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AB157481

Anti-Thromboxane synthase antibody [EPR7333(2)]

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(3 Publications)

Rabbit Recombinant Monoclonal Thromboxane synthase antibody. Suitable for WB and reacts with Human samples. Cited in 3 publications.

View Alternative Names

CYP5, CYP5A1, TXAS, TBXAS1, Thromboxane-A synthase, TXA synthase, TXS, Cytochrome P450 5A1, Hydroperoxy icosatetraenoate dehydratase

1 Images
Western blot - Anti-Thromboxane synthase antibody [EPR7333(2)] (AB157481)
  • WB

Unknown

Western blot - Anti-Thromboxane synthase antibody [EPR7333(2)] (AB157481)

All lanes:

Western blot - Anti-Thromboxane synthase antibody [EPR7333(2)] (ab157481) at 1/1000 dilution

Lane 1:

WI38 cell lysate at 10 µg

Lane 2:

Fetal liver lysate at 10 µg

Secondary

All lanes:

HRP labelled goat anti-rabbit at 1/2000 dilution

Predicted band size: 61 kDa

false

  • Carrier free

    Anti-Thromboxane synthase antibody [EPR7333(2)] - BSA and Azide free

Key facts

Host species

Rabbit

Clonality

Monoclonal

Clone number

EPR7333(2)

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

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Reactivity data

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Product details

Patented technology
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.

What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:

  • - High batch-to-batch consistency and reproducibility
  • - Improved sensitivity and specificity
  • - Long-term security of supply
  • - Animal-free batch production

For more information, read more on recombinant antibodies.

Species reactivity
Rat: We have preliminary internal testing data to indicate this antibody may not react with this species.
Please contact us for more information.

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Properties and storage information

Form
Liquid
Purity
Tissue culture supernatant
Storage buffer
pH: 7.2 - 7.4 Preservative: 0.01% Sodium azide Constituents: PBS, 50% Tissue culture supernatant, 40% Glycerol (glycerin, glycerine), 0.05% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
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Supplementary information

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

Thromboxane synthase also known as TBXAS1 is an enzyme that plays an important role in the biosynthesis of thromboxane A2 from prostaglandin H2. It is a 60 kDa protein primarily expressed in platelets and megakaryocytes as well as in cells within the lung kidney and spleen. By catalyzing the conversion of prostaglandin H2 to thromboxane A2 it influences the regulation of vasoconstriction and platelet aggregation.
Biological function summary

Thromboxane A2 generated by thromboxane synthase acts as a potent vasoconstrictor and promotes platelet aggregation important for hemostasis. This enzyme does not function as part of a larger complex but independently facilitates thromboxane A2 production. Its action significantly contributes to cardiovascular function where it modulates vascular tone and platelet activity.

Pathways

Thromboxane synthase is integral to the arachidonic acid metabolic pathway and the eicosanoid signaling pathway. The enzyme interacts closely with cyclooxygenase enzymes COX-1 and COX-2 in these pathways as they provide the prostaglandin H2 substrate for thromboxane A2 synthesis. By influencing these pathways thromboxane synthase indirectly affects inflammation and cardiovascular regulation.

The activity of thromboxane synthase is associated with cardiovascular diseases and disorders such as myocardial infarction and stroke. Overproduction of thromboxane A2 facilitated by this enzyme can lead to excessive platelet aggregation and vasoconstriction contributing to these conditions. Thromboxane synthase is also related to COX-2 which is implicated in inflammatory responses and is a target for anti-inflammatory drugs like aspirin and other COX inhibitors.
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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

Catalyzes the conversion of prostaglandin H2 (PGH2) to thromboxane A2 (TXA2), a potent inducer of blood vessel constriction and platelet aggregation (PubMed : 11097184, PubMed : 11297515, PubMed : 22735388, PubMed : 24009185, PubMed : 8436233, PubMed : 9873013). Cleaves also PGH2 to 12-hydroxy-heptadecatrienoicacid (12-HHT) and malondialdehyde, which is known to act as a mediator of DNA damage. 12-HHT and malondialdehyde are formed stoichiometrically in the same amounts as TXA2 (PubMed : 11297515, PubMed : 22735388, PubMed : 9873013). Additionally, displays dehydratase activity, toward (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate (15(S)-HPETE) producing 15-KETE and 15-HETE (PubMed : 17459323).
See full target information TBXAS1
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Publications (3)

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

Oncology letters 25:186 PubMed37065787

2023

HBXIP knockdown inhibits FHL2 to promote cycle arrest and suppress cervical cancer cell proliferation, invasion and migration.

Applications

Unspecified application

Species

Unspecified reactive species

Xia Gao,Lina Yang

Frontiers in immunology 13:963123 PubMed36016933

2022

Identification of nine signature proteins involved in periodontitis by integrated analysis of TMT proteomics and transcriptomics.

Applications

Unspecified application

Species

Unspecified reactive species

Wei Liu,Wei Qiu,Zhendong Huang,Kaiying Zhang,Keke Wu,Ke Deng,Yuanting Chen,Ruiming Guo,Buling Wu,Ting Chen,Fuchun Fang

Cell reports 27:3062-3080.e11 PubMed31167148

2019

Molecular Profiling and Functional Analysis of Macrophage-Derived Tumor Extracellular Vesicles.

Applications

Unspecified application

Species

Unspecified reactive species

Chiara Cianciaruso,Tim Beltraminelli,Florent Duval,Sina Nassiri,Romain Hamelin,André Mozes,Hector Gallart-Ayala,Gerardo Ceada Torres,Bruno Torchia,Carola H Ries,Julijana Ivanisevic,Michele De Palma
View all publications
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