plasmin structure
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Common Name | plasmin | ||
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CAS Number | 9001-90-5 | Molecular Weight | N/A | |
Density | N/A | Boiling Point | N/A | |
Molecular Formula | C28H38N6O9S | Melting Point | N/A | |
MSDS | USA | Flash Point | N/A |
Use of plasminPlasmin is an important protease present in blood that degrades many plasma proteins, including fibrin clots. Plasmin can also act as a potent regulator of the immune process and can directly interact with various cell types, including monocytes, macrophages, and dendritic cells[1][2]. |
Name | N-[(4-Methylphenyl)sulfonyl]glycylprolyl-N-(4-nitrophenyl)lysinamide acetate (1:1) |
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Synonym | More Synonyms |
Description | Plasmin is an important protease present in blood that degrades many plasma proteins, including fibrin clots. Plasmin can also act as a potent regulator of the immune process and can directly interact with various cell types, including monocytes, macrophages, and dendritic cells[1][2]. |
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Related Catalog | |
In Vitro | Plasmin (20 μg/mL, 24 h) 在小鼠皮质管上皮细胞系 (MCT) 中可以激活 PAR-1,强烈诱导 ERK 磷酸化,降解 e -钙粘蛋白[1]。 |
References |
Molecular Formula | C28H38N6O9S |
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Appearance of Characters | lyophilized powder |
Storage condition | −20°C |
Hazard Codes | B,Xn |
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Risk Phrases | 36/37/38-42 |
Safety Phrases | 2-22-24-26-36/37-45-24/25 |
RIDADR | NONH for all modes of transport |
WGK Germany | 3 |
Plasmin-mediated activation of pandemic H1N1 influenza virus hemagglutinin is independent of the viral neuraminidase.
J. Virol. 87(9) , 5161-9, (2013) Influenza virus is well recognized to modulate host tropism and pathogenesis based on mutations in the proteolytic cleavage site of the viral hemagglutinin (HA), which activates HA and exposes the fus... |
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Effects of black cohosh on the plasminogen activator system in vascular smooth muscle cells.
Maturitas 76(1) , 75-80, (2013) The rhizome of the Cimicifuga racemosa plant (commonly known as black cohosh) has been used for menopausal complaints. Studies regarding the cardiovascular effects of black cohosh are lacking. We inve... |
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Functional characterization of a slow and tight-binding inhibitor of plasmin isolated from Russell's viper venom.
Biochim. Biophys. Acta 1840(1) , 153-9, (2014) Snake venoms are rich in Kunitz-type protease inhibitors that may have therapeutic applications. However, apart from trypsin or chymotrypsin inhibition, the functions of most of these inhibitors have ... |
MFCD00131921 |
Lysinamide, N-[(4-methylphenyl)sulfonyl]glycylprolyl-N-(4-nitrophenyl)-, acetate (1:1) |
N-[(4-Methylphenyl)sulfonyl]glycylprolyl-N-(4-nitrophenyl)lysinamide acetate (1:1) |