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rabbit anti ace2 polyclonal primary antibody  (ProSci Incorporated)


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    Structured Review

    ProSci Incorporated rabbit anti ace2 polyclonal primary antibody
    Figure 1. DHA reduces both ACE1 and <t>ACE2</t> levels in key rat tissues. Western blotting was used to measure ACE1 and ACE2 levels relative to total protein load, as
    Rabbit Anti Ace2 Polyclonal Primary Antibody, supplied by ProSci Incorporated, used in various techniques. Bioz Stars score: 93/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti ace2 polyclonal primary antibody/product/ProSci Incorporated
    Average 93 stars, based on 8 article reviews
    rabbit anti ace2 polyclonal primary antibody - by Bioz Stars, 2026-02
    93/100 stars

    Images

    1) Product Images from "Long Chain N3-PUFA Decreases ACE2 Protein Levels and Prevents SARS-CoV-2 Cell Entry."

    Article Title: Long Chain N3-PUFA Decreases ACE2 Protein Levels and Prevents SARS-CoV-2 Cell Entry.

    Journal: International journal of molecular sciences

    doi: 10.3390/ijms232213825

    Figure 1. DHA reduces both ACE1 and ACE2 levels in key rat tissues. Western blotting was used to measure ACE1 and ACE2 levels relative to total protein load, as
    Figure Legend Snippet: Figure 1. DHA reduces both ACE1 and ACE2 levels in key rat tissues. Western blotting was used to measure ACE1 and ACE2 levels relative to total protein load, as

    Techniques Used: Western Blot

    Figure 2. DHA differentially modulates ACE1 and ACE2 levels in growing and quiescent EA.hy926 en- dothelial cells. Western blotting was used to compare ACE1 and ACE2 relative to total protein load, as measured by Ponceau S in growing cells treated with ALA, EPA, or DHA at the indicated concentrations (µM) for (a) 8 and (b) 24 h, as well as in quiescent cells treated with n3-PUFA for (c) 8 and (d) 24 h. The band intensities of ACE2 and ACE1 were quantified and are graphically presented in panels (e,f), respectively; the 100 kDa band (grey bars) represents non-glycosylated ACE2, whereas the 130 kDa band (black bars) corresponds to N-glycosylated ACE2. Data are presented as mean ± SEM, n = 3; bars not sharing a common letter in the graphs are significantly different (p < 0.05) based on Duncan’s multiple range or LSD post-hoc tests.
    Figure Legend Snippet: Figure 2. DHA differentially modulates ACE1 and ACE2 levels in growing and quiescent EA.hy926 en- dothelial cells. Western blotting was used to compare ACE1 and ACE2 relative to total protein load, as measured by Ponceau S in growing cells treated with ALA, EPA, or DHA at the indicated concentrations (µM) for (a) 8 and (b) 24 h, as well as in quiescent cells treated with n3-PUFA for (c) 8 and (d) 24 h. The band intensities of ACE2 and ACE1 were quantified and are graphically presented in panels (e,f), respectively; the 100 kDa band (grey bars) represents non-glycosylated ACE2, whereas the 130 kDa band (black bars) corresponds to N-glycosylated ACE2. Data are presented as mean ± SEM, n = 3; bars not sharing a common letter in the graphs are significantly different (p < 0.05) based on Duncan’s multiple range or LSD post-hoc tests.

    Techniques Used: Western Blot

    Figure 5. Schematic of proposed mechanism of action. LCn3-PUFAs, EPA and DHA, reduce ACE2 protein levels. These n3-PUFAs may also decrease ACE2 glycosylation. These mechanisms may explain how DHA blocks SARS-CoV-2 pseudovirus entry into HEK293 cells. LCn3-PUFAs also downregulate ACE1 protein levels, thus maintaining the balance between ACE1 and ACE2, and diminishing the risk of adverse CVD outcomes. This figure was prepared by S. Huang using Microsoft PowerPoint software version 16.16.27.
    Figure Legend Snippet: Figure 5. Schematic of proposed mechanism of action. LCn3-PUFAs, EPA and DHA, reduce ACE2 protein levels. These n3-PUFAs may also decrease ACE2 glycosylation. These mechanisms may explain how DHA blocks SARS-CoV-2 pseudovirus entry into HEK293 cells. LCn3-PUFAs also downregulate ACE1 protein levels, thus maintaining the balance between ACE1 and ACE2, and diminishing the risk of adverse CVD outcomes. This figure was prepared by S. Huang using Microsoft PowerPoint software version 16.16.27.

