SERPINA8 Human

Serpin Peptidase Inhibitor, Clade A Member 8 Human Recombinant
Cat. No.
BT23670
Source
HEK 293.
Synonyms
Angiotensinogen, Serpin A8, AGT, SERPINA8, ANHU.
Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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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 Flag tag at C-Terminus.
The Human SERPINA8 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
SERPINA8 (Serpin Peptidase Inhibitor, Clade A Member 8) is also known as pre-angiotensinogen, or angiotensinogen precursor. It is primarily produced in the liver. When blood pressure drops, the enzyme renin cleaves SERPINA8 to produce angiotensin I. Angiotensin I is then converted to the active hormone angiotensin II by angiotensin-converting enzyme (ACE). SERPINA8 plays a crucial role in blood pressure regulation and is implicated in the development of hypertension and preeclampsia. Mutations in the SERPINA8 gene are associated with an increased risk of essential hypertension and can cause renal tubular dysgenesis, a severe developmental disorder of the kidneys. Furthermore, defects in this gene have been linked to non-familial structural atrial fibrillation and inflammatory bowel disease.
Description
Recombinant Human SERPINA8 is produced in HEK cells. It is a single-chain polypeptide containing 462 amino acids (a.a 34-485), with a C-terminal 2 a.a linker and an 8 a.a Flag tag. This protein is glycosylated and has a calculated molecular mass of 51.0 kDa. Purification is achieved through proprietary chromatographic techniques.
Physical Appearance
White lyophilized powder.
Formulation
The product is sterile filtered (0.4 µm) and lyophilized from a 0.5 mg/ml solution in 20 mM Tris buffer, 50 mM NaCl, pH 7.5.
Solubility
To reconstitute, add deionized water to achieve a working concentration of 0.5 mg/ml. Allow the lyophilized pellet to dissolve completely. Note: This product is not sterile. Before using in cell culture, filter the solution through an appropriate sterile filter.
Stability
Store the lyophilized protein at -20°C. After reconstitution, aliquot the product to minimize freeze-thaw cycles. The reconstituted protein remains stable at 4°C for a limited time (at least two weeks with no observable changes).
Purity
Purity is determined to be greater than 95% by SDS-PAGE analysis.
Synonyms
Angiotensinogen, Serpin A8, AGT, SERPINA8, ANHU.
Source
HEK 293.
Amino Acid 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.

Product Science Overview

Introduction

Serpin Peptidase Inhibitor, Clade A Member 8 (SERPINA8), also known as Angiotensinogen (AGT), is a member of the serine protease inhibitor (serpin) family. This family is characterized by its ability to inhibit proteases, which are enzymes that break down proteins. SERPINA8 plays a crucial role in the renin-angiotensin system, which is essential for blood pressure regulation and fluid balance in the body.

Structure and Function

SERPINA8 is an α-2-globulin protein produced constitutively by the liver and released into the bloodstream . It is a precursor to angiotensin I, which is further converted to angiotensin II, a potent vasoconstrictor that increases blood pressure. The protein’s structure includes an exposed reactive center loop (RCL) that interacts with the active site of target proteases, inhibiting their activity .

Physiological Role

The primary function of SERPINA8 is to regulate blood pressure and electrolyte balance through the renin-angiotensin system. When blood pressure drops, renin is released from the kidneys, which cleaves angiotensinogen to produce angiotensin I. Angiotensin I is then converted to angiotensin II by the angiotensin-converting enzyme (ACE). Angiotensin II acts on various tissues to increase blood pressure by constricting blood vessels, stimulating aldosterone release, and promoting sodium and water retention .

Clinical Significance

Mutations or dysregulation of SERPINA8 can lead to various health issues. Elevated levels of angiotensinogen are associated with hypertension, while deficiencies can result in hypotension. Additionally, SERPINA8 has been implicated in the pathogenesis of cardiovascular diseases, kidney disorders, and metabolic syndromes .

Research and Therapeutic Potential

Recombinant SERPINA8 is used in research to study its role in the renin-angiotensin system and its potential as a therapeutic target. Understanding the mechanisms of SERPINA8 can lead to the development of new treatments for hypertension and related cardiovascular diseases. Additionally, inhibitors of the renin-angiotensin system, such as ACE inhibitors and angiotensin receptor blockers (ARBs), are commonly used to manage high blood pressure and heart failure .

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