ACE2 Antibodies

Angiotensin-converting enzyme 2 (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. .

Gene Information

Human
Gene Name:	ACE2
Uniprot:	Q9BYF1
Entrez:	59272

Family

Belongs to:
peptidase M2 family

Alternative Names

ACE2; ACE-2; ACEH; ACEHangiotensin I converting enzyme 2; ACE-related carboxypeptidase; angiotensin I converting enzyme (peptidyl-dipeptidase A) 2; angiotensin-converting enzyme 2; Angiotensin-converting enzyme homolog; DKFZp434A014; EC 3.4.17; EC 3.4.17.23; Metalloprotease MPROT15

Molecular Weight

Mass (kDA):
92.463 kDA

Genomic Context

Human
Location:	Xp22.2
Sequence:	X; NC_000023.11 (15494520..15602158, complement)

Tissue Specificity

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 (at protein level). Expressed in heart, kidney, testis, and gastrointestinal system.

Subcellular Localizations

[Processed angiotensin-converting enzyme 2]: Secreted.; Cell membrane; Single-pass type I membrane protein. Cytoplasm. Detected in both cell membrane and cytoplasm in neurons.

Diseases

• Hypertensive Disease
• Severe Acute Respiratory Syndrome
• Kidney Diseases
• Cardiovascular Diseases
• Hypertrophy
• Fibrosis
• Diabetes Mellitus
• Heart Failure
• Diabetic Nephropathy
• Inflammation
• Injury To Kidney
• Myocardial Infarction

• Cardiac Hypertrophy
• Infarction
• Diabetes Mellitus, Experimental
• Atherosclerosis
• Pathologic Vasoconstriction
• Infective Disorder
• Proteinuria Of Undiagnosed Cause

Pathways

• Pathogenesis
• Localization
• Cell Cycle
• Vasoconstriction
• Mitosis
• Cell Proliferation
• Transport
• Regulation Of Blood Pressure
• Excretion
• Membrane Fusion
• Cell Division
• Cytokinesis
• Virulence

• Cell Growth
• Immune Response
• Secretion
• Mating
• Glycosylation
• Angiogenesis
• Tropism

PTMs

• Cleavage
• Phosphorylation
• Glycosylation
• Deglycosylation

• Biotinylation
• Oxidation
• Carboxylation
• Nitration

• Reduction

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/ACE2

Best Uses Of The ACE2 Marker

ACE2 is a crucial regulator of heart function. This enzyme is involved in controlling blood pressure, a process that can affect the heart's performance. This article will explore the ways in which ACE2 interacts with SARS coronavirus 2/SARS CoV-2 spike protein and AP2M1, TMPRSS2 and.

ACE2 is an important regulator of heart function.

ACE2 plays an important role in the heart's function. A new study showed that a peptide called apelin-13 increased ACE2 expression in cardiomyocytes isolated. It did not increase ACE2 expression within endothelial cells of the coronary artery. This suggests that apelin may be useful in improving heart function. In a previous study we found that apelin decreased the weight of mice and improved their heart functions.

ACE2 regulates heart function by inhibiting the process of inflammation. Heart failure can be caused by the inflamed response to MI. However it is the RAAS components are believed to be significant regulators of the function of the heart. While this research isn't conclusive, it has uncovered evidence that ACE2 may play a critical role in heart function. Moreover, ACE2 is produced specifically in the heart.

While evidence suggests that ACE2 is a key regulator of heart function, it is still not clear what its role in the development of heart disease. However, genetic evidence suggests that it is a crucial regulator of cardiac function. However, further research will be needed to clarify the role of ACE2 within human heart failure. So far, this research is the first to determine the role of ACE2 in the heart's function. It is a prime candidate for therapeutic interventions.

ACE2 may be related to the SARS-CoV-2 virus-induced acute myocardial injury. Infection with the SARS-CoV-2 virus humans decreases ACE2 expression. In mice, ACE2-dependent myocardial inflammations were also observed suggesting a role of ACE2 in the SARS/CoV-2 illness. As the first step towards developing a vaccine that is effective against COVID-19, more research is required.

It interacts with SARS coronavirus-2/SARS-CoV-2 spike protein

The ACE2 gene was identified as a significant component of the SARS coronavirus-2/SARs-CoV-2 virus. It contains eight hundred and five amino acids. There are two variants of the ACE2 gene. One represents an alternate promoter, and one codon area. Variant 2 has an altered N-terminus, and does not contain carboxypeptidase activities. The two variants differ in the size of the ACE2 gene with the first one coding for the longest isoform, while

SARS-CoV-2 spike protein is coupled to the ACE2. This interaction is mediated by the S1 subunit, as well as the S2/S1's Cleavage site. The ACE2 is a ligand that primes HR1 to achieve enhanced fusion using a furin protease, whereas ACE2 is a binding agent with high affinity to the spike protein of SARS-CoV-2. The cleavage site S1/S2 is essential for viral entry into the host, and inhibition of this site can lead to the development of new inhibitory therapeutics.

