GZMB Human, sf9
Granzyme B, T-Cell Serine Protease 1-3E, Cathepsin G-Like 1, Granzyme B (Granzyme 2, Cytotoxic T-Lymphocyte-Associated Serine Esterase 1, Cytotoxic T-Lymphocyte Proteinase 2, Cytotoxic Serine Protease B , Human Lymphocyte Protein, Fragmentin 2, EC 3.4.21.79, CTSGL1, CTLA1 , CSPB , CGL1, SECT , C11, HLP , Cytotoxic T-Lymphocyte-Associated Serine Esterase 1, Lymphocyte Protease, Fragmentin-2 , Granzyme 2 , Granzyme-2 , EC 3.4.21, CTLA-1 , CGL-1, CSP-B, CCPI , GRB.
Greater than 95.0% as determined by SDS-PAGE.
Description
GZMB produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 235 amino acids (19-247a.a.) and having a molecular mass of 26.5kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). GZMB is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Granzyme B, T-Cell Serine Protease 1-3E, Cathepsin G-Like 1, Granzyme B (Granzyme 2, Cytotoxic T-Lymphocyte-Associated Serine Esterase 1, Cytotoxic T-Lymphocyte Proteinase 2, Cytotoxic Serine Protease B , Human Lymphocyte Protein, Fragmentin 2, EC 3.4.21.79, CTSGL1, CTLA1 , CSPB , CGL1, SECT , C11, HLP , Cytotoxic T-Lymphocyte-Associated Serine Esterase 1, Lymphocyte Protease, Fragmentin-2 , Granzyme 2 , Granzyme-2 , EC 3.4.21, CTLA-1 , CGL-1, CSP-B, CCPI , GRB.
GEIIGGHEAK PHSRPYMAYL MIWDQKSLKR CGGFLIRDDF VLTAAHCWGS SINVTLGAHN IKEQEPTQQF IPVKRPIPHP AYNPKNFSND IMLLQLERKA KRTRAVQPLR LPSNKAQVKP GQTCSVAGWG QTAPLGKHSH TLQEVKMTVQ EDRKCESDLR HYYDSTIELC VGDPEIKKTS FKGDSGGPLV CNKVAQGIVS YGRNNGMPPR ACTKVSSFVH WIKKTMKRYH HHHHH
Product Science Overview
Granzyme B is a member of the granzyme family of serine proteases. The human recombinant form of Granzyme B, produced in Sf9 cells, is a single, glycosylated polypeptide chain containing 235 amino acids. The molecular mass of this recombinant protein is approximately 26.5 kDa, although it may appear at around 28-40 kDa on SDS-PAGE due to glycosylation .
The recombinant protein is expressed with a C-terminal His-tag, which facilitates its purification using chromatographic techniques. The expression system used for producing this recombinant protein is the Sf9 insect cell line, which is derived from the fall armyworm, Spodoptera frugiperda. This system is commonly used for the production of recombinant proteins due to its ability to perform post-translational modifications, such as glycosylation, which are essential for the proper folding and function of many proteins.
Granzyme B is a key player in the immune response, particularly in the process of cytotoxicity mediated by cytotoxic T lymphocytes (CTLs) and NK cells. Upon recognition of a target cell, CTLs and NK cells release granules containing Granzyme B and perforin. Perforin forms pores in the target cell membrane, allowing Granzyme B to enter the cytoplasm of the target cell.
Once inside the target cell, Granzyme B cleaves and activates various substrates, including caspases, which are crucial for the execution of apoptosis. This leads to the rapid induction of programmed cell death, effectively eliminating the harmful target cell. Granzyme B can also degrade extracellular matrix proteins and alter inflammation if present in the extracellular milieu .
The role of Granzyme B in immune-mediated cytotoxicity makes it a critical factor in the body’s defense against infections and cancer. However, dysregulation of Granzyme B activity can contribute to various pathological conditions. For example, elevated levels of Granzyme B have been observed in acute coronary syndrome and acute myocardial infarction, indicating its potential involvement in cardiovascular diseases .
Additionally, Granzyme B has been implicated in autoimmune diseases, where its aberrant activity can lead to tissue damage. Understanding the regulation and function of Granzyme B is therefore important for developing therapeutic strategies for a range of diseases.
Recombinant Granzyme B is widely used in research to study its role in immune responses and apoptosis. It is also utilized in various assays to investigate the mechanisms of cytotoxicity and to screen for potential inhibitors that could modulate its activity. The availability of human recombinant Granzyme B produced in Sf9 cells provides a valuable tool for these studies, as it closely mimics the native protein in terms of structure and function.
