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Explore our products against Granzyme B available for RUO use. These antibodies can be used for applications such as Intracellular staining (flow cytometry) and Western blot against Human, Mouse and Rat targets. Our Granzyme B-specific antibodies were developed in Mouse and have Mouse (BALB/c) IgG1 κ and Mouse IgG2a isotypes. Our anti-Granzyme B-specific antibodies have been used in over 100 articles in peer-reviewed journals. Review over 10 figures from product development to select the best reagents for your needs.
Description: This gene encodes a member of the granzyme subfamily of proteins, part of the peptidase S1 family of serine proteases. The encoded preproprotein is secreted by natural killer (NK) cells and cytotoxic T lymphocytes (CTLs) and proteolytically processed to generate the active protease, which induces target cell apoptosis. This protein also processes cytokines and degrades extracellular matrix proteins, and these roles are implicated in chronic inflammation and wound healing. Expression of this gene may be elevated in human patients with cardiac fibrosis.
Description: This gene encodes a member of the granzyme subfamily of proteins, part of the peptidase S1 family of serine proteases. The encoded preproprotein is secreted by natural killer (NK) cells and cytotoxic T lymphocytes (CTLs) and proteolytically processed to generate the active protease, which induces target cell apoptosis. This protein also processes cytokines and degrades extracellular matrix proteins, and these roles are implicated in chronic inflammation and wound healing. Mice lacking a functional copy of this gene exhibit impaired immune cell-mediated cytolysis.
Function: Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse. It cleaves after Asp. Once delivered into the target cell, acts by catalyzing cleavage of gasdermin-E (GSDME), releasing the pore-forming moiety of GSDME, thereby triggering pyroptosis and target cell death. Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution. Cleaves caspase-3, -9 and -10 (CASP3, CASP9 and CASP10, respectively) to give rise to active enzymes mediating apoptosis. Cleaves and activates CASP7 in response to bacterial infection, promoting plasma membrane repair.
Molecular Function: Hydrolase, Protease, Serine protease
Subcellular location: Secreted, Cytolytic granule
kDa: 29
Function: Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse. It cleaves after Asp. Once delivered into the target cell, acts by catalyzing cleavage of gasdermin-E (GSDME), releasing the pore-forming moiety of GSDME, thereby triggering pyroptosis and target cell death (By similarity). Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution (By similarity). Cleaves caspase-3 and -9 (CASP3 and CASP9, respectively) to give rise to active enzymes mediating apoptosis. Cleaves and activates CASP7 in response to bacterial infection, promoting plasma membrane repair.
Molecular Function: Hydrolase, Protease, Serine protease
Subcellular location: Secreted, Cytolytic granule
kDa: 28
C11, CTLA-1 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 1-3, GZB, CCP1, Ctla1, Ctla-1, CCP-1/C11CTLA-1, Cytotoxic cell protease 1 (CCP1), CCP1
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