FCCS is an effective method to measure protein interactions. It can also analyze proteins that have not been thoroughly purified. Interaction detection systems using FCCS can help in the identification of inhibitors for SARS-CoV-2. The results of this study demonstrate that FCCS-based interaction detection systems can be a useful tool to speed up the screening of SARS-CoV-2.

Understanding the interaction between SARS-CoV-2 and ACE2 could lead to the development of a reliable vaccine and treatment for SARS-CoV-induced COVID-19. It is vital to recognize that there is no vaccine for SARS and there is no method to prevent the disease via vaccination. Further studies on these two proteins could lead to the creation of neutralizing antibodies.

It interacts with TMPRSS2

This study examined the role of the ACE2 Marker as it relates to the pathogenesis and progression of COVID-19. This gene was identified to be expressed in 34 types of tumors, and was found to be in inverse relationship with TMPRSS2 expression in 15 of them. While the expression of ACE2 was not constant across all types of tumors, there was a positive relationship between this gene and macrophage M2 expression in the normal kidney tumor tissue.

We examined the expression levels of TMPRSS2 (ACE2) in 34 different types of tumors. The ISG signature was used to differentiate the tumors. The levels of expression were determined by comparing expression of ace2 in each type to that of the normal tissue. We also separated the tumors by race and age. Eight tumor types expressed high levels of TMPRSS2, while only three showed elevated levels of ACE2 in normal tissue.

The increased expression of ACE2 in lung cells was linked with protection against SARS-CoV-2 and could lead to a higher sequestration rate of the virus. However the increased expression of ACE2 does not automatically activate downstream processes. To determine the role of this gene in the SARS-CoV-2 infection it is necessary to further study its characterization. In addition, the downregulation of ACE2 could hinder the clearance of Ang II cells, which may lead to tissue damage. However, this can be beneficial in limiting the spread of the virus.

Numerous studies have revealed that ACE2 is linked to a range of conditions and symptoms. This suggests that TMPRSS2 may play a role in COVID-19 disease. Although it is not clear whether ACE2 plays a part in COVID-19, a small number of cases have suggested an unquestionably strong link with COVID-19 infection and this gene. However, it is unclear whether these two genes are the cause for the toxic effects of COVID-19 that are seen in cancer patients of human origin.

It is able to interact AP2M1

Researchers in Wuhan, China discovered a new coronavirus virus in December of this year. The 2019-nCoV viruses has been responsible for the deaths of thousands in China as well as around the world. The virus had the same receptor as SARS-CoV that was identified using single-cell RNA-Seq. It was discovered that it was concentrated in type II alveolar cell types. This could have significant implications for antiviral drug development.

There is no definitive proof that the ACE2 marker hinders the binding of the viral S protein to ACE2, but it could be a surrogate for neutralisation. The ACE2-binding epitope can be hindered by the crystal structure of the antibody. This opposition to the viral protein causes its entry into the host cell. Other studies have suggested that anti-RBD antibodies may be inhibitors specific to species. Antibodies targeting ACE2 are more potent than those that recognize other regions of the ACE2 protein.

Antibodies to detect ACE2 are used extensively in a variety of biological assays. They can be multiclonal or monoclonal and react with ACE2 proteins in different animal samples. Boster Bio used rabbit and mouse as models in the development of their ACE2 antibodies. ACE2 is a component of the angiotensin-converting enzyme. It is a possible regulator of heart function.

The ACE2 enzyme is part of the peptidase M2 family. It is a single-pass transmembrane protease enzyme with high homology to angiotensin-converting enzyme. Its role in the renin-angiotensin system is the inactivation of angiotensin II. These antibodies can be used to identify, monitoring disease progression, and improving treatment.

It prevents viral binding ACE2

Boster Bio's ACE2 marker blocks the binding of viruses. This antibody binds only to a small amount of human ACE2 in amino acids 180-230. This antigen can also be found as blocking peptide. Prices and lengths of immunogens can vary. To purchase this antibody you must contact the manufacturer. This antigen is effective against many strains of viruses. We recommend you buy the peptide with an anti-inflammatory peptide.

Eight cysteine residues compose the human ACE2 protein. Six of them are disulfide bond , and two are accessible to S-nitrosylate by reversible nuclear attack on Nitrosonitrogen. This marker inhibits viral binding by targeting the S2 subunit. The S2 subunit is responsible for binding the virus to host cells. It is crucial to know the mechanism by which the SARS coronavirus interacts with host cells.

ACE2 is a protein that is found on the surface of a variety of types of cells. This protein inhibits viral binding to the immune system, by preventing its function. SARS-CoV-2 viruses bind to ACE2 and act as a cell-to-cell gateway. The protein is found in a variety of cell types, including epithelial cellsthat line the body and act as barrier to protect against infection.

A variety of cell types were tested to determine the ability of the ACE2 marker to block binding proteins of the SARS-CoV-2 spike. HeLa-ACE2 cells were exposed for 100 mg to 'old' SNO to determine if the marker inhibits the binding of viral proteins. To test the SNO-proteins, the biotin-switch method was used.