Recombinant Human PLAU Protein, N-His

Reference: YHB88301
Product nameRecombinant Human PLAU Protein, N-His
Origin speciesHuman
Expression systemEukaryotic expression
Molecular weight30.00 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeThr186-Leu431
Aliases /SynonymsPLAU, uPA, U-plasminogen activator, Urokinase-type plasminogen activator
ReferenceYHB88301
NoteFor research use only.

Description of Recombinant Human PLAU Protein, N-His

Recombinant Human PLAU Protein: Structure, Activity, and Applications

Recombinant human PLAU protein, also known as urokinase-type plasminogen activator (uPA), is a key enzyme involved in the regulation of the fibrinolytic system. It is a serine protease that converts plasminogen to plasmin, which plays a crucial role in the breakdown of blood clots and extracellular matrix components. In this article, we will discuss the structure, activity, and applications of recombinant human PLAU protein.

Structure of Recombinant Human PLAU Protein

Recombinant human PLAU protein is a single-chain glycoprotein with a molecular weight of approximately 54 kDa. It is composed of three distinct domains: the N-terminal domain, the kringle domain, and the catalytic domain. The N-terminal domain is responsible for binding to its receptor, urokinase plasminogen activator receptor (uPAR), while the kringle domain is involved in the regulation of plasminogen activation. The catalytic domain contains the active site and is responsible for the proteolytic activity of the protein.

The structure of recombinant human PLAU protein is highly conserved among different species, with a sequence identity of 60% between human and mouse PLAU protein. It also shares a high degree of structural similarity with other members of the plasminogen activator family, such as tissue-type plasminogen activator (tPA) and streptokinase.

Activity of Recombinant Human PLAU Protein

Recombinant human PLAU protein is a potent activator of plasminogen, converting it to the active enzyme plasmin. This activity is crucial for the dissolution of blood clots and the remodeling of the extracellular matrix. PLAU is also involved in the activation of other proteases, such as matrix metalloproteinases, which play a role in tissue remodeling and wound healing.

The activity of recombinant human PLAU protein is tightly regulated by its inhibitor, plasminogen activator inhibitor-1 (PAI-1). PAI-1 binds to PLAU and inhibits its activity, preventing excessive fibrinolysis and maintaining the balance between clot formation and dissolution.

Applications of Recombinant Human PLAU Protein

Recombinant human PLAU protein has a wide range of applications in both research and clinical settings. One of its main uses is in the treatment of thrombotic disorders, such as pulmonary embolism and deep vein thrombosis. PLAU is also used in the management of acute myocardial infarction, where it is administered as a thrombolytic agent to dissolve blood clots in the coronary arteries.

In addition to its role in fibrinolysis, recombinant human PLAU protein has been implicated in various other physiological processes, including cell migration, angiogenesis, and tumor growth. Its overexpression has been linked to the progression of various cancers, making it a potential target for cancer therapy.

Recombinant human PLAU protein is also widely used in research as a tool for studying the fibrinolytic system. It is used in in vitro assays to measure plasminogen activation and fibrinolysis and in animal studies to investigate the role of PLAU in various physiological and pathological processes.

In Conclusion

Recombinant human PLAU protein is a crucial enzyme involved in the regulation of the fibrinolytic system. Its structure, activity, and applications have been extensively studied, and it has emerged as a promising therapeutic target for various diseases. Further research on this protein and its interactions with other components of the fibrinolytic system may lead to the development of novel treatments for thrombotic disorders and cancer.

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