Recombinant Human CASP7/caspase 7 Protein (His Tag) | PKSH031914

Recombinant Human CASP7/caspase 7 Protein (His Tag) | PKSH031914 | Gentaur US, UK & Europe Disrtribition

Synonyms: CASP-7;CMH-1;ICE-LAP3;LICE2;MCH3

Active Protein: N/A

Activity: A DNA sequence encoding the human CASP7 (P55210-1) (Met 1-Gln 303) was fused with a polyhistidine tag at the C-terminus.

Protein Construction: A DNA sequence encoding the human CASP7 (P55210-1) (Met 1-Gln 303) was fused with a polyhistidine tag at the C-terminus.

Fusion Tag: C-His

Species: Human

Expressed Host: E.coli

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 90 % as determined by reducing SDS-PAGE.

Endotoxin: Please contact us for more information.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 35kDa

Formulation: Lyophilized from sterile 20mM HEPES, 100mM NaCl, 1mM EDTA, 0.10% Sucrose, 0.1% chaps, pH 7.5

Reconstitution: Please refer to the printed manual for detailed information.

Background: Caspase 7, also known as caspase-7 and MCH3, belongs to the cysteine-aspartic acid protease (caspase) family. Caspases play a role in the signal transduction pathways of apoptosis, necrosis and inflammation. There are two major classes of caspases: initiators and effectors. The initiator isoforms (caspases-1, -4, -5, -8, -9, -10, -11, -12) are activated by, and interact with, upstream adaptor molecules through protein-protein interaction domains known as CARD and DED. Effector caspases (-3, -6, -7) are responsible for cleaving downstream substrates and are sometimes referred to as the executioner caspases. Caspase 7 exists in lung, skeletal muscle, liver, kidney, spleen and heart, and moderately in testis. Caspase 7 cannot be detected in the brain. Caspase 7 functions in the activation cascade of caspases responsible for apoptosis execution. It cleaves and activates sterol regulatory element binding proteins (SREBPs). It proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp- -Gly-217' bond. Overexpression promotes programmed cell death.

Research Area: N/A