in process

Results: N/A

Binding Capacity: N/A

Unit Definition: One unit of the recombinant caspase-5 is the enzyme activity that cleaves 1 nmol of the caspase substrate WEHD-pNA (pNA: pnitroanaline) per hour at 37°C in a reaction solution containing 50 mM Hepes, pH 7.2, 50 mM NaCl, 0.1% Chaps, 10 mM EDTA, 5% Glycerol, and 10 mM DTT.

Molecular Weight: 20.2 kDa

Concentration: N/A

Appearance: Lyophilized powder

Physical form description: Lyophilized powder

Reconstitution Instructions: Reconstitution in HO to a concentration of 0.1-1.0 mg/ml. This solution can then be diluted into other aqueous buffers

Amino acid sequence: N/A