    Techniques Used: Glycoproteomics, Software



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    ( A ) Relative <t>ACE2</t> expression levels in different U1 and U937 cells ( left ) and representative histograms of median fluorescence intensity (MFI) for each condition ( right ). Among U1, different conditions were evaluated, such as US: unstimulated U1; cfv: U1 exposed to SARS-CoV-2 cell-free; U937: unstimulated U937. U1 exposed to conditioned media (CM) obtained from non-infected MDM (Ni), MDM exposed to SARS-CoV-2 (Wh), MDM polarized (M1, or M2). PMA (Phorbol 12-myristate 13-acetate): positive control for reversal on both HIV-latently infected cell models. Data show the mean ± SEM, and statistical significance was calculated by one-way ANOVA. ( B ) Kinetics of the SARS-CoV-2 (Wh variant, MOI: 0.1) replication in myeloid (U1, U937) cells measured using RT-qPCR targeted to N and ORF1a genes in culture supernatant, as described in M&M. T0: supernatant obtained after three cell washes. 72 h: 3 days post-infection. Data are expressed as mean ± SD obtained from 4 independent experiments. (* p < 0.05; *** p < 0.001).
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    LL37 suppresses S1 associating with <t>ACE2</t> by blocking RBD. (A) Ribbon structure of LL37 (PDB: 2K6O) in lipid micelles. (B) IC 50 determination. Results shown as the mean ± standard deviation (SD) were processed by a nonlinear curve fit. (C) Binding kinetics for LL37 and RBD. (D) Binding kinetics for ACE2 and RBD. (E) BLI-based RBD blocking assay. (F) Immunofluorescence microscopy revealing the inhibition of LL37 on S1 (Green) adhering to A549 cells and the coating of LL37 (Green) on the cell membrane. The region of interest in the S1-treated group is magnified in the embedding graph. The scale bar indicates 20 μm. (G) Protein bands of S1 pretreated with increasing concentrations of LL37 binding to A549 cells. β-actin is the reference.
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    Image Search Results


    ( A ) Relative ACE2 expression levels in different U1 and U937 cells ( left ) and representative histograms of median fluorescence intensity (MFI) for each condition ( right ). Among U1, different conditions were evaluated, such as US: unstimulated U1; cfv: U1 exposed to SARS-CoV-2 cell-free; U937: unstimulated U937. U1 exposed to conditioned media (CM) obtained from non-infected MDM (Ni), MDM exposed to SARS-CoV-2 (Wh), MDM polarized (M1, or M2). PMA (Phorbol 12-myristate 13-acetate): positive control for reversal on both HIV-latently infected cell models. Data show the mean ± SEM, and statistical significance was calculated by one-way ANOVA. ( B ) Kinetics of the SARS-CoV-2 (Wh variant, MOI: 0.1) replication in myeloid (U1, U937) cells measured using RT-qPCR targeted to N and ORF1a genes in culture supernatant, as described in M&M. T0: supernatant obtained after three cell washes. 72 h: 3 days post-infection. Data are expressed as mean ± SD obtained from 4 independent experiments. (* p < 0.05; *** p < 0.001).

