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Mouse Monoclonal eNOS phospho S632 antibody. Suitable for WB and reacts with Human samples. Cited in 15 publications. Immunogen corresponding to Synthetic Peptide within Mouse Nitric oxide synthase, endothelial phospho S632.

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Images

Western blot - Anti-eNOS (phospho S632) antibody [M232] (AB76199), expandable thumbnail
  • Western blot - Anti-eNOS (phospho S632) antibody [M232] (AB76199), expandable thumbnail

Publications

Key facts

Isotype
IgG1
Host species
Mouse
Storage buffer

Preservative: 0.05% Sodium azide
Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.1% BSA

Form
Liquid
Clonality
Monoclonal

Immunogen

  • Synthetic Peptide within Mouse Nitric oxide synthase, endothelial phospho S632. The exact immunogen used to generate this antibody is proprietary information. Database link P70313

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Reactivity data

Select an application
Product promiseTestedExpectedPredictedNot recommended
WB
Human
Tested
Rat
Predicted

Tested
Tested

Species
Human
Dilution info
1/500
Notes

-

Predicted
Predicted

Species
Rat
Dilution info
-
Notes

-

Target data

Function

Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets. May play a significant role in normal and abnormal limb development.

Alternative names

Ecnos, Nitric oxide synthase 3, Constitutive NOS, EC-NOS, NOS type III, cNOS, NOSIII, Endothelial NOS, eNOS

Recommended products

Mouse Monoclonal eNOS phospho S632 antibody. Suitable for WB and reacts with Human samples. Cited in 15 publications. Immunogen corresponding to Synthetic Peptide within Mouse Nitric oxide synthase, endothelial phospho S632.

Key facts

Isotype
IgG1
Form
Liquid
Clonality
Monoclonal
Immunogen
  • Synthetic Peptide within Mouse Nitric oxide synthase, endothelial phospho S632. The exact immunogen used to generate this antibody is proprietary information. Database link P70313
Clone number
M232
Purification technique
Affinity purification Protein A
Specificity

ab76199 is not expected to react with other NOS family members due to low homology.

Concentration
Loading...

Storage

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Storage information
Stable for 12 months at -20°C

Notes

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Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.
Activity summary

ENOS also known as endothelial nitric oxide synthase is an enzyme important for the production of nitric oxide (NO) in blood vessels. This protein with a molecular weight of approximately 133 kDa is expressed mostly in endothelial cells. eNOS plays a mechanical role in synthesizing NO from L-arginine a process requiring cofactors such as NADPH and oxygen. The activity of eNOS can be investigated through techniques such as Western blot with specific assays like phospho-eNOS ELISA available to measure its phosphorylated forms indicating activated states of the enzyme.

Biological function summary

ENOS contributes significantly to the regulation of vascular tone and blood flow by promoting vasodilation. It does not function alone; instead it forms complexes with other proteins to exert its full effect. eNOS activity influences the process of angiogenesis inflammation modulation and platelet aggregation. Through its ability to produce nitric oxide eNOS acts as a signaling molecule helping maintain vascular homeostasis.

Pathways

ENOS is a critical player in the NO signaling pathway and interacts intricately with the PI3K/Akt pathway. Nitric oxide produced by eNOS has a role in signaling cascades that lead to vascular dilation and reduced blood pressure. The PI3K/Akt pathway regulates eNOS activity via phosphorylation enhancing NO production. Other proteins like caveolin-1 and calmodulin modulate eNOS impacting these pathways' outcomes.

Associated diseases and disorders

ENOS is associated with cardiovascular conditions like atherosclerosis and hypertension. Dysfunction of eNOS can lead to reduced NO production impairing vasodilation and contributing to these diseases. In cardiovascular disorders eNOS interacts with proteins such as the angiotensin II type 1 receptor which can negatively impact its function exacerbating disease states. Investigating eNOS and its related proteins provides insight into potential therapeutic targets for improving cardiovascular health.

Product promise

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2 product images

  • Western blot - Anti-eNOS (phospho S632) antibody [M232] (ab76199), expandable thumbnail

    Western blot - Anti-eNOS (phospho S632) antibody [M232] (ab76199)

    The 120 kDa band may be a truncated form of eNOS.

    All lanes: Western blot - Anti-eNOS (phospho S632) antibody [M232] (ab76199) at 1/500 dilution

    Lane 1: human umbilical vein endothelialcells, untreated

    Lane 2: human umbilical vein endothelialcells, treated with lambda phosphatase

    Predicted band size: 133 kDa

    Observed band size: 120 kDa, 140 kDa

  • Western blot - Anti-eNOS (phospho S632) antibody [M232] (ab76199), expandable thumbnail

    Image collected and cropped by CiteAb under a CC-BY license from the publication

    Western blot - Anti-eNOS (phospho S632) antibody [M232] (ab76199)

    eNOS (phospho S632) western blot using anti-eNOS (phospho S632) antibody [M232] ab76199. Publication image and figure legend from Gupta, A., Anjomani-Virmouni, S., et al., 2017, Mol Cell, PubMed 28306514.


    ab76199 was used in this publication in western blot. This may not be the same as the application(s) guaranteed by Abcam. For a full list of applications guaranteed by Abcam for ab76199 please see the product overview.

    PARK2 Depletion Leads to Enhanced S-nitrosylation and Ubiquitination of PTEN(A) Anti-PTEN immunoprecipitates (IP) derived from MYC-tagged-transfected PTEN HCT116 cells expressing GFP or PARK2 shRNA.(B) Fluorometric measurement of S-nitrosylated PTEN between shGFP and shPARK2 HCT116 cells. SNO-PTEN was assessed by NO release, causing the conversion of DAN to the fluorescent compound NAT (p = 0.009).(C and D) Immunoblot analysis of (C) whole-cell lysates and (D) anti-PTEN immunoprecipitates (IP) derived from HA-ubiquitin (Ub) and Myc-tagged PTEN-transfected HCT116 cells expressing GFP or PARK2 shRNA. Where indicated, cells were treated with MG132 (10 μM) for 6 hr before collection.(E–G) Immunoblot analysis and anti-PTEN immunoprecipitates derived from (E) Myc-tagged WT or C83S mutant PTEN-transfected HCT116 cells expressing GFP or PARK2 shRNA; (F) WT PTEN-transfected shGFP and shPARK2 HCT116 cells, 48 hr post-transfection with scrambled or AMPK α1 and AMPK α2 siRNAs; and (G) parental HCT116 treated (or not treated) with the allosteric AMPK activator 991 for 5 hr (20 μM) following 2 hr serum starvation (left) or with 25-mM glucose-containing DMEM (middle) for 6 hr or with oligomycin (5 μM) for 2 hr. Data are represented as mean ± SEM.See also Figures S5 and S6.

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