Recombinant Human Granzyme B/GZMB Protein (His Tag) | PKSH031663

Recombinant Human Granzyme B/GZMB Protein (His Tag) | PKSH031663 | Gentaur US, UK & Europe Disrtribition

Synonyms: CCPI;CGL-1;CGL1;CSP-B;CSPB;CTLA1;CTSGL1;HLP;SECT

Active Protein: N/A

Activity: A DNA sequence encoding the proform of human Granzyme B (NP_004122.1) (Met 1-Tyr 247) was expressed with a C-terminal polyhistidine tag.

Protein Construction: A DNA sequence encoding the proform of human Granzyme B (NP_004122.1) (Met 1-Tyr 247) was expressed with a C-terminal polyhistidine tag.

Fusion Tag: C-His

Species: Human

Expressed Host: HEK293 Cells

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

Purity: > 97 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

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: 27 kDa

Formulation: Lyophilized from sterile PBS, pH 7.4

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

Background: Granzyme B, also known as GZMB, is the most prominent member of the granzyme family of cell death-inducing serine proteases expressed in the granules of cytotoxic T lymphocytes (CTLs) and NK cells. Granzyme B enters the target cells depending on another membrane-binding granule protein, perforin, results in the activation of effector caspases and mitochondrial depolarization through caspase-dependent and -independent pathways, and consequently induces rapid cell apoptosis. Over 30 substrates of GZMB have been identified including the key substrate caspase-3, ICAD and Bid. GZMB is suggested to protect the host by lysing cells bearing on their surface 'nonself' antigens such as bacterial and viral infected-cells and tumor cells, and accordingly plays an essential role in immunosurveillance.

Research Area: N/A