CHYMASE

Modify Date: 2024-01-06 19:36:43

CHYMASE Structure
CHYMASE structure
Common Name CHYMASE
CAS Number 97501-92-3 Molecular Weight N/A
Density N/A Boiling Point N/A
Molecular Formula N/A Melting Point N/A
MSDS USA Flash Point N/A

 Use of CHYMASE


Chymase is a protein-digester enzyme found primarily in mast cells (MC), fibroblasts, and vascular endothelial cells. Chymase is released into the extracellular stroma in the context of inflammatory signals, tissue injury and cellular stress. Chymase is also involved in angiotensin II (Ang II) production, which is used in cardiovascular disease studies[1].

 Names

Name CHYMASE

 CHYMASE Biological Activity

Description Chymase is a protein-digester enzyme found primarily in mast cells (MC), fibroblasts, and vascular endothelial cells. Chymase is released into the extracellular stroma in the context of inflammatory signals, tissue injury and cellular stress. Chymase is also involved in angiotensin II (Ang II) production, which is used in cardiovascular disease studies[1].
Related Catalog
References

[1]. Ahmad S, et al. Chymase inhibitors for the treatment of cardiac diseases: a patent review (2010-2018). Expert Opin Ther Pat. 2018 Nov;28(11):755-764.  

 Chemical & Physical Properties

Storage condition −20°C

 Safety Information

Personal Protective Equipment Eyeshields;Gloves;half-mask respirator (US);multi-purpose combination respirator cartridge (US)
Hazard Codes B
RIDADR NONH for all modes of transport
WGK Germany 1

 Articles46

More Articles
Primacy of angiotensin converting enzyme in angiotensin-(1-12) metabolism.

Am. J. Physiol. Heart Circ. Physiol. 305(5) , H644-50, (2013)

Angiotensin-(1-12) [ANG-(1-12)], a new member of the renin-angiotensin system, is recognized as a renin independent precursor for ANG II. However, the processing of ANG-(1-12) in the circulation in vi...

Cathepsin C is a tissue-specific regulator of squamous carcinogenesis.

Genes Dev. 27(19) , 2086-98, (2013)

Serine and cysteine cathepsin (Cts) proteases are an important class of intracellular and pericellular enzymes mediating multiple aspects of tumor development. Emblematic of these is CtsB, reported to...

Heparanase-mediated cleavage of macromolecular heparin accelerates release of granular components of mast cells from extracellular matrices.

Biochem. J. 458(2) , 291-9, (2014)

Heparanase cleaves macromolecular heparin in the secretory granules of connective tissue-type mast cells. We investigated roles of the cleavage under a microenvironment mimicking where the mast cells ...