Haematologic Technologies - Human Plasmin

HUMAN PLASMINOGEN The domain structure of human plasminogen is represented where: K1-K5 = the 5 kringle domains, B-CHAIN = catalytic domain of plasmin , and the arrows indicate the sites of proteolytic cleavage by plasmin, elastase, and plasminogen activators (PA'S).

PURCHASING AND PRODUCT INFORMATION

Catalog Number

HCPM-0140

~~MCPM-5140~~*

Description

Human Plasmin

Mouse Plasmin

Size

500 µg

50 µg

Formulation

50% Glycerol/Water (v/v)

Storage

-20^oC

Purity

>95% by SDS-PAGE

Activity Determination

Chromogenic assay

Shelf Life (properly stored)

12 months

Compliment fluorogenic substrate: HTI Catalog # SN-5

Sample Gel Information:

Gel: Novex 4-12% Bis-Tris

Load: Human Plasmin, 1 µg per lane

Buffer: MES

Standard: SeeBluePlus 2; Myosin (191 kDa), Phosphorylase B (97 kDa), BSA (64 kDa), Glutamic Dehydrogenase (51 kDa), Alcohol Dehydrogenase (39 kDa), Carbonic Anhydrase (28 kDa), Myoglobin Red (19 kDa), Lysozyme (14 kDa)

Sample publications referencing our Plasmin:

Zheng, H., et al., Arthritis Research & Therapy 2009, 11:R93. (Plasmin/Anti-plasmin assay)

This publication list is not all encompassing, and is only meant to provide limited examples of how Haematologic Technologies' products are used. We encourage you to search the literature for other examples pertinent to your experimentation, and to contact us with any technical questions.

U.S. Pricing

Product inquiry

SAMPLE DATA SHEET

ORDER NOW!

*Due to mouse plasma quality issues our mouse proteins are not being sold until further notice. At the present time we cannot give a completion date. Thank you.

Overview of Plasmin

Plasminogen (whether Glu-1, Lys-77 or Val-442) is converted to the active serine protease plasmin by hydrolysis of the Arg560-Val561 peptide bond yielding an NH₂-terminal heavy (A) chain and a COOH-terminal light (B) chain linked by 2 disulfide bonds (1-3). This conversion is catalyzed by a variety of physiological and pathological activators, including urinary type plasminogen activators, tissue type plasminogen activators, streptokinase, staphylokinase, kallikrein, factors IXa and XIIa. The COOH-terminal derived light chain (Mr=26,000) contains the catalytic triad (His42, Asp85 and Ser180) as well as the streptokinase binding site. The NH₂-terminal derived heavy chain ranges in molecular weight from 63,000 to 12,000 depending on the type of plasminogen from which it originated. In the absence of inhibitors, plasmin cleaves the amino-terminal Glu1 to Lys76 peptide from plasmin (plasminogen) to yield Lys-plasmin, which has a greater affinity for fibrin than the Glu form. The heavy chain of Lys-plasminogen contains 5 triple loop disulfide bridged regions of internal sequence homology known as kringles. Kringles 1-4 contain the ω-aminocarboxylic acid and fibrin binding sites.

Plasmin is a serine protease with broad specificity which, in addition to cleavage of fibrin, is capable of activation and/or degradation of compounds of the coagulation, kinin generation and complement systems. Although plasmin can be inhibited by a number of plasma protease inhibitors in vitro, regulation of plasmin in vivo is thought to occur mainly through its interaction with α2-antiplasmin, and to a lesser extent, α2-macroglobulin.

Human Lys-plasmin is prepared from homogeneous Glu-plasminogen using urokinase, as described by Robbins et al. (3). Plasmin is supplied in 50% (vol/vol) glycerol/H₂O and should be stored at -20°C. Activity is measured by chromogenic substrate assay and purity is judged by SDS gel electrophoresis.

Properties of Plasmin

Localization:

Plasma

Mode of action:

Enzyme involved in fibrinolysis

Molecular weight:

83,000 (lys-plasmin) (4)

Extinction coefficient:

1 %

1 c m, 280 nm

= 17.0 (4)

Isoelectric point:

6.7-8.3 (3)

Structure:

Two subunits, Mr=57,000 and Mr=26,000, disulfide linked, 5 kringle domains 22 disulfide bridges, NH₂-terminal lysine.

Percent carbohydrate:

Approximately 2% (2)