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AB83214

PE Anti-Heme Oxygenase 1 antibody [HO-1-2]

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(6 Publications)

Mouse Monoclonal Heme Oxygenase 1 antibody - conjugated to PE. Suitable for Flow Cyt (Intra) and reacts with Human samples. Cited in 6 publications. Immunogen corresponding to Native Full Length Protein corresponding to Rat Hmox1.

View Alternative Names

HO, HO1, HMOX1, Heme oxygenase 1, HO-1

1 Images
Flow Cytometry (Intracellular) - PE Anti-Heme Oxygenase 1 antibody [HO-1-2] (AB83214)
  • Flow Cyt (Intra)

Unknown

Flow Cytometry (Intracellular) - PE Anti-Heme Oxygenase 1 antibody [HO-1-2] (AB83214)

106 Jurkat cells stained using ab83214 at a concentration of 10 μg/mL.

This image was generated using the ascites version of the product.

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

HO-1-2

Isotype

IgG2b

Conjugation

PE

Excitation/Emission

Ex: 480;565nm, Em: 578nm

Carrier free

No

Reacts with

Human

Applications

Flow Cyt (Intra)

applications

Immunogen

Native Full Length Protein corresponding to Rat Hmox1.

P06762

Reactivity data

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Product details

This product was changed from ascites to tissue culture supernatant on 22nd May 2019. Please note that the dilutions may need to be adjusted accordingly. If you have any questions, please do not hesitate to contact our scientific support team.

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Storage buffer
Preservative: 0.09% Sodium azide Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C

Supplementary information

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

Heme Oxygenase 1 also known as HO-1 or HMOX1 is an enzyme that plays an important mechanistic role in heme catabolism. It catalyzes the degradation of heme into biliverdin carbon monoxide and free iron. This process involves the cleavage of the heme ring. HO-1 has a molecular weight of approximately 32 kDa. It is widely expressed in numerous tissues but is especially abundant in the liver and spleen. Its expression is induced by heme and other stress stimuli such as heavy metals cytokines and reactive oxygen species.
Biological function summary

Heme Oxygenase 1 serves important protective functions in the body. It is not part of a larger complex but its products such as carbon monoxide and biliverdin have their own biological activities. Carbon monoxide produced by HO-1 has antiflammatory properties and can modulate apoptotic pathways. Biliverdin is reduced to bilirubin which acts as an antioxidant. The enzyme therefore directly influences cellular stress responses and maintains cellular homeostasis through these processes.

Pathways

Heme Oxygenase 1 is integrally involved in oxidative stress response and heme metabolism. It participates in the cellular response to oxidative damage by reducing oxidative stress and promoting cytoprotection. Through its heme degradation activity it is connected with the synthesis of biologically active molecules like bilirubin and carbon monoxide. Heme Oxygenase 1 activity is related to other proteins in oxidative stress pathways such as Nuclear Factor Erythroid 2-Related Factor 2 (Nrf2) which regulates its expression and globins which are sources of heme for HO-1 activity.

Heme Oxygenase 1 has been linked to conditions like cardiovascular diseases and neurodegenerative disorders. Its expression can attenuate the severity of atherosclerosis where oxidative stress is an important factor. In neurodegenerative diseases HO-1’s antioxidant properties may provide neuroprotection by mitigating oxidative damage. The protein's interactions with inflammatory cytokines such as Interleukin-6 and tumor necrosis factor-alpha influence its activity in these disease contexts.

Product protocols

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

Target data

Heme oxygenase 1. Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron (PubMed : 11121422, PubMed : 19556236, PubMed : 7703255). Affords protection against programmed cell death and this cytoprotective effect relies on its ability to catabolize free heme and prevent it from sensitizing cells to undergo apoptosis (PubMed : 20055707).. Heme oxygenase 1. (Microbial infection) During SARS-COV-2 infection, promotes SARS-CoV-2 ORF3A-mediated autophagy but is unlikely to be required for ORF3A-mediated induction of reticulophagy.. Heme oxygenase 1 soluble form. Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron.
See full target information HMOX1

Publications (6)

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

Acta pharmaceutica Sinica. B 14:3983-4000 PubMed39309491

2024

Heme oxygenase 1-mediated ferroptosis in Kupffer cells initiates liver injury during heat stroke.

Applications

Unspecified application

Species

Unspecified reactive species

Ru Li,Riqing Wei,Chenxin Liu,Keying Zhang,Sixiao He,Zhifeng Liu,Junhao Huang,Youyong Tang,Qiyuan An,Ligen Lin,Lishe Gan,Liying Zhao,Xiaoming Zou,Fudi Wang,Yuan Ping,Qiang Ma

Cancer immunology, immunotherapy : CII 72:2233-2244 PubMed36869896

2023

M2 tumor-associated macrophages resist to oxidative stress through heme oxygenase-1 in the colorectal cancer tumor microenvironment.

Applications

Unspecified application

Species

Unspecified reactive species

Misato Ito,Kosaku Mimura,Shotaro Nakajima,Hirokazu Okayama,Katsuharu Saito,Takahiro Nakajima,Tomohiro Kikuchi,Hisashi Onozawa,Shotaro Fujita,Wataru Sakamoto,Motonobu Saito,Tomoyuki Momma,Zenichiro Saze,Koji Kono

Journal of immunology (Baltimore, Md. : 1950) 206:1493-1504 PubMed33627377

2021

Conserved Epigenetic Programming and Enhanced Heme Metabolism Drive Memory B Cell Reactivation.

Applications

Unspecified application

Species

Unspecified reactive species

Madeline J Price,Christopher D Scharer,Anna K Kania,Troy D Randall,Jeremy M Boss

Cell death and differentiation 24:1224-1238 PubMed28524859

2017

Mesenchymal stem cells sense mitochondria released from damaged cells as danger signals to activate their rescue properties.

Applications

Flow Cyt

Species

Human

Meriem Mahrouf-Yorgov,Lionel Augeul,Claire Crola Da Silva,Maud Jourdan,Muriel Rigolet,Sylvie Manin,René Ferrera,Michel Ovize,Adeline Henry,Aurélie Guguin,Jean-Paul Meningaud,Jean-Luc Dubois-Randé,Roberto Motterlini,Roberta Foresti,Anne-Marie Rodriguez

Scientific reports 7:755 PubMed28389660

2017

Characteristics of the heme catabolic pathway in mild unconjugated hyperbilirubinemia and their associations with inflammation and disease prevention.

Applications

Flow Cyt

Species

Human

Christine Mölzer,Marlies Wallner,Carina Kern,Anela