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AB238506

Anti-EPX antibody

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(5 Publications)

Rabbit Polyclonal EPX antibody. Suitable for IHC-P and reacts with Human samples. Cited in 5 publications. Immunogen corresponding to Recombinant Fragment Protein within Human EPX aa 100-300.

View Alternative Names

EPER, EPO, EPP, EPX, Eosinophil peroxidase

2 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-EPX antibody (AB238506)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-EPX antibody (AB238506)

Paraffin-embedded human endometrial cancer tissue stained for EPX using ab238506 at 1/300 dilution in immunohistochemical analysis.

After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30 minutes at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-EPX antibody (AB238506)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-EPX antibody (AB238506)

Paraffin-embedded human ovarian cancer tissue stained for EPX using ab238506 at 1/300 dilution in immunohistochemical analysis.

After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30 minutes at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P

applications

Immunogen

Recombinant Fragment Protein within Human EPX aa 100-300. The exact immunogen used to generate this antibody is proprietary information.

P11678

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "IHCP" : {"fullname" : "Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections)", "shortname":"IHC-P"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "IHCP-species-checked": "testedAndGuaranteed", "IHCP-species-dilution-info": "1/200 - 1/500", "IHCP-species-notes": "<p></p> Perform heat-mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol." } } }
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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Purification notes
Purity >95%.
Storage buffer
pH: 7.4 Preservative: 0.03% Proclin 300 Constituents: PBS, 50% Glycerol (glycerin, glycerine)
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
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Supplementary information

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

EPX also known as eosinophil peroxidase or e p x is an enzyme with a molecular mass of approximately 71 kDa. This enzyme is mainly expressed in eosinophils a type of white blood cell involved in the immune response. EPX is located in the granules of eosinophils and it plays a role in the catalysis of halide ions and hydrogen peroxide to produce hypohalous acids which are potent antimicrobial agents. These acids contribute to the killing of bacteria and other pathogens making the enzyme a critical component of the immune system.
Biological function summary

Eosinophil peroxidase participates in the body's defense against parasitic infections and allergic reactions. It is not known to be a part of a larger protein complex but it does interact with other proteins within the immune response setting. EPX helps in generating reactive oxygen species which have antimicrobial properties and are important in immune signaling pathways. Although it can lead to tissue damage when overproduced its controlled activity is necessary for effective immune function.

Pathways

Eosinophil peroxidase's activity intersects with the respiratory burst pathway and the detoxification pathway. The enzyme contributes to the formation of reactive oxygen species in the respiratory burst pathway which is important for pathogen destruction. EPX is also connected with enzymes like myeloperoxidase (MPO) that function similarly in the immune response though EPX is more specific to eosinophils. This specialization makes it an important player in eosinophil-associated diseases and disorders.

Eosinophil peroxidase has links to asthma and allergic diseases. Its activity in producing reactive oxygen species and hypohalous acids can exacerbate airway inflammation in asthma resulting in tissue damage. Additionally EPX has been studied in the context of autoimmune conditions as its dysregulated activity may contribute to inflammation. Its interaction with other proteins like myeloperoxidase could also influence such diseases highlighting the enzyme's role in pathological processes beyond its beneficial antimicrobial functions.
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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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Target data

Mediates tyrosine nitration of secondary granule proteins in mature resting eosinophils. Shows significant inhibitory activity towards Mycobacterium tuberculosis H37Rv by inducing bacterial fragmentation and lysis.
See full target information EPX
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Publications (5)

Recent publications for all applications. Explore the full list and refine your search

Viruses 16: PubMed38932247

2024

Spontaneous Lethal Outbreak of Influenza A Virus Infection in Vaccinated Sows on Two Farms Suggesting the Occurrence of Vaccine-Associated Enhanced Respiratory Disease with Eosinophilic Lung Pathology.

Applications

Unspecified application

Species

Unspecified reactive species

Wencke Reineking,Isabel Hennig-Pauka,Ludger Schröder,Ulf Höner,Elena Schreiber,Lukas Geiping,Simon Lassnig,Marta C Bonilla,Marion Hewicker-Trautwein,Nicole de Buhr

Discover. Oncology 14:64 PubMed37160815

2023

Targeting EFNA1 suppresses tumor progression via the cMYC-modulated cell cycle and autophagy in esophageal squamous cell carcinoma.

Applications

Unspecified application

Species

Unspecified reactive species

Houxiang Jiang,Shaoxiang Wang,Ying Liu,Chaopan Zheng,Lipeng Chen,Kai Zheng,Zhenyu Xu,Yong Dai,Hongtao Jin,Zhiqiang Cheng,Chang Zou,Li Fu,Kaisheng Liu,Xiaoshi Ma

American journal of rhinology & allergy 37:402-409 PubMed36740860

2023

CCAD or eCRS: Defining Eosinophilic Subpopulations in Chronic Rhinosinusitis.

Applications

Unspecified application

Species

Unspecified reactive species

Andrea Sit,Raquel Alvarado,Peter Earls,Janet Rimmer,Larry Kalish,Raewyn Campbell,William Sewell,Richard J Harvey

Cancers 14: PubMed36428768

2022

Activated Eosinophils Predict Longer Progression-Free Survival under Immune Checkpoint Inhibition in Melanoma.

Applications

Unspecified application

Species

Unspecified reactive species

Nadine L Ammann,Yasmin F Schwietzer,Christian Mess,Julia-Christina Stadler,Glenn Geidel,Julian Kött,Klaus Pantel,Stefan W Schneider,Jochen Utikal,Alexander T Bauer,Christoffer Gebhardt

Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology 52:1403-1413 PubMed35475305

2022

Mepolizumab decreases tissue eosinophils while increasing type-2 cytokines in eosinophilic chronic rhinosinusitis.

Applications

Unspecified application

Species

Unspecified reactive species

Sophie Walter,Jacqueline Ho,Raquel Alvarado,Greg Smith,David R Croucher,Sharron Liang,Jessica W Grayson,João Mangussi-Gomes,Simone L Van Es,Peter Earls,Janet Rimmer,Raewyn Campbell,Larry Kalish,Raymond Sacks,Richard J Harvey
View all publications
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Product promise

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