    Journal: Viruses

    Article Title: SARS-CoV-2 Modulation of HIV Latency Reversal in a Myeloid Cell Line: Direct and Bystander Effects

    doi: 10.3390/v16081310

    Figure Lengend Snippet: ( A ) Relative ACE2 expression levels in different U1 and U937 cells ( left ) and representative histograms of median fluorescence intensity (MFI) for each condition ( right ). Among U1, different conditions were evaluated, such as US: unstimulated U1; cfv: U1 exposed to SARS-CoV-2 cell-free; U937: unstimulated U937. U1 exposed to conditioned media (CM) obtained from non-infected MDM (Ni), MDM exposed to SARS-CoV-2 (Wh), MDM polarized (M1, or M2). PMA (Phorbol 12-myristate 13-acetate): positive control for reversal on both HIV-latently infected cell models. Data show the mean ± SEM, and statistical significance was calculated by one-way ANOVA. ( B ) Kinetics of the SARS-CoV-2 (Wh variant, MOI: 0.1) replication in myeloid (U1, U937) cells measured using RT-qPCR targeted to N and ORF1a genes in culture supernatant, as described in M&M. T0: supernatant obtained after three cell washes. 72 h: 3 days post-infection. Data are expressed as mean ± SD obtained from 4 independent experiments. (* p < 0.05; *** p < 0.001).

    Article Snippet: A rabbit anti-human ACE2 primary polyclonal Ab (ab272690, Abcam, Cambridge, UK) and goat anti-rabbit IgG secondary (PE) (Abcam, UK) were used for ACE2 quantification.

    Techniques: Expressing, Fluorescence, Infection, Positive Control, Variant Assay, Quantitative RT-PCR

    Figure 1. DHA reduces both ACE1 and ACE2 levels in key rat tissues. Western blotting was used to measure ACE1 and ACE2 levels relative to total protein load, as

    Journal: International journal of molecular sciences

    Article Title: Long Chain N3-PUFA Decreases ACE2 Protein Levels and Prevents SARS-CoV-2 Cell Entry.

    doi: 10.3390/ijms232213825

    Figure Lengend Snippet: Figure 1. DHA reduces both ACE1 and ACE2 levels in key rat tissues. Western blotting was used to measure ACE1 and ACE2 levels relative to total protein load, as

    Article Snippet: Rabbit anti-ACE2 polyclonal primary antibody (Catalog #: 3217, ProSci, San Diego, CA, USA) and StarBright Blue 700 Goat Anti-Rabbit secondary antibody (Catalog#: 12004162, Bio-Rad, Hercules, CA, USA) were used to detect ACE2.

    Techniques: Western Blot

    Figure 2. DHA differentially modulates ACE1 and ACE2 levels in growing and quiescent EA.hy926 en- dothelial cells. Western blotting was used to compare ACE1 and ACE2 relative to total protein load, as measured by Ponceau S in growing cells treated with ALA, EPA, or DHA at the indicated concentrations (µM) for (a) 8 and (b) 24 h, as well as in quiescent cells treated with n3-PUFA for (c) 8 and (d) 24 h. The band intensities of ACE2 and ACE1 were quantified and are graphically presented in panels (e,f), respectively; the 100 kDa band (grey bars) represents non-glycosylated ACE2, whereas the 130 kDa band (black bars) corresponds to N-glycosylated ACE2. Data are presented as mean ± SEM, n = 3; bars not sharing a common letter in the graphs are significantly different (p < 0.05) based on Duncan’s multiple range or LSD post-hoc tests.

    Journal: International journal of molecular sciences

    Article Title: Long Chain N3-PUFA Decreases ACE2 Protein Levels and Prevents SARS-CoV-2 Cell Entry.

    doi: 10.3390/ijms232213825

    Figure Lengend Snippet: Figure 2. DHA differentially modulates ACE1 and ACE2 levels in growing and quiescent EA.hy926 en- dothelial cells. Western blotting was used to compare ACE1 and ACE2 relative to total protein load, as measured by Ponceau S in growing cells treated with ALA, EPA, or DHA at the indicated concentrations (µM) for (a) 8 and (b) 24 h, as well as in quiescent cells treated with n3-PUFA for (c) 8 and (d) 24 h. The band intensities of ACE2 and ACE1 were quantified and are graphically presented in panels (e,f), respectively; the 100 kDa band (grey bars) represents non-glycosylated ACE2, whereas the 130 kDa band (black bars) corresponds to N-glycosylated ACE2. Data are presented as mean ± SEM, n = 3; bars not sharing a common letter in the graphs are significantly different (p < 0.05) based on Duncan’s multiple range or LSD post-hoc tests.

