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SDS-PAGE

ACE2 / Angiotensin-Converting Enzyme 2 Recombinant Protein | ACE2 recombinant protein

Human ACE2 / Angiotensin-Converting Enzyme 2 Protein (Fc Tag)

Gene Names
ACE2; ACEH
Purity
> 90 % as determined by SDS-PAGE.
Synonyms
ACE2 / Angiotensin-Converting Enzyme 2; Human ACE2 / Angiotensin-Converting Enzyme 2 Protein (Fc Tag); ACE2; Angiotensin-Converting Enzyme 2; ACE2 recombinant protein
Ordering
For Research Use Only!
Host
Human Cells
Purity/Purification
> 90 % as determined by SDS-PAGE.
Form/Format
Lyophilized from sterile PBS, pH 7.4
Sequence Length
805
Application Notes
The recombinant human ACE2 consists 957 amino acids and predicts a molecular mass of 110 kDa.
Predicted N Terminal
Gln 18
Endotoxin
<1.0 EU per mug protein as determined by the LAL method.
Preparation and Storage
Samples are stable for up to twelve months from date of receipt at -70 degree C

SDS-PAGE

SDS-PAGE
Related Product Information for ACE2 recombinant protein
Background: Angiotensin-converting enzyme 2 (ACE2), a first homolog of ACE, regulates the renin angiotensin system (RAS) by counterbalancing ACE activity. Accumulating evidence in recent years has demonstrated a physiological and pathological role of ACE2 in the cardiovascular, renal and respiratory systems. ACE2 also has an important role in blood pressure control. This enzyme, an homolog of ACE, hydrolyzes angiotensin (Ang) I to produce Ang- (1-9), which is subsequently converted into Ang- (1-7) by a neutral endopeptidase and ACE. ACE2 releases Ang- (1-7) more efficiently than its catalysis of Ang- (1-9) by cleavage of Pro (7)-Phe (8) bound in Ang II. Thus, the major biologically active product of ACE2 is Ang- (1-7), which is considered to be a beneficial peptide of the RAS cascade in the cardiovascular system. A physiological role for ACE2 has been implicated in hypertension, cardiac function, heart function and diabetes, and as a receptor of the severe acute respiratory syndrome coronavirus. In the acute respiratory distress syndrome (ARDS), ACE, AngII, and AT1R promote the disease pathogenesis, whereas ACE2 and the AT2R protect from ARDS. Importantly, ACE2 has been identified as a key SARS-coronavirus receptor and plays a protective role in severe acute respiratory syndrome (SARS) pathogenesis. Furthermore, the recent explosion of research into the ACE2 homolog, collectrin, has revealed a new physiological function of ACE2 as an amino acid transporter, which explains the pathogenic role of gene mutations in Hartnup disorder. This review summarizes and discusses the recently unveiled roles for ACE2 in disease pathogenesis.

Description: A DNA sequence encoding the human ACE2 (NP_068576.1) (Met1-Ser740) was expressed with the Fc region of mouse IgG1 at the C-terminus.

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
63,912 Da
NCBI Official Full Name
angiotensin-converting enzyme 2
NCBI Official Synonym Full Names
angiotensin I converting enzyme 2
NCBI Official Symbol
ACE2
NCBI Official Synonym Symbols
ACEH
NCBI Protein Information
angiotensin-converting enzyme 2
UniProt Protein Name
Angiotensin-converting enzyme 2
UniProt Gene Name
ACE2
UniProt Synonym Gene Names
ACEH

NCBI Description

The protein encoded by this gene belongs to the angiotensin-converting enzyme family of dipeptidyl carboxydipeptidases and has considerable homology to human angiotensin 1 converting enzyme. This secreted protein catalyzes the cleavage of angiotensin I into angiotensin 1-9, and angiotensin II into the vasodilator angiotensin 1-7. The organ- and cell-specific expression of this gene suggests that it may play a role in the regulation of cardiovascular and renal function, as well as fertility. In addition, the encoded protein is a functional receptor for the spike glycoprotein of the human coronaviruses SARS and HCoV-NL63. [provided by RefSeq, Jul 2008]

Uniprot Description

ACE2: Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin- 13 and dynorphin-13 with high efficiency. May be an important regulator of heart function. In case of human coronaviruses SARS and HCoV-NL63 infections, serve as functional receptor for the spike glycoprotein of both coronaviruses. Interacts with ITGB1. Interacts with SARS-CoV and HCoV- NL63 spike glycoprotein. Up-regulated in failing heart. Expressed in endothelial cells from small and large arteries, and in arterial smooth muscle cells. Expressed in lung alveolar epithelial cells, enterocytes of the small intestine, Leydig cells and Sertoli cells. Expressed in heart, kidney, testis, and gastrointestinal system. Activated by chloride and fluoride, but not bromide. Inhibited by MLN-4760, cFP_Leu, and EDTA, but not by the ACE inhibitors linosipril, captopril and enalaprilat. Belongs to the peptidase M2 family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 3.4.17.23; Membrane protein, integral; Protease

Chromosomal Location of Human Ortholog: Xp22.2

Cellular Component: cell surface; extracellular region; extracellular space; lipid raft; plasma membrane

Molecular Function: carboxypeptidase activity; endopeptidase activity; glycoprotein binding; metallocarboxypeptidase activity; metallopeptidase activity; peptidyl-dipeptidase activity; protein binding; viral receptor activity; zinc ion binding

Biological Process: angiotensin catabolic process in blood; angiotensin maturation; angiotensin mediated drinking behavior; entry of virus into host cell; receptor biosynthetic process; regulation of cell proliferation; regulation of cytokine production; regulation of inflammatory response; regulation of systemic arterial blood pressure by renin-angiotensin; regulation of vasoconstriction; regulation of vasodilation; virion attachment, binding of host cell surface receptor

Research Articles on ACE2

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Product Notes

The ACE2 ace2 (Catalog #AAA2546522) is a Recombinant Protein produced from Human Cells and is intended for research purposes only. The product is available for immediate purchase. The recombinant human ACE2 consists 957 amino acids and predicts a molecular mass of 110 kDa. Researchers should empirically determine the suitability of the ACE2 ace2 for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. It is sometimes possible for the material contained within the vial of "ACE2 / Angiotensin-Converting Enzyme 2, 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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