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SerpinA8 / Angiotensinogen / AGT Antibody, Mouse MAb

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Human AGT Antibody Product Information
Immunogen:Recombinant Human SerpinA8 protein (Catalog#10994-H08H)
Clone ID:6A10B4B5
Ig Type:Mouse IgG2b
Formulation:0.2 μm filtered solution in PBS with 5% trehalose
Preparation:This antibody was produced from a hybridoma resulting from the fusion of a mouse myeloma with B cells obtained from a mouse immunized with purified, recombinant Human SerpinA8 / angiotensinogen (rh SerpinA8; Catalog#10994-H08H; NP_000020.1; Met 1-Ala 485). The IgG fraction of the cell culture supernatant was purified by Protein A affinity chromatography.
Human AGT Antibody Usage Guide
Specificity:Human SerpinA8 / Angiotensinogen
No cross-reactivity in WB and ELISA with
Human SerpinA1 / A1AT
Human SerpinA3 / SERPINA3 / AACT
Human SerpinA5 / Protein C inhibitor
Human SerpinD1 / HC2
Human SerpinF2 / SERPINF2
Human SerpinG1 / C1IN
Human SerpinI1 / Protease inhibitor 12
Human SerpinC1 /SERPINC1/ Antithrombin-III
Human cell lysate (293 cell line)

ELISA: 0.5-1 μg/mL

This antibody can be used at 0.5-1 μg/mL with the appropriate secondary reagents to detect Human SerpinA8. The detection limit for Human SerpinA8 is 0.16 ng/well.

Storage:This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free.
Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.
Other AGT Antibody Products
Angiotensinogen/SerpinA8 Background

Angiotensinogen, also known as AGT and SerpinA8, is a member of the serpin family. It is an α-2-globulin that is produced constitutively and released into the circulation mainly by the liver. Angiotensinogen is a essential component of the renin-angiotensin system (RAS) and a potent regulator of blood pressure. Angiotensinogen can be schematically considered to consist of a combination of an angiotensin I (Ang I) function, located at the N-terminal end, and the presence of a serpin (serine protease inhibitor) structure at the opposite end. Angiotensinogen is cleaved into three chains: Angiotensin-1 (Ang I), Angiotensin-2 (Ang II), and Angiotensin-3 (Ang III). Angiotensin-1 is a substrate of ACE (angiotensin converting enzyme) that removes a dipeptide to yield the physiologically active peptide angiotensin-2. Angiotensin-1 and angiotensin-2 can be further processed to generate angiotensin-3, angiotensin-4. Angiotensin 1-7 is cleaved from angiotensin-2 by ACE2. Angiotensin-2 acts directly on vascular smooth muscle as a potent vasoconstrictor, affects cardiac contractility and heart rate through its action on the sympathetic nervous system. Defects in AGT are associated with susceptibility to essential hypertension and renal tubular dysgenesis (RTD). Several serpins (antithrombin, maspin, pigment epithelial-derived factor, and kallistatin) have been recently shown to exert an antiangiogenic activity, suggesting a common mechanism of endothelial cell proliferation and migration. Angiotensinogen/AGT and its renin-cleaved product, des(Ang I)AGT, are also angiogenesis inhibitors, both in vitro and in vivo at concentrations within the range of those observed in plasma. The Angiotensinogen products, that is angiotensin II and possibly angiotensin II-related products, have been found to act locally in modulating adipose tissue growth in an autocrine/paracrine manner. The transient or chronic overexpression of angiotensinogen in adipose tissue favors lipogenesis in adipocytes and leads to a 'vicious' circle whereby adipose tissue development is further increased.

Human Angiotensinogen/SerpinA8 References
  • Ailhaud G, et al. (2002) Angiotensinogen, adipocyte differentiation and fat mass enlargement. Curr Opin Clin Nutr Metab Care. 5(4): 385-9.
  • Corvol P, et al. (2003) Inhibition of angiogenesis: a new function for angiotensinogen and des(angiotensin I)angiotensinogen. Curr Hypertens Rep. 5(2): 149-54.
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