    Article Snippet: Rabbit anti-ACE2 polyclonal primary antibody (Catalog #: 3217, ProSci, San Diego, CA, USA) and StarBright Blue 700 Goat Anti-Rabbit secondary antibody (Catalog#: 12004162, Bio-Rad, Hercules, CA, USA) were used to detect ACE2.

    Techniques: Western Blot

    Figure 5. Schematic of proposed mechanism of action. LCn3-PUFAs, EPA and DHA, reduce ACE2 protein levels. These n3-PUFAs may also decrease ACE2 glycosylation. These mechanisms may explain how DHA blocks SARS-CoV-2 pseudovirus entry into HEK293 cells. LCn3-PUFAs also downregulate ACE1 protein levels, thus maintaining the balance between ACE1 and ACE2, and diminishing the risk of adverse CVD outcomes. This figure was prepared by S. Huang using Microsoft PowerPoint software version 16.16.27.

    Journal: International journal of molecular sciences

    Article Title: Long Chain N3-PUFA Decreases ACE2 Protein Levels and Prevents SARS-CoV-2 Cell Entry.

    doi: 10.3390/ijms232213825

    Figure Lengend Snippet: Figure 5. Schematic of proposed mechanism of action. LCn3-PUFAs, EPA and DHA, reduce ACE2 protein levels. These n3-PUFAs may also decrease ACE2 glycosylation. These mechanisms may explain how DHA blocks SARS-CoV-2 pseudovirus entry into HEK293 cells. LCn3-PUFAs also downregulate ACE1 protein levels, thus maintaining the balance between ACE1 and ACE2, and diminishing the risk of adverse CVD outcomes. This figure was prepared by S. Huang using Microsoft PowerPoint software version 16.16.27.

    Article Snippet: Rabbit anti-ACE2 polyclonal primary antibody (Catalog #: 3217, ProSci, San Diego, CA, USA) and StarBright Blue 700 Goat Anti-Rabbit secondary antibody (Catalog#: 12004162, Bio-Rad, Hercules, CA, USA) were used to detect ACE2.

    Techniques: Glycoproteomics, Software

    LL37 suppresses S1 associating with ACE2 by blocking RBD. (A) Ribbon structure of LL37 (PDB: 2K6O) in lipid micelles. (B) IC 50 determination. Results shown as the mean ± standard deviation (SD) were processed by a nonlinear curve fit. (C) Binding kinetics for LL37 and RBD. (D) Binding kinetics for ACE2 and RBD. (E) BLI-based RBD blocking assay. (F) Immunofluorescence microscopy revealing the inhibition of LL37 on S1 (Green) adhering to A549 cells and the coating of LL37 (Green) on the cell membrane. The region of interest in the S1-treated group is magnified in the embedding graph. The scale bar indicates 20 μm. (G) Protein bands of S1 pretreated with increasing concentrations of LL37 binding to A549 cells. β-actin is the reference.

    Journal: ACS Infectious Diseases

    Article Title: Human Cathelicidin Inhibits SARS-CoV-2 Infection: Killing Two Birds with One Stone

    doi: 10.1021/acsinfecdis.1c00096

    Figure Lengend Snippet: LL37 suppresses S1 associating with ACE2 by blocking RBD. (A) Ribbon structure of LL37 (PDB: 2K6O) in lipid micelles. (B) IC 50 determination. Results shown as the mean ± standard deviation (SD) were processed by a nonlinear curve fit. (C) Binding kinetics for LL37 and RBD. (D) Binding kinetics for ACE2 and RBD. (E) BLI-based RBD blocking assay. (F) Immunofluorescence microscopy revealing the inhibition of LL37 on S1 (Green) adhering to A549 cells and the coating of LL37 (Green) on the cell membrane. The region of interest in the S1-treated group is magnified in the embedding graph. The scale bar indicates 20 μm. (G) Protein bands of S1 pretreated with increasing concentrations of LL37 binding to A549 cells. β-actin is the reference.

