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Serpin Peptidase Inhibitor Recombinant Protein | SERPINA8 recombinant protein

Recombinant Human Serpin Peptidase Inhibitor, Clade A Member 8

Gene Names
AGT; ANHU; SERPINA8
Purity
Purity as determined by densitometric image analysis is greater than 95%.
Synonyms
Serpin Peptidase Inhibitor; Recombinant Human Serpin Peptidase Inhibitor; Clade A Member 8; SERPINA8 Human; Clade A Member 8 Human Recombinant; Angiotensinogen; Serpin A8; AGT; SERPINA8; ANHU; SERPINA8 recombinant protein
Ordering
For Research Use Only!
Host
HEK 293
Purity/Purification
Purity as determined by densitometric image analysis is greater than 95%.
Form/Format
Filtered (0.4 um) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Filtered White lyophilized (freeze-dried) powder.
Sequence
DRVYIHPFHL VIHNESTCEQ LAKANAGKPK DPTFIPAPIQ AKTSPVDEKA LQDQLVLVAA KLDTEDKLRA AMVGMLANFL GFRIYGMHSE LWGVVHGATV LSPTAVFGTL ASLYLGALDH TADRLQAILG VPWKDKNCTS RLDAHKVLSA LQAVQGLLVA QGRADSQAQL LLSTVVGVFT APGLHLKQPF VQGLALYTPV VLPRSLDFTE LDVAAEKIDR FMQAVTGWKT GCSLTGASVD STLAFNTYVH FQGKMKGFSL LAEPQEFWVD NSTSVSVPML SGMGTFQHWS DIQDNFSVTQ VSFTESACLL LIQPHYASDL DKVEGLTFQQ NSLNWMKKLS PRTIHLTMPQ LVLQGSYDLQ DLLAQAELPA ILHTELNLQK LSNDRIRVGE VLNSIFFELE ADEREPTEST QQLNKPEVLE VTLNRPFLFA VYDQSATALH FLGRVANPLS TART DYKDDD DK.
Sequence Length
485
Solubility
It is recommended to add 200 ul deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. SERPINA8 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Preparation and Storage
Store lyophilized protein at -20 degree C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4 degree C for a limited period of time; it does not show any change after two weeks at 4 degree C.
Related Product Information for SERPINA8 recombinant protein
Description: SERPINA8 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (a.a 34-485) containing a total of 462 amino acids, having a molecular mass of 51.0kDa (calculated) and fused to a 2 a.a C-terminal linker and an 8 a.a DYKDDDDK tag at C-Terminus.The Human SERPINA8 is purified by proprietary chromatographic techniques.

Introduction: Serpin Peptidase Inhibitor, Clade A Member 8 (SERPINA8), which is a pre-angiotensinogen or angiotensinogen precursor, is expressed in the liver and cleaved by the enzyme renin in response to lowered blood pressure. The ensuing product, angiotensin I, is at that point cleaved by angiotensin converting enzyme (ACE) to produce the physiologically active enzyme angiotensin II. SERPINA8 protein is involved in maintaining blood pressure and in the pathogenesis of essential hypertension and preeclampsia. SERPINA8 gene mutations are linked with susceptibility to essential hypertension, and may cause renal tubular dysgenesis, which is a severe disorder of renal tubular development. Defects in the SERPINA8 gene are also linked with non-familial structural atrial fibrillation, and inflammatory bowel disease.
Product Categories/Family for SERPINA8 recombinant protein

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
183
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
53,154 Da
NCBI Official Full Name
angiotensinogen preproprotein
NCBI Official Synonym Full Names
angiotensinogen (serpin peptidase inhibitor, clade A, member 8)
NCBI Official Symbol
AGT
NCBI Official Synonym Symbols
ANHU; SERPINA8
NCBI Protein Information
angiotensinogen; alpha-1 antiproteinase, antitrypsin; angiotensin I; angiotensin II; pre-angiotensinogen; serine (or cysteine) proteinase inhibitor; serpin A8
UniProt Protein Name
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: extracellular space; cytoplasm; extracellular region

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

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

Disease: Renal Tubular Dysgenesis; Hypertension, Essential

Research Articles on SERPINA8

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Product Notes

The SERPINA8 agt (Catalog #AAA145734) is a Recombinant Protein produced from HEK 293 and is intended for research purposes only. The product is available for immediate purchase. The amino acid sequence is listed below: DRVYIHPFHL VIHNESTCEQ LAKANAGKPK DPTFIPAPIQ AKTSPVDEKA LQDQLVLVAA KLDTEDKLRA AMVGMLANFL GFRIYGMHSE LWGVVHGATV LSPTAVFGTL ASLYLGALDH TADRLQAILG VPWKDKNCTS RLDAHKVLSA LQAVQGLLVA QGRADSQAQL LLSTVVGVFT APGLHLKQPF VQGLALYTPV VLPRSLDFTE LDVAAEKIDR FMQAVTGWKT GCSLTGASVD STLAFNTYVH FQGKMKGFSL LAEPQEFWVD NSTSVSVPML SGMGTFQHWS DIQDNFSVTQ VSFTESACLL LIQPHYASDL DKVEGLTFQQ NSLNWMKKLS PRTIHLTMPQ LVLQGSYDLQ DLLAQAELPA ILHTELNLQK LSNDRIRVGE VLNSIFFELE ADEREPTEST QQLNKPEVLE VTLNRPFLFA VYDQSATALH FLGRVANPLS TART DYKDDD DK.. It is sometimes possible for the material contained within the vial of "Serpin Peptidase Inhibitor, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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