R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
Granzyme M (E7B4W) Rabbit mAb #37765
Filter:
- WB
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 25-30 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
Granzyme M (E7B4W) Rabbit mAb recognizes endogenous levels of total Granzyme M protein. This antibody does not cross-react with human Granzyme A, B, H, or K proteins.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala141 of human Granzyme M 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 M prefers to cleave after a Methionine or Leucine residue, and proteolyzes a restricted set of macromolecular substrates (4-7). Granzyme M is highly expressed in NK, NKT, γδ T cells, and in differentiated effector CD8+ T cells, suggesting a role for Granzyme M in both innate and adaptive immunity (4-11). After perforin-mediated entry into a target cell, various reports show Granzyme M can induce apoptosis and tumor cell death, stimulate LPS-mediated inflammation, or inhibit viral replication (4,11-15).
Granzyme M prefers to cleave after a Methionine or Leucine residue, and proteolyzes a restricted set of macromolecular substrates (4-7). Granzyme M is highly expressed in NK, NKT, γδ T cells, and in differentiated effector CD8+ T cells, suggesting a role for Granzyme M in both innate and adaptive immunity (4-11). After perforin-mediated entry into a target cell, various reports show Granzyme M can induce apoptosis and tumor cell death, stimulate LPS-mediated inflammation, or inhibit viral replication (4,11-15).
- 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.
- de Poot, S.A. and Bovenschen, N. (2014) Cell Death Differ 21, 359-68.
- Smyth, M.J. et al. (1993) J Immunol 151, 6195-205.
- Kelly, J.M. et al. (1996) Immunogenetics 44, 340-50.
- Mahrus, S. et al. (2004) J Biol Chem 279, 54275-82.
- Smyth, M.J. et al. (1995) Immunogenetics 42, 101-11.
- de Koning, P.J. et al. (2010) Mol Immunol 47, 903-11.
- Bade, B. et al. (2005) Int Immunol 17, 1419-28.
- van Domselaar, R. et al. (2013) Cell Death Differ 20, 419-29.
- Lu, H. et al. (2006) J Immunol 177, 1171-8.
- de Poot, S.A. et al. (2014) Cell Death Differ 21, 416-26.
- van Domselaar, R. et al. (2010) J Immunol 185, 7605-13.
- Anthony, D.A. et al. (2010) J Immunol 185, 1794-803.
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