    Article Snippet: ACE2, the Flag tag, and the His tag were detected using an anti-ACE2 rabbit polyclonal primary antibody (10108-T24, Sino Biological, 1:1000), the anti-Flag tag rabbit monoclonal primary antibody (1:1000), and the anti-His tag mouse monoclonal primary antibody (1:1000), respectively.

    Techniques: Blocking Assay, Standard Deviation, Binding Assay, Immunofluorescence, Microscopy, Inhibition, Membrane

    Complex structures of LL37 with SARS-CoV-2 RBD (A) and ACE2 (B). RBD and ACE2 (PDB: 6M0J) are shown in the ribbon structure. LL37 is shown in the red ribbon on the right. Salt bridges, hydrogen bonds, and hydrophobic interactions are shown in orange, yellow, and purple, respectively.

    Journal: ACS Infectious Diseases

    Article Title: Human Cathelicidin Inhibits SARS-CoV-2 Infection: Killing Two Birds with One Stone

    doi: 10.1021/acsinfecdis.1c00096

    Figure Lengend Snippet: Complex structures of LL37 with SARS-CoV-2 RBD (A) and ACE2 (B). RBD and ACE2 (PDB: 6M0J) are shown in the ribbon structure. LL37 is shown in the red ribbon on the right. Salt bridges, hydrogen bonds, and hydrophobic interactions are shown in orange, yellow, and purple, respectively.

    Article Snippet: ACE2, the Flag tag, and the His tag were detected using an anti-ACE2 rabbit polyclonal primary antibody (10108-T24, Sino Biological, 1:1000), the anti-Flag tag rabbit monoclonal primary antibody (1:1000), and the anti-His tag mouse monoclonal primary antibody (1:1000), respectively.

    Techniques:

    LL37 attenuates S1 binding to cells by cloaking ACE2. (A) Binding kinetics for LL37 and ACE2. (B) BLI-based ACE2 blocking assay. (C) Protein bands of S1 binding to A549 cells pretreated with increasing concentrations of LL37. β-actin is the reference. (D) Pseudovirion neutralization assay. Results are shown as the mean ± SD. Compared with the peptide-free group, the cells pretreated with 5 and 10 μg/mL LL37 were less sensitive to SARS-CoV-2 S pseudovirion infection. ***, P < 0.001.

    Journal: ACS Infectious Diseases

    Article Title: Human Cathelicidin Inhibits SARS-CoV-2 Infection: Killing Two Birds with One Stone

    doi: 10.1021/acsinfecdis.1c00096

    Figure Lengend Snippet: LL37 attenuates S1 binding to cells by cloaking ACE2. (A) Binding kinetics for LL37 and ACE2. (B) BLI-based ACE2 blocking assay. (C) Protein bands of S1 binding to A549 cells pretreated with increasing concentrations of LL37. β-actin is the reference. (D) Pseudovirion neutralization assay. Results are shown as the mean ± SD. Compared with the peptide-free group, the cells pretreated with 5 and 10 μg/mL LL37 were less sensitive to SARS-CoV-2 S pseudovirion infection. ***, P < 0.001.

    Article Snippet: ACE2, the Flag tag, and the His tag were detected using an anti-ACE2 rabbit polyclonal primary antibody (10108-T24, Sino Biological, 1:1000), the anti-Flag tag rabbit monoclonal primary antibody (1:1000), and the anti-His tag mouse monoclonal primary antibody (1:1000), respectively.

    Techniques: Binding Assay, Blocking Assay, Neutralization, Infection

    LL37 treatment inhibits pseudovirion infection in mouse lungs. (A) Diagrammatic drawing depicting the pseudovirion-based mouse infection model. Adenovirus, Adv ; pseudovirion, Pv. (B) Protein bands of ACE2, Flag-tag, and His-tag in Lewis cells infected by the adenoviruses and pseudovirions. β-actin is the reference. In the sham group, the cells were treated with sterile PBS. (C) EGFP mRNA expression relative to β-actin. Results are shown as the mean ± SD **, P < 0.01, compared to the sham group in which mice were treated with saline solution. (D) Protein bands of Flag-tag and His-tag in mouse lungs. β-Actin is the reference. (E) Immunofluorescence microscopy revealing the inhibition of LL37 on pseudovirion infection in vivo . The scale bar is 20 μm.

    Journal: ACS Infectious Diseases

    Article Title: Human Cathelicidin Inhibits SARS-CoV-2 Infection: Killing Two Birds with One Stone

    doi: 10.1021/acsinfecdis.1c00096

    Figure Lengend Snippet: LL37 treatment inhibits pseudovirion infection in mouse lungs. (A) Diagrammatic drawing depicting the pseudovirion-based mouse infection model. Adenovirus, Adv ; pseudovirion, Pv. (B) Protein bands of ACE2, Flag-tag, and His-tag in Lewis cells infected by the adenoviruses and pseudovirions. β-actin is the reference. In the sham group, the cells were treated with sterile PBS. (C) EGFP mRNA expression relative to β-actin. Results are shown as the mean ± SD **, P < 0.01, compared to the sham group in which mice were treated with saline solution. (D) Protein bands of Flag-tag and His-tag in mouse lungs. β-Actin is the reference. (E) Immunofluorescence microscopy revealing the inhibition of LL37 on pseudovirion infection in vivo . The scale bar is 20 μm.

    Article Snippet: ACE2, the Flag tag, and the His tag were detected using an anti-ACE2 rabbit polyclonal primary antibody (10108-T24, Sino Biological, 1:1000), the anti-Flag tag rabbit monoclonal primary antibody (1:1000), and the anti-His tag mouse monoclonal primary antibody (1:1000), respectively.

    Techniques: Infection, FLAG-tag, Sterility, Expressing, Saline, Immunofluorescence, Microscopy, Inhibition, In Vivo

    Representative photomicrographs of anti‐angiotensin‐converting enzyme 2 (ACE2) immunolabeling from a 10‐year‐old male neutered French Bulldog that was euthanized secondary to upper airway obstruction (A‐C), a 10‐year‐old female spayed mixed breed dog euthanized for severe congestive heart failure (CHF) because of degenerative mitral valve disease (DMVD) (D, E), and 10‐year‐old female spayed Chihuahua also euthanized for severe CHF due to DMVD (F). Photomicrographs of negative controls are presented in Supporting Information. ×20, A, D; ×40, B, C, E, F

    Journal: Journal of Veterinary Internal Medicine

    Article Title: Plasma and tissue angiotensin‐converting enzyme 2 activity and plasma equilibrium concentrations of angiotensin peptides in dogs with heart disease

    doi: 10.1111/jvim.15548

    Figure Lengend Snippet: Representative photomicrographs of anti‐angiotensin‐converting enzyme 2 (ACE2) immunolabeling from a 10‐year‐old male neutered French Bulldog that was euthanized secondary to upper airway obstruction (A‐C), a 10‐year‐old female spayed mixed breed dog euthanized for severe congestive heart failure (CHF) because of degenerative mitral valve disease (DMVD) (D, E), and 10‐year‐old female spayed Chihuahua also euthanized for severe CHF due to DMVD (F). Photomicrographs of negative controls are presented in Supporting Information. ×20, A, D; ×40, B, C, E, F

    Article Snippet: A rabbit polyclonal primary antibody against ACE2 (ARP53751‐P050, Aviva Systems Biology, San Diego, California) was used at a dilution of 1:1200 and incubated on the sections for 45 minutes at room temperature (RT).

    Techniques: Immunolabeling

    Signalment and existing treatments in 33 dogs undergoing assessment of plasma  angiotensin‐converting enzyme 2   (ACE2)  activity, including healthy dogs and dogs with congestive heart failure (CHF) because of degenerative mitral valve disease. Data shown as count or median (interquartile range)

    Journal: Journal of Veterinary Internal Medicine

    Article Title: Plasma and tissue angiotensin‐converting enzyme 2 activity and plasma equilibrium concentrations of angiotensin peptides in dogs with heart disease

    doi: 10.1111/jvim.15548

    Figure Lengend Snippet: Signalment and existing treatments in 33 dogs undergoing assessment of plasma angiotensin‐converting enzyme 2 (ACE2) activity, including healthy dogs and dogs with congestive heart failure (CHF) because of degenerative mitral valve disease. Data shown as count or median (interquartile range)

    Article Snippet: A rabbit polyclonal primary antibody against ACE2 (ARP53751‐P050, Aviva Systems Biology, San Diego, California) was used at a dilution of 1:1200 and incubated on the sections for 45 minutes at room temperature (RT).

    Techniques: Clinical Proteomics, Activity Assay, Medications, Sampling

    Plasma angiotensin‐converting enzyme 2 (ACE2) activity in 18 healthy dogs and 15 dogs with congestive heart failure because of degenerative mitral valve disease (DMVD)

    Journal: Journal of Veterinary Internal Medicine

    Article Title: Plasma and tissue angiotensin‐converting enzyme 2 activity and plasma equilibrium concentrations of angiotensin peptides in dogs with heart disease

    doi: 10.1111/jvim.15548

    Figure Lengend Snippet: Plasma angiotensin‐converting enzyme 2 (ACE2) activity in 18 healthy dogs and 15 dogs with congestive heart failure because of degenerative mitral valve disease (DMVD)

    Article Snippet: A rabbit polyclonal primary antibody against ACE2 (ARP53751‐P050, Aviva Systems Biology, San Diego, California) was used at a dilution of 1:1200 and incubated on the sections for 45 minutes at room temperature (RT).

    Techniques: Clinical Proteomics, Activity Assay

    Kidney and left ventricular (LV) myocardium angiotensin‐converting enzyme 2 (ACE2) activity in dogs euthanized for or died of noncardiac disease versus end‐stage degenerative mitral valve disease (DMVD)

    Journal: Journal of Veterinary Internal Medicine

    Article Title: Plasma and tissue angiotensin‐converting enzyme 2 activity and plasma equilibrium concentrations of angiotensin peptides in dogs with heart disease

    doi: 10.1111/jvim.15548

    Figure Lengend Snippet: Kidney and left ventricular (LV) myocardium angiotensin‐converting enzyme 2 (ACE2) activity in dogs euthanized for or died of noncardiac disease versus end‐stage degenerative mitral valve disease (DMVD)

    Article Snippet: A rabbit polyclonal primary antibody against ACE2 (ARP53751‐P050, Aviva Systems Biology, San Diego, California) was used at a dilution of 1:1200 and incubated on the sections for 45 minutes at room temperature (RT).

    Techniques: Activity Assay

    Equilibrium concentrations of angiotensin peptides (APs) and angiotensin converting enzyme (ACE) and angiotensin‐converting‐enzyme 2 (ACE2) pathways within a broader view of the renin‐angiotensin‐aldosterone system (RAAS) permits evaluation of the relative concentration and relationship between the various APs. The sizes of the circles are proportional to the median equilibrium concentration (pg/mL) of each AP. See text for description of the modified clinical staging system. AmP, aminopeptidase; DAP, aspartyl aminopeptidase; NEP, neutral endopeptidase. Other abbreviations same as in Figure

    Journal: Journal of Veterinary Internal Medicine

    Article Title: Plasma and tissue angiotensin‐converting enzyme 2 activity and plasma equilibrium concentrations of angiotensin peptides in dogs with heart disease

    doi: 10.1111/jvim.15548

    Figure Lengend Snippet: Equilibrium concentrations of angiotensin peptides (APs) and angiotensin converting enzyme (ACE) and angiotensin‐converting‐enzyme 2 (ACE2) pathways within a broader view of the renin‐angiotensin‐aldosterone system (RAAS) permits evaluation of the relative concentration and relationship between the various APs. The sizes of the circles are proportional to the median equilibrium concentration (pg/mL) of each AP. See text for description of the modified clinical staging system. AmP, aminopeptidase; DAP, aspartyl aminopeptidase; NEP, neutral endopeptidase. Other abbreviations same as in Figure

    Article Snippet: A rabbit polyclonal primary antibody against ACE2 (ARP53751‐P050, Aviva Systems Biology, San Diego, California) was used at a dilution of 1:1200 and incubated on the sections for 45 minutes at room temperature (RT).

    Techniques: Concentration Assay, Modification

    Plasma equilibrium concentrations of select angiotensin peptides (APs) before and after incubation with 5 μg/mL recombinant human ACE2 (rhACE2) from 6 dogs with stage B2 (top panel) and 7 dogs with stage C (bottom panel) degenerative mitral valve disease. The sizes of the circles are proportional to the median equilibrium concentration (pg/mL) of each AP. See text for description of the modified clinical staging system. * P < .05 versus baseline

    Journal: Journal of Veterinary Internal Medicine

    Article Title: Plasma and tissue angiotensin‐converting enzyme 2 activity and plasma equilibrium concentrations of angiotensin peptides in dogs with heart disease

    doi: 10.1111/jvim.15548

    Figure Lengend Snippet: Plasma equilibrium concentrations of select angiotensin peptides (APs) before and after incubation with 5 μg/mL recombinant human ACE2 (rhACE2) from 6 dogs with stage B2 (top panel) and 7 dogs with stage C (bottom panel) degenerative mitral valve disease. The sizes of the circles are proportional to the median equilibrium concentration (pg/mL) of each AP. See text for description of the modified clinical staging system. * P < .05 versus baseline

    Article Snippet: A rabbit polyclonal primary antibody against ACE2 (ARP53751‐P050, Aviva Systems Biology, San Diego, California) was used at a dilution of 1:1200 and incubated on the sections for 45 minutes at room temperature (RT).

    Techniques: Clinical Proteomics, Incubation, Recombinant, Concentration Assay, Modification

    The activity of angiotensin converting enzyme (ACE) and angiotensin‐converting enzyme 2 (ACE2) and other peptidases on various angiotensin peptides (APs) within a more comprehensive renin‐angiotensin‐aldosterone system (RAAS) than what is traditionally considered. Each amino acid's identifying letter and number with respect to sequence within the parent molecule, angiotensin I (AT1[1‐10]), is shown. Other abbreviations same as in Figures and

    Journal: Journal of Veterinary Internal Medicine

    Article Title: Plasma and tissue angiotensin‐converting enzyme 2 activity and plasma equilibrium concentrations of angiotensin peptides in dogs with heart disease

    doi: 10.1111/jvim.15548

    Figure Lengend Snippet: The activity of angiotensin converting enzyme (ACE) and angiotensin‐converting enzyme 2 (ACE2) and other peptidases on various angiotensin peptides (APs) within a more comprehensive renin‐angiotensin‐aldosterone system (RAAS) than what is traditionally considered. Each amino acid's identifying letter and number with respect to sequence within the parent molecule, angiotensin I (AT1[1‐10]), is shown. Other abbreviations same as in Figures and

    Article Snippet: A rabbit polyclonal primary antibody against ACE2 (ARP53751‐P050, Aviva Systems Biology, San Diego, California) was used at a dilution of 1:1200 and incubated on the sections for 45 minutes at room temperature (RT).

    Techniques: Activity Assay, Sequencing