Technical Data
M2414-01
Mast Cell Chymase (Biotin)
Description:
Mast cell chymase (EC 3.4.21.39), a member of the granzyme subfamily of the S1 family of peptidases, cleaves chymase C-terminal to Phenylalanine, Tyrosine, Tryptophan, and Leucine residues (in order of preference). Chymase is stored in mast cell granules within the cell and is the major secreated mast cell protease. Secreated mast cell chymase is believed to be involved in extracellular matrix degradation, vasoactive peptide generation, and regulation of gland secreation.

Applications:
Suitable for use in Immunohistochemistry and Immunocytochemistry. Not recommended for Western Blot. Other applications have not been tested.

Recommended Dilutions:
Immunohistochemistry/Immunocytochemistry: 0.5-1ug/ml; For optimal results, tissues or cytospin preparations should be fixed in Carnoy’s Fluid (60% ethanol, 30% chloroform, 10% glacial acetic acid). Not recommended for use on formaldehyde fixed tissue.
Optimal dilutions to be determined by the researcher.

Source:
Culture Supernatant

Positive Control:
Lung, Heart, Skin, Placenta

Storage and Stability:
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
TypeIsotypeCloneGrade
MabIgG1,k2Q1506Highly Purified
SizeStorageShippingSourceHost
100ug-20°CBlue IceHumanMouse
Concentration:
~1mg/ml
Immunogen:
Chymase purified from human skin.
Purity:
Purified by ammonium sulfate precipitation and DEAE-Sephacyl chromatography.
Form
Supplied as a liquid in PBS, pH 7.1, 15mg/ml BSA, 0.1% sodium azide. Labeled with Biotin.
Specificity:
Recognizes human mast cell chymase.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Horny, H-P., et al., J. Clin. Pathol. 56: 103-106 (2003). 2. Beil, W., et al., Pathobiology 70: 303-313 (2002). 3. Beil, W. and Pammer, J., Histochemistry and Cell Biology 116: 483-493 (2001). 4. McKerrow, J., et al., Molecular Medicine 6: 450-460 (2000). 5. Terada, T. and Matsunaga, Y., J. Hepatology 33: 961-966 (2000). 6. Vinke, J., et al., Eur. Respir. J. 13: 797-803 (1999). 7. Buckley, M., et al., J. Pathol. 186: 67-74 (1998). 8. KleinJan, A., et al., Allergy 51: 614-620 (1996). 9. Irani, A., et al., Clin. Exp. Allergy 20: 53-58 (1990). 10. Irani, A., et al., J. Allergy Clin. Immunol. 86: 34-39 (1990). 11. Schechter, N., et al., J. Immunol. 140: 2652-2661 (1990). 12. Craig, S. and Schwartz, L., Lab. Invest. 63: 581-585 (1990). 13. Craig, S., et al., Lab. Invest. 60: 147-157 (1989). 14. Irani, A., et al., J. Histochem. Cytochem. 37: 1509-1515 (1989). 15. Furitsu, T., et al., PNAS USA 86: 10,039-10,043 (1989). 16. Craig, S., et al., Lab. Invest. 58: 682-691 (1988). 17. Castells, M., et al., J. Immunol. 138: 2184-2189 (1987). 18. Irani, A., et al., J. Immunol. 138: 4381-4386 (1987). 19. Schwartz, L., et al., J. Immunol. 138: 2611-2615 (1987). 20. Irani, A., et al., PNAS USA 83: 4464-4468 (1986).