Caspase 10 Human Caspase Cysteine Peptidase Enzymatic LeadHunter Assay - TW

Background Information:

Caspases are the executioners of programmed cell death (apoptosis), a normal process used physiologically to eliminate specific cells or cell types without damaging surrounding cells or causing an inflammatory response. All caspases belong to a family of proteases characterized by a cysteine residue in the active site and display specificity for Asp residues. Caspases are present in all cells as a procaspase, which becomes activated through proteolytic cleavage by other proteases including other caspases. Caspase 10, expressed in many tissues and cell lines, cleaves and activates caspase 3, 4, 6, 7, 8, and 9, which causes the proteolytic cleavage of many key proteins such as PARP (poly (ADP-ribose) polymerase). Cleavage of PARP occurs in many different systems during apoptosis. Caspase 10 has two death effector domains (DEDs) that bind to the DED in the adapter molecule FADD and recruits TNFR1 to form complexes with these receptors. Caspase 10 is therefore involved in the TNFR1 induced apoptosis. Caspase inhibitors are currently sought as therapeutics for such diseases as Alzheimer's, Parkinson's and cerebral/myocardial ischemia.

Family:

Protease

Sub Family:

Caspase

Class:

Cysteine Peptidase

Protein Name:

Caspase 10

Uniprot Number:

Q92851

Gene Name:

CASP10

Gene ID:

843

Gene Aliases:

MCH4

Accession Number:

NM_032977

Organism:

Human

Construct Details:

Fragment, Recombinant