R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
Tryptase (E9R8A) Rabbit mAb #51550
Filter:
- WB
- IF
- F
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 25-40 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IF-Immunofluorescence
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunofluorescence (Immunocytochemistry) | 1:800 - 1:1600 |
| Flow Cytometry (Fixed/Permeabilized) | 1:200 - 1:400 |
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
Tryptase (E9R8A) Rabbit mAb recognizes endogenous levels of total Tryptase protein.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with recombinant protein specific to human Tryptase protein.
Background
Tryptase is the most abundant neutral serine protease expressed in the secretory granules of all human mast cells (1). Tryptase is secreted upon the coupled activation-degranulation response of mast cells in peripheral tissues to physical factors such as trauma, toxins, venoms, endogenous mediators, and immune mechanisms (IgE-dependent and IgE-independent) (2). Tryptase has distinct enzymatic functions that depend on the monomeric or homotetrameric state of this protein, the pH of the environment, and the presence or absence of heparin (3-5). Tryptase has the ability to cleave extracellular substrates such as vasoactive intestinal peptides (6), calcitonin gene-related peptides (7), fibronectins (8), fibrinogens (3), and kininogens (9). Tryptase is also a potent growth factor for epithelial cells, airway smooth muscle cells, and fibroblasts (10-13).
- Vanderslice, P. et al. (1990) Proc Natl Acad Sci U S A 87, 3811-5.
- Krishnaswamy, G. et al. (2001) Front Biosci 6, D1109-27.
- Fukuoka, Y. and Schwartz, L.B. (2007) Int Immunopharmacol 7, 1900-8.
- Ren, S. et al. (1998) J Immunol 160, 4561-9.
- Sakai, K. et al. (1996) J Clin Invest 97, 988-95.
- Tam, E.K. and Caughey, G.H. (1990) Am J Respir Cell Mol Biol 3, 27-32.
- Walls, A.F. et al. (1992) Biochem Pharmacol 43, 1243-8.
- Lohi, J. et al. (1992) J Cell Biochem 50, 337-49.
- Walls, A.F. et al. (1992) Biochem Soc Trans 20, 260S.
- Cairns, J.A. and Walls, A.F. (1996) J Immunol 156, 275-83.
- Ruoss, S.J. et al. (1991) J Clin Invest 88, 493-9.
- Brown, J.K. et al. (1995) Am J Respir Cell Mol Biol 13, 227-36.
- Gruber, B.L. et al. (1997) J Immunol 158, 2310-7.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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