Angiotensinogen Recombinant Protein | AGT recombinant protein

Recombinant Human Angiotensinogen

Cat. Num. AAA954800

• Gene Names: AGT; ANHU; SERPINA8
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Angiotensinogen; Recombinant Human Angiotensinogen; Serpin A8; AGT recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 34-485, Full length protein
• Sequence: DRVYIHPFHLVIHNESTCEQLAKANAGKPKDPTFIPAPIQAKTSPVDEKALQDQLVLVAAKLDTEDKLRAAMVGMLANFLGFRIYGMHSELWGVVHGATVLSPTAVFGTLASLYLGALDHTADRLQAILGVPWKDKNCTSRLDAHKVLSALQAVQGLLVAQGRADSQAQLLLSTVVGVFTAPGLHLKQPFVQGLALYTPVVLPRSLDFTELDVAAEKIDRFMQAVTGWKTGCSLMGASVDSTLAFNTYVHFQGKMKGFSLLAEPQEFWVDNSTSVSVPMLSGMGTFQHWSDIQDNFSVTQVPFTESACLLLIQPHYASDLDKVEGLTFQQNSLNWMKKLSPRTIHLTMPQLVLQGSYDLQDLLAQAELPAILHTELNLQKLSNDRIRVGEVLNSIFFELEADEREPTESTQQLNKPEVLEVTLNRPFLFAVYDQSATALHFLGRVANPLSTA
• Sequence Length: 452

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-Page

Related Product Information for AGT recombinant protein

Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis. 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, and alters renal sodium and water absorption through its ability to stimulate the zona glomerulosa cells of the adrenal cortex to synthesize and secrete aldosterone. Angiotensin-3: stimulates aldosterone release. Angiotensin 1-7: is a ligand for the G-protein coupled receptor MAS1. Has vasodilator and antidiuretic effects. Has an antithrombotic effect that involves MAS1-mediated release of nitric oxide from platelets.

Product Categories/Family for AGT recombinant protein

Cardiovascular

References

Primary structure of human preangiotensinogen deduced from the cloned cDNA sequence.Kageyama R., Ohkubo H., Nakanishi S.Biochemistry 23:3603-3609(1984) Structure of human angiotensinogen gene.Gaillard I., Clauser E., Corvol P.DNA 8:87-99(1989) Structure and expression of the human angiotensinogen gene. Identification of a unique and highly active promoter.Fukamizu A., Takahashi S., Seo M.S., Tada M., Tanimoto K., Uehara S., Murakami K.J. Biol. Chem. 265:7576-7582(1990) Molecular cloning of human angiotensinogen cDNA and evidence for the presence of its mRNA in rat heart.Kunapuli S.P., Kumar A.Circ. Res. 60:786-790(1987) Tissue specific hormonal regulation of the rat angiotensinogen gene expression.Kunapuli S.P., Benedict C.R., Kumar A.Arch. Biochem. Biophys. 254:642-646(1987) The amino terminal amino acid sequence of human angiotensinogen.Tewksbury D.A., Dart R.A., Travis J.Biochem. Biophys. Res. Commun. 99:1311-1315(1981) Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma.Oxvig C., Haaning J., Kristensen L., Wagner J.M., Rubin I., Stigbrand T., Gleich G.J., Sottrup-Jensen L.J. Biol. Chem. 270:13645-13651(1995) Enzymatic degradation and electrophoresis of human angiotensin I.Arakawa K., Minohara A., Yamada J., Nakamura M.Biochim. Biophys. Acta 168:106-112(1968) Processing of rat and human angiotensinogen precursors by microsomal membranes.Campbell D.J., Bouhnik J., Coezy E., Menard J., Corvol P.Mol. Cell. Endocrinol. 43:31-40(1985) Angiotensin III (DES-Aspartic Acid-1) -Angiotensin II. Evidence and speculation for its role as an important agonist in the renin - angiotensin system.Goodfriend T.L., Peach M.J.Circ. Res. 36:38-48(1975) The renin-angiotensin-aldosterone system a specific target for hypertension management.Weir M.R., Dzau V.J.Am. J. Hypertens. 12:205S-213S(1999) A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9.Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M., Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R., Breitbart R.E., Acton S.Circ. Res. 87:E1-E9(2000) Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase.Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.J. Biol. Chem. 277:14838-14843(2002) Evaluation of angiotensin-converting enzyme (ACE) , its homologue ACE2 and neprilysin in angiotensin peptide metabolism.Rice G.I., Thomas D.A., Grant P.J., Turner A.J., Hooper N.M.Biochem. J. 383:45-51(2004) Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.J. Proteome Res. 4:2070-2080(2005) Mass-spectrometric identification of a novel angiotensin peptide in human plasma.Jankowski V., Vanholder R., van der Giet M., Tolle M., Karadogan S., Gobom J., Furkert J., Oksche A., Krause E., Tran T.N., Tepel M., Schuchardt M., Schluter H., Wiedon A., Beyermann M., Bader M., Todiras M., Zidek W., Jankowski J.Arterioscler. Thromb. Vasc. Biol. 27:297-302(2007) Renin-angiotensin system revisited.Fyhrquist F., Saijonmaa O.J. Intern. Med. 264:224-236(2008) Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.J. Proteome Res. 8:651-661(2009) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) The octapeptide angiotensin II adopts a well-defined structure in a phospholipid environment.Carpenter K.A., Wilkes B.C., Schiller P.W.Eur. J. Biochem. 251:448-453(1998) Comparison of the solution structures of angiotensin I & II. Implication for structure-function relationship.Spyroulias G.A., Nikolakopoulou P., Tzakos A., Gerothanassis I.P., Magafa V., Manessi-Zoupa E., Cordopatis P.Eur. J. Biochem. 270:2163-2173(2003) A redox switch in angiotensinogen modulates angiotensin release.Zhou A., Carrell R.W., Murphy M.P., Wei Z., Yan Y., Stanley P.L., Stein P.E., Broughton Pipkin F., Read R.J.Nature 468:108-111(2010) Molecular basis of human hypertension role of angiotensinogen.Jeunemaitre X., Soubrier F., Kotelevtsev Y.V., Lifton R.P., Williams C.S., Charru A., Hunt S.C., Hopkins P.N., Williams R.R., Lalouel J.-M., Corvol P.Cell 71:169-180(1992) A molecular variant of angiotensinogen associated with preeclampsia.Ward K., Hata A., Jeunemaitre X., Helin C., Nelson L., Namikawa C., Farrington P.F., Ogasawara M., Suzumori K., Tomoda S., Berrebi S., Sasaki M., Corvol P., Lifton R.P., Lalouel J.-M.Nat. Genet. 4:59-61(1993) Detection and characterization of new mutations in the human angiotensinogen gene (AGT) .Hixson J.E., Powers P.K.Hum. Genet. 96:110-112(1995) A mutation of angiotensinogen in a patient with preeclampsia leads to altered kinetics of the renin-angiotensin system.Inoue I., Rohrwasser A., Helin C., Jeunemaitre X., Crain P., Bohlender J., Lifton R.P., Corvol P., Ward K., Lalouel J.-M.J. Biol. Chem. 270:11430-11436(1995) The natural mutation Y248C of human angiotensinogen leads to abnormal glycosylation and altered immunological recognition of the protein.Gimenez-Roqueplo A.P., Leconte I., Cohen P., Simon D., Guyene T.T., Celerier J., Pau B., Corvol P., Clauser E., Jeunemaitre X.J. Biol. Chem. 271:9838-9844(1996) Mutations in genes in the renin-angiotensin system are associated with autosomal recessive renal tubular dysgenesis.Gribouval O., Gonzales M., Neuhaus T., Aziza J., Bieth E., Laurent N., Bouton J.M., Feuillet F., Makni S., Ben Amar H., Laube G., Delezoide A.-L., Bouvier R., Dijoud F., Ollagnon-Roman E., Roume J., Joubert M., Antignac C., Gubler M.-C.Nat. Genet. 37:964-968(2005)

NCBI and Uniprot Product Information

• NCBI GeneID: 183
• UniProt Accession #: P01019; Q16358; Q16359; Q96F91
• Molecular Weight: 57.91kD
• NCBI Official Synonym Full Names: angiotensinogen
• NCBI Official Symbol: AGT
• NCBI Official Synonym Symbols: ANHU; SERPINA8
• UniProt Protein Name: Angiotensinogen
• Protein Family: Angiotensinogen
• UniProt Gene Name: AGT
• UniProt Synonym Gene Names: SERPINA8; Ang I; Ang II; Ang III; Ang IV
• UniProt Entry Name: ANGT_HUMAN

NCBI Description

The protein encoded by this gene, pre-angiotensinogen or angiotensinogen precursor, is expressed in the liver and is cleaved by the enzyme renin in response to lowered blood pressure. The resulting product, angiotensin I, is then cleaved by angiotensin converting enzyme (ACE) to generate the physiologically active enzyme angiotensin II. The protein is involved in maintaining blood pressure and in the pathogenesis of essential hypertension and preeclampsia. Mutations in this gene are associated with susceptibility to essential hypertension, and can cause renal tubular dysgenesis, a severe disorder of renal tubular development. Defects in this gene have also been associated with non-familial structural atrial fibrillation, and inflammatory bowel disease. [provided by RefSeq, Jul 2008]

Uniprot Description

angiotensin: Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis. In response to lowered blood pressure, the enzyme renin cleaves angiotensinogen to produce angiotensin-1 (angiotensin 1-10). Angiotensin-1 is a substrate of ACE (angiotensin converting enzyme) that removes a dipeptide to yield the physiologically active peptide angiotensin-2 (angiotensin 1- 8). Angiotensin-1 and angiotensin-2 can be further processed to generate angiotensin-3 (angiotensin 2-8), angiotensin-4 (angiotensin 3-8). Angiotensin 1-7 is cleaved from angiotensin-2 by ACE2 or from angiotensin-1 by MME (neprilysin). Angiotensin 1-9 is cleaved from angiotensin-1 by ACE2. Genetic variations in AGT are a cause of susceptibility to essential hypertension (EHT). Essential hypertension is a condition in which blood pressure is consistently higher than normal with no identifiable cause. Defects in AGT are a cause of renal tubular dysgenesis (RTD). RTD is an autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype). Belongs to the serpin family.

Protein type: Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 1q42.2

Cellular Component: cytoplasm; extracellular region; extracellular space

Molecular Function: growth factor activity; hormone activity; protein binding; serine-type endopeptidase inhibitor activity; sodium channel regulator activity; superoxide-generating NADPH oxidase activator activity; type 1 angiotensin receptor binding; type 2 angiotensin receptor binding

Biological Process: activation of NF-kappaB transcription factor; activation of NF-kappaB-inducing kinase; aging; angiotensin maturation; angiotensin mediated drinking behavior; angiotensin mediated regulation of renal output; angiotensin mediated vasoconstriction involved in regulation of systemic arterial blood pressure; artery smooth muscle contraction; astrocyte activation; blood vessel development; blood vessel remodeling; cell surface receptor linked signal transduction; cell-cell signaling; cell-matrix adhesion; cellular lipid metabolic process; cellular protein metabolic process; cellular sodium ion homeostasis; cytokine secretion; establishment of blood-nerve barrier; excretion; extracellular matrix organization and biogenesis; female pregnancy; fibroblast proliferation; G-protein coupled receptor protein signaling pathway; G-protein signaling, coupled to cGMP nucleotide second messenger; G-protein signaling, coupled to IP3 second messenger (phospholipase C activating); kidney development; negative regulation of angiogenesis; negative regulation of cell growth; negative regulation of cell proliferation; negative regulation of nerve growth factor receptor signaling pathway; negative regulation of neuron apoptosis; negative regulation of tissue remodeling; nitric oxide mediated signal transduction; ovarian follicle rupture; peristalsis; phospholipase C activation; positive regulation of cellular protein metabolic process; positive regulation of cytokine production; positive regulation of epidermal growth factor receptor signaling pathway; positive regulation of fatty acid biosynthetic process; positive regulation of fibroblast proliferation; positive regulation of inflammatory response; positive regulation of MAPKKK cascade; positive regulation of multicellular organism growth; positive regulation of NAD(P)H oxidase activity; positive regulation of nitric oxide biosynthetic process; positive regulation of organ growth; positive regulation of peptidyl-serine phosphorylation; positive regulation of peptidyl-tyrosine phosphorylation; positive regulation of phosphoinositide 3-kinase cascade; positive regulation of superoxide release; positive regulation of transcription, DNA-dependent; positive regulation of vasodilation; regulation of blood pressure; regulation of calcium ion transport; regulation of cell growth; regulation of cell proliferation; regulation of heart rate; regulation of long-term neuronal synaptic plasticity; regulation of norepinephrine secretion; regulation of transmission of nerve impulse; regulation of vasoconstriction; renal response to blood flow during renin-angiotensin regulation of systemic arterial blood pressure; renal system process; renin-angiotensin regulation of aldosterone production; renin-angiotensin regulation of blood vessel size; renin-angiotensin regulation of blood volume; response to cold; response to muscle activity involved in regulation of muscle adaptation; response to salt stress; smooth muscle cell differentiation; smooth muscle cell proliferation; stress-activated MAPK cascade; ureteric bud branching; vasodilation

Disease: Hypertension, Essential; Renal Tubular Dysgenesis