GZMB Mouse
Granzyme B, C11, CTLA-1, Cathepsin G-like 1, CTSGL1, Cytotoxic T-lymphocyte proteinase 2, Lymphocyte protease, Fragmentin-2, Granzyme-2, Human lymphocyte protein, HLP, SECT, T-cell serine protease 1-3E, CGL1, CSPB, CTLA1, GRB, GZMB, CCPI, CGL-1, CSP-B.
Greater than 90.0% as determined by SDS-PAGE.
Description
GZMB Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 235 amino acids (19-247 aa) and having a molecular mass of 26.3kDa.
GZMB is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Product Specs
Granzyme-B, also known as GZMB, is a serine protease found primarily in the granules of cytotoxic T cells and natural killer (NK) cells. It plays a crucial role in cell-mediated apoptosis by inducing programmed cell death in target cells. GZMB is secreted alongside perforin, a pore-forming protein, which allows GZMB to enter the target cell and initiate apoptosis.
Recombinant Mouse GZMB, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain with a molecular weight of 26.3 kDa. It encompasses amino acids 19-247, corresponding to the mature protein, and has a 6-amino acid His-tag fused at the C-terminus. The protein undergoes purification using proprietary chromatographic techniques.
The GZMB solution is provided at a concentration of 0.25 mg/ml in a buffer containing 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
For short-term storage (2-4 weeks), store the GZMB solution at 4°C. For long-term storage, it is recommended to store the solution at -20°C. To further enhance stability during long-term storage, consider adding a carrier protein like HSA or BSA (0.1%). Avoid repeated freeze-thaw cycles to maintain protein integrity.
The purity of GZMB is determined by SDS-PAGE analysis and is guaranteed to be greater than 90%.
The biological activity of GZMB is determined by measuring its ability to cleave the substrate Boc-Ala-Ala-Asp-SBzl at 37°C. One unit of activity is defined as the amount of enzyme required to cleave 1 picomole of substrate per minute. The specific activity of GZMB is greater than 9,000 pmol/min/µg.
Granzyme B, C11, CTLA-1, Cathepsin G-like 1, CTSGL1, Cytotoxic T-lymphocyte proteinase 2, Lymphocyte protease, Fragmentin-2, Granzyme-2, Human lymphocyte protein, HLP, SECT, T-cell serine protease 1-3E, CGL1, CSPB, CTLA1, GRB, GZMB, CCPI, CGL-1, CSP-B.
GEIIGGHEVK PHSRPYMALL SIKDQQPEAI CGGFLIREDF VLTAAHCEGS IINVTLGAHN
IKEQEKTQQV IPMVKCIPHP DYNPKTFSND IMLLKLKSKA KRTRAVRPLN LPRRNVNVKP
GDVCYVAGWG RMAPMGKYSN TLQEVELTVQ KDRECESYFK NRYNKTNQIC AGDPKTKRAS
FRGDSGGPLV CKKVAAGIVS YGYKDGSPPR AFTKVSSFLS WIKKTMKSSH HHHHH
Product Science Overview
Granzyme B is a member of the granzyme family, which consists of several serine proteases. The enzyme is synthesized as an inactive precursor and is activated upon entering the target cell. It is known for its ability to cleave specific substrates, leading to the activation of caspases, which are essential for the execution of apoptosis .
Granzyme B is delivered into target cells through the action of another protein called perforin. Perforin forms pores in the target cell membrane, allowing Granzyme B to enter the cell. Once inside, Granzyme B cleaves and activates various substrates, including caspases, which then orchestrate the cell’s apoptotic machinery .
Recombinant Granzyme B from mouse is widely used in research to study its role in immune responses and apoptosis. It is also utilized in various assays to understand its interaction with other proteins and its potential therapeutic applications. The recombinant form is typically produced in cell lines such as mouse myeloma cells and is purified to high levels of activity and purity .
Granzyme B has been implicated in various diseases and conditions. Its role in inducing apoptosis makes it a critical player in immune surveillance against cancer and viral infections. Additionally, dysregulation of Granzyme B activity has been associated with autoimmune diseases and chronic inflammatory conditions .
