SAB3500346
Anti-ACE2 antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
Synonyme(s) :
Anti-ACE2
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About This Item
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41
Produits recommandés
Source biologique
rabbit
Conjugué
unconjugated
Forme d'anticorps
affinity isolated antibody
Type de produit anticorps
primary antibodies
Clone
polyclonal
Forme
buffered aqueous solution
Espèces réactives
mouse, human
Technique(s)
immunofluorescence: suitable
immunohistochemistry: suitable
indirect ELISA: suitable
western blot: suitable
Numéro d'accès NCBI
Numéro d'accès UniProt
Conditions d'expédition
dry ice
Température de stockage
−20°C
Modification post-traductionnelle de la cible
unmodified
Informations sur le gène
human ... ACE2(59272)
Description générale
Angiotensin-converting enzyme-2 (ACE2), is a membrane-associated and secreted enzyme, encoded by the gene mapped to human chromosome Xp22.2. Ace 2 is a human homolog of ACE and is expressed mainly on vascular endothelium of heart, kidney, and testis. Ace2 structure comprises a N-terminal PD and a C-terminal collectrin-like domain (CLD).
Immunogène
ACE2 antibody was raised against a synthetic peptide corresponding to amino acids near the center of human ACE2.
Actions biochimiques/physiologiques
Angiotensin-converting enzyme-2 (ACE2) catalyzes the conversion of Ang I to Ang1-9. It might also be involved in maintaining the balance of local renin-angiotensin system (RAS) in heart and kidney. Ace 2 acts as a functional receptor for spike glycoprotein of severe acute respiratory syndrome-coronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2), which is a causative agent for coronavirus disease 2019 (COVID-19). Downregulated expression of Ace 2 causes cardiovascular diseases.
Caractéristiques et avantages
Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.
Liaison
The action of this antibody can be blocked using blocking peptide SBP3500346.
Forme physique
Supplied in PBS with 0.02% sodium azide.
Clause de non-responsabilité
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Description
Tarif
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 2
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Les clients ont également consulté
Lin Wang et al.
Theranostics, 11(2), 649-664 (2021-01-05)
The novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has caused a worldwide epidemic of the lethal respiratory coronavirus disease (COVID-19), necessitating urgent development of specific and effective therapeutic tools. Among several therapeutic targets of coronaviruses, the spike protein is
Elisa Avolio et al.
Clinical science (London, England : 1979), 135(24), 2667-2689 (2021-11-23)
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) causes a broad range of clinical responses including prominent microvascular damage. The capacity of SARS-CoV-2 to infect vascular cells is still debated. Additionally, the SARS-CoV-2 Spike (S) protein may act as a
Zhen Zou et al.
Nature communications, 5, 3594-3594 (2014-05-08)
The potential for avian influenza H5N1 outbreaks has increased in recent years. Thus, it is paramount to develop novel strategies to alleviate death rates. Here we show that avian influenza A H5N1-infected patients exhibit markedly increased serum levels of angiotensin
Yang-Kai Wang et al.
American journal of physiology. Heart and circulatory physiology, 307(2), H182-H190 (2014-05-20)
The rostral ventrolateral medulla (RVLM) plays a key role in cardiovascular regulation. It has been reported that tonically active glutamatergic input to the RVLM is increased in hypertensive rats, whereas angiotensin-converting enzyme 2 (ACE2) in the brain has been suggested
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