Granzyme H (E3H7W) Rabbit mAb (Alexa Fluor® 488 Conjugate) #23455
- F
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | |
| Source/Isotype | Rabbit IgG |
Application Key:
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Description
Product Usage Information
| Application | Dilution |
|---|---|
| Flow Cytometry (Fixed/Permeabilized) | 1:50 |
Storage
Protocol
Specificity / Sensitivity
Granzyme H (E3H7W) Rabbit mAb (Alexa Fluor® 488 Conjugate) recognizes endogenous levels of total Granzyme H protein. This antibody does not cross-react with human Granzyme A, B, or K proteins. This antibody does not cross-react with mouse Granzyme B proteins.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gln195 of human Granzyme H protein.
Background
Granzymes are a family of serine proteases expressed by cytotoxic T lymphocytes and natural killer (NK) cells and are key components of immune responses to pathogens and transformed cells (1). Granzymes are synthesized as zymogens and are processed into mature enzymes by cleavage of a leader sequence. They are released by exocytosis in lysosome-like granules containing perforin, a membrane pore-forming protein. Granzyme B has the strongest apoptotic activity of all the granzymes as a result of its caspase-like ability to cleave substrates at aspartic acid residues thereby activating procaspases directly and cleaving downstream caspase substrates (2,3).
Granzyme H has chymotrypsin-like thioester activity with a preference for hydrophobic, aromatic amino acid residues, such as phenylalanine, tyrosine, or methionine, at the P1 site (4,5). Granzyme H is predominantly expressed at high levels in NK cells, but not in T lymphocytes, and has also been described in mast cells (6-8). After perforin-mediated entry into a target cell, Granzyme H induces many hallmarks of programmed cell death, such as mitochondrial depolarization, generation of reactive oxygen species, DNA degradation, and chromatin condensation (9,10).
- Trapani, J.A. (2001) Genome Biol. 2, REVIEWS 3014.
- Lord, S.J. et al. (2003) Immunol. Rev. 193, 31-8.
- Trapani, J.A. and Sutton, V.R. (2003) Curr. Opin. Immunol. 15, 533-43.
- Edwards, K.M. et al. (1999) J Biol Chem 274, 30468-73.
- Mahrus, S. and Craik, C.S. (2005) Chem Biol 12, 567-77.
- Sedelies, K.A. et al. (2004) J Biol Chem 279, 26581-7.
- Bade, B. et al. (2005) Int Immunol 17, 1419-28.
- Rönnberg, E. et al. (2014) Int Arch Allergy Immunol 165, 68-74.
- Fellows, E. et al. (2007) Blood 110, 544-52.
- Hou, Q. et al. (2008) Mol Immunol 45, 1044-55.
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