Kallikrein

Modify Date: 2024-01-11 09:39:10

Kallikrein Structure
Kallikrein structure
Common Name Kallikrein
CAS Number 9001-01-8 Molecular Weight 283.277
Density 1.3±0.1 g/cm3 Boiling Point 471.1±45.0 °C at 760 mmHg
Molecular Formula C13H17NO6 Melting Point N/A
MSDS USA Flash Point 238.7±28.7 °C

 Use of Kallikrein


Kallikrein is capable of forming the kallikrenase kalinin system (KKS) in plasma and tissues, producing bradykinin and kalin peptides, respectively[1].

 Names

Name Kallikrein
Synonym More Synonyms

 Kallikrein Biological Activity

Description Kallikrein is capable of forming the kallikrenase kalinin system (KKS) in plasma and tissues, producing bradykinin and kalin peptides, respectively[1].
Related Catalog
References

[1]. Campbell DJ, et al. The kallikrein-kinin system in humans. Clin Exp Pharmacol Physiol. 2001 Dec;28(12):1060-5.  

 Chemical & Physical Properties

Density 1.3±0.1 g/cm3
Boiling Point 471.1±45.0 °C at 760 mmHg
Molecular Formula C13H17NO6
Molecular Weight 283.277
Flash Point 238.7±28.7 °C
Exact Mass 283.105591
LogP 2.10
Appearance of Characters lyophilized powder
Vapour Pressure 0.0±1.2 mmHg at 25°C
Index of Refraction 1.543
Storage condition 2-8°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 3
RTECS NZ2017050

 Articles68

More Articles
BMPR2 is required for postimplantation uterine function and pregnancy maintenance.

J. Clin. Invest. 123(6) , 2539-50, (2013)

Abnormalities in cell-cell communication and growth factor signaling pathways can lead to defects in maternal-fetal interactions during pregnancy, including immunologic rejection of the fetal/placenta...

The structure of human microplasmin in complex with textilinin-1, an aprotinin-like inhibitor from the Australian brown snake.

PLoS ONE 8(1) , e54104, (2013)

Textilinin-1 is a Kunitz-type serine protease inhibitor from Australian brown snake venom. Its ability to potently and specifically inhibit human plasmin (K(i) = 0.44 nM) makes it a potential therapeu...

Neutron and X-ray crystallographic analysis of Achromobacter protease I at pD 8.0: protonation states and hydration structure in the free-form.

Biochim. Biophys. Acta 1834(8) , 1642-7, (2013)

The structure of the free-form of Achromobacter protease I (API) at pD 8.0 was refined by simultaneous use of single crystal X-ray and neutron diffraction data sets to investigate the protonation stat...

 Synonyms

MFCD00131428
5-(Ethoxycarbonyl)-4-(2-ethoxy-2-oxoethyl)-2-methyl-1H-pyrrole-3-carboxylic acid
1H-Pyrrole-2,4-dicarboxylic acid, 3-(2-ethoxy-2-oxoethyl)-5-methyl-, 2-ethyl ester
kallidinogenase
The content on this webpage is sourced from various professional data sources. If you have any questions or concerns regarding the content, please feel free to contact service1@chemsrc.com.