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Native Chicken Plasmin protein is a Full Length protein, expressed in Native, with >95% purity and suitable for SDS-PAGE.

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Key facts

Purity

>95% SDS-PAGE

Expression system

Native

Tags

Tag free

Applications

SDS-PAGE

Biologically active

No

Reactivity data

Application

SDS-PAGE

Reactivity

Reacts

Dilution info

-

Notes

-

Associated Products

Select an associated product type

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Alternative names

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Native Chicken Plasmin protein is a Full Length protein, expressed in Native, with >95% purity and suitable for SDS-PAGE.

Key facts

Purity

>95% SDS-PAGE

Expression system

Native

Applications

SDS-PAGE

Animal free

No

Concentration
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Storage buffer

pH: 7.4
Constituents: 2.38% HEPES, 0.58% Sodium chloride

Sequence info

Amino acid sequence

Accession

Protein length

Full Length

Nature

Native

Specifications

Form

Liquid

Additional notes

Prepared from plasminogen by activation with immobilized Human uPA.

Storage

Shipped at conditions

Dry Ice

Appropriate short-term storage conditions

-80°C

Appropriate long-term storage conditions

-80°C

Aliquoting information

Upon delivery aliquot

Storage information

Avoid freeze / thaw cycle

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Plasmin a serine protease enzyme with a mass of approximately 79 kDa is an important player in the fibrinolytic system. Commonly referred to by alternate names like profibrinolysin or fibrinolysin it is mainly expressed in the liver and circulates in the blood as an inactive zymogen called plasminogen. Plasminogen is activated to plasmin through the action of activators such as tissue plasminogen activator (tPA) and urokinase (uPA). The activation to plasmin involves a cleavage at specific peptide bonds which exposes the active site that allows it to function as a protease.

Biological function summary

The enzyme plasmin degrades fibrin in blood clots a critical function in the process of clot resolution. It belongs to the family of serine proteases and does not form part of a larger protein complex. The activity of plasmin is modulated by inhibitors like alpha-2-antiplasmin which bind to plasmin and prevent excessive degradation of fibrin. Bovine plasmin shares similar functions and serves as a model for studying human plasmin activity. Researchers often measure plasmin activity through specific assays to understand changes in fibrinolytic activity within the body.

Pathways

Plasmin plays an integral role in the fibrinolytic pathway and is also involved in tissue remodeling and wound healing. The fibrinolytic pathway centers on the balance of plasminogen activation and inhibition which directly influences thrombolysis. Proteins such as tPA and uPA facilitate the conversion of plasminogen to plasmin and are tightly regulated to ensure proper physiological function. In the context of wound healing plasmin helps activate matrix metalloproteases leading to extracellular matrix breakdown and cell migration.

Associated diseases and disorders

The regulation of plasmin is closely associated with pathological conditions such as thrombosis and liver disease. An overactive plasmin system can result in conditions like excessive bleeding or hemorrhage while inadequate plasmin activity may lead to thrombosis due to impaired clot breakdown. The interaction between plasmin and plasmin inhibitors like alpha-2-antiplasmin is critical in diseases such as liver cirrhosis where imbalances in fibrinolysis can have significant clinical outcomes. Understanding these interactions helps in developing therapeutic strategies to modulate plasmin activity in various disorders.

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