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Brand: ProteoGenix

Recombinant Human SERPINA12, N-GST

Host species:
Escherichia coli (E.coli)
Origin species:
Human
Molecular weight:
37.43 kDa

$392.00

100ug + 392 loyalty points
Asn52–Arg143
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Recombinant Human SERPINA12, N-GST

Recombinant Human SERPINA12, N-GST

Product name Recombinant Human SERPINA12, N-GST
Origin species Human
Expression system Prokaryotic expression
Molecular weight 37.43 kDa
Buffer Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Delivery condition Dry Ice
Delivery lead time in business days 3-5 days if in stock; 3-5 weeks if production needed
Storage condition 4°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)
Brand ProteoGenix
Host species Escherichia coli (E.coli)
Fragment Type Asn52-Arg143
Aliases /Synonyms Vaspin, Visceral adipose-specific serpin, Visceral adipose tissue-derived serine protease inhibitor, OL-64, Serpin A12, SERPINA12
Reference ARO-P12901
Note For research use only.
Molecular Constructor
Asn52–Arg143

Introduction to Recombinant Human SERPINA12

Recombinant Human SERPINA12, also known as angiotensinogen (AGT), is a protein that plays a crucial role in the renin-angiotensin system (RAS). It is primarily produced in the liver and is the precursor of angiotensin, a hormone that regulates blood pressure and fluid balance in the body. Recombinant Human SERPINA12 is a genetically engineered version of the naturally occurring protein, produced through recombinant DNA technology. This technology allows for the production of large quantities of pure and highly specific proteins for use in various research and clinical applications.

Structure of Recombinant Human SERPINA12

Recombinant Human SERPINA12 is a 452-amino acid protein with a molecular weight of approximately 50 kDa. It is composed of three domains: the N-terminal domain, the central domain, and the C-terminal domain. The N-terminal domain is responsible for the binding of angiotensinogen to its receptor, while the central domain contains the cleavage site for the enzyme renin. The C-terminal domain is involved in the regulation of the protein’s activity.

The crystal structure of Recombinant Human SERPINA12 has been determined, revealing a compact globular structure with a high degree of flexibility. This flexibility allows for the protein to undergo conformational changes, which are necessary for its biological activity.

Activity of Recombinant Human SERPINA12

The primary function of Recombinant Human SERPINA12 is the production of angiotensin, a hormone that regulates blood pressure and fluid balance in the body. This is achieved through a multi-step process involving several enzymes, including renin, angiotensin-converting enzyme (ACE), and angiotensin-converting enzyme 2 (ACE2).

First, renin cleaves the N-terminal domain of Recombinant Human SERPINA12, producing angiotensin I. This is then converted to angiotensin II by ACE, which is a potent vasoconstrictor. Angiotensin II also stimulates the release of aldosterone, a hormone that regulates sodium and water balance in the body. On the other hand, ACE2 cleaves angiotensin II to produce angiotensin 1-7, which has vasodilatory and anti-inflammatory effects.

In addition to its role in the RAS, Recombinant Human SERPINA12 has been shown to have anti-inflammatory and antioxidant properties. It can also interact with other proteins, such as plasminogen and tissue-type plasminogen activator, to regulate blood clotting and fibrinolysis.

Applications of Recombinant Human SERPINA12

Recombinant Human SERPINA12 has a wide range of applications in research and clinical settings. Its ability to regulate blood pressure and fluid balance makes it a potential therapeutic target for hypertension and other cardiovascular diseases. It has also been implicated in the pathogenesis of preeclampsia, a potentially life-threatening condition during pregnancy, and Recombinant Human SERPINA12 may have a role in its diagnosis and treatment.

Furthermore, Recombinant Human SERPINA12 has been used in studies investigating the role of the RAS in various diseases, such as diabetes, kidney disease, and heart failure. It has also been studied in the context of inflammation and oxidative stress-related disorders.

In addition, Recombinant Human SERPINA12 is a valuable tool for protein-protein interaction studies and drug screening assays, as its interactions with other proteins are critical for its biological activity.

Conclusion

In summary, Recombinant Human SERPINA12 is a genetically engineered version of the naturally occurring protein angiotensinogen. It plays a crucial role in the RAS, regulating blood pressure and fluid balance in the body. Its structure, activity, and applications make it a valuable tool in various research and clinical settings, with potential therapeutic implications for cardiovascular

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