ACE2 Rat

Angiotensin Converting Enzyme 2 Rat Recombinant
Cat. No.
BT24722
Source
Sf9, Baculovirus cells.
Synonyms

ACE2, 2010305L05Rik, Angiotensin I Converting Enzyme, Angiotensin I Converting, Enzyme (Peptidyl-Dipeptidase A), Angiotensin-Converting Enzyme Homolog, Angiotensin-Converting Enzyme, ACE-Related Carboxypeptidase, Metalloprotease MPROT15, Peptidyl-Dipeptidase A, ACEH, EC 3.4.17.23, EC 3.4.17.

Appearance
Sterile Filtered colorless solution.
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.
Shipped with Ice Packs
In Stock

Description

ACE2 Rat produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 731 amino acids (18-740 aa) and having a molecular mass of 84.7kDa. ACE2 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction

Angiotensin-converting enzyme 2 (ACE2) is an enzyme found on the surface of cells in various organs, including the kidneys, intestines, lungs, heart, and arteries. It serves as an entry point for SARS coronaviruses, including SARS-CoV-2. The virus uses its spike (S) glycoprotein, a protein on its outer shell, to bind to ACE2. The S protein has two main domains, S1 and S2. The S1 domain, particularly its receptor-binding domain, interacts with ACE2. SARS-CoV and MERS-CoV both utilize their S1 C-terminal domains to attach to ACE2. Structurally, ACE2 is a transmembrane protein with an extracellular N-terminal domain containing the catalytic site and an intracellular C-terminal tail. It functions as a mono-carboxypeptidase, an enzyme that cleaves peptide bonds. ACE2 is involved in converting angiotensin I to angiotensin 1-9 and angiotensin II to angiotensin 1-7, playing a role in regulating blood pressure and other physiological processes.

Description

ACE2 Rat, produced using Sf9 insect cells and Baculovirus expression system, is a single, glycosylated polypeptide chain. It consists of 731 amino acids (specifically, amino acids 18 to 740), resulting in a molecular weight of 84.7kDa. The ACE2 protein has an 8 amino acid Histidine tag (His-Tag) added to its C-terminus to facilitate purification, which is carried out using proprietary chromatographic techniques.

Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation

The ACE2 solution is supplied in a buffer consisting of 10% Glycerol and Phosphate-Buffered Saline with a pH of 7.4.

Stability

For short-term storage (up to 2-4 weeks), the ACE2 solution can be stored at refrigerated temperature (4°C). For extended storage, it is recommended to freeze the solution at -20°C. To ensure stability during long-term storage, consider adding a carrier protein like HSA or BSA at a concentration of 0.1%. It is crucial to avoid repeated freezing and thawing of the ACE2 solution to maintain its integrity and activity.

Purity

The purity of ACE2 Rat is determined to be greater than 95% using SDS-PAGE analysis.

Biological Activity

The specific activity of ACE2 Rat is measured to be greater than 150 picomoles per minute per microgram (pmol/min/ug). Specific activity, in this context, refers to the enzyme's ability to hydrolyze 1.0 picomole of the substrate McaYVADAPK(Dnp)-OH per minute at a pH of 7.5 and a temperature of 25°C.

Synonyms

ACE2, 2010305L05Rik, Angiotensin I Converting Enzyme, Angiotensin I Converting, Enzyme (Peptidyl-Dipeptidase A), Angiotensin-Converting Enzyme Homolog, Angiotensin-Converting Enzyme, ACE-Related Carboxypeptidase, Metalloprotease MPROT15, Peptidyl-Dipeptidase A, ACEH, EC 3.4.17.23, EC 3.4.17.

Source
Sf9, Baculovirus cells.
Amino Acid Sequence

QSLIEEKAES FLNKFNQEAE DLSYQSSLAS WNYNTNITEE NAQKMNEAAA KWSAFYEEQS KIAQNFSLQE IQNATIKRQL KALQQSGSSA LSPDKNKQLN TILNTMSTIY STGKVCNSMN PQECFLLEPG LDEIMATSTD YNRRLWAWEG WRAEVGKQLR PLYEEYVVLK NEMARANNYE DYGDYWRGDY EAEGVEGYNY NRNQLIEDVE NTFKEIKPLY EQLHAYVRTK LMEVYPSYIS PTGCLPAHLL GDMWGRFWTN LYPLTTPFLQ KPNIDVTDAM VNQSWDAERI FKEAEKFFVS VGLPQMTPGF WTNSMLTEPG DDRKVVCHPT AWDLGHGDFR IKMCTKVTMD NFLTAHHEMG HIQYDMAYAK QPFLLRNGAN EGFHEAVGEI MSLSAATPKH LKSIGLLPSN FQEDNETEIN FLLKQALTIV GTLPFTYMLE KWRWMVFQDK IPREQWTKKW WEMKREIVGV VEPLPHDETY CDPASLFHVS NDYSFIRYYT RTIYQFQFQE ALCQAAKHDG PLHKCDISNS TEAGQKLLNM LSLGNSGPWT LALENVVGSR NMDVKPLLNY FQPLFVWLKE QNRNSTVGWS TDWSPYADQS IKVRISLKSA LGKNAYEWTD NEMYLFRSSV AYAMREYFSR EKNQTVPFGE ADVWVSDLKP RVSFNFFVTS PKNVSDIIPR SEVEEAIRMS RGRINDIFGL NDNSLEFLGI YPTLKPPYEP PVTLEHHHHH H.

Product Science Overview

Introduction

Angiotensin Converting Enzyme 2 (ACE2) is a crucial enzyme in the renin-angiotensin system (RAS), which plays a significant role in regulating blood pressure, fluid, and electrolyte balance. ACE2 is a homolog of the angiotensin-converting enzyme (ACE) and was discovered approximately 20 years ago . It has garnered significant attention due to its dual role as a counter-regulator of the RAS and as a receptor for coronaviruses, including SARS-CoV and SARS-CoV-2 .

Structure and Function

ACE2 is a monocarboxypeptidase that removes single amino acids from the C-terminus of its substrates . Unlike ACE, which converts angiotensin I (Ang I) to angiotensin II (Ang II), ACE2 converts Ang I to angiotensin 1-9 (Ang-(1-9)) and Ang II to angiotensin 1-7 (Ang-(1-7)) . The latter conversion is particularly significant as Ang-(1-7) has vasodilatory and anti-inflammatory properties, counteracting the effects of Ang II .

Recombinant ACE2

Recombinant ACE2 (rACE2) refers to the enzyme produced through recombinant DNA technology, which allows for the expression of ACE2 in various host cells. This recombinant form is used in research to study the enzyme’s function and potential therapeutic applications. For instance, studies have shown that rACE2 can effectively degrade Ang II, thereby normalizing blood pressure and providing a potential therapeutic target for conditions characterized by Ang II overactivity .

Role in Disease and Therapeutics

ACE2 has been implicated in several diseases, including cardiovascular diseases, lung injury, and diabetes . Its role as a receptor for SARS-CoV and SARS-CoV-2 has also highlighted its importance in infectious diseases . Recombinant ACE2 has shown promise in protecting against acute lung injury induced by these viruses . Additionally, ACE2’s ability to counter-regulate the RAS makes it a potential therapeutic target for conditions like hypertension and heart failure .

Research and Applications

Research on ACE2 has expanded significantly, especially in the context of COVID-19. Studies have demonstrated that rACE2 can inhibit SARS-CoV-2 proliferation in vitro, suggesting potential therapeutic applications . Furthermore, ACE2’s protective effects against chronic diseases and its role in the RAS make it a valuable target for drug development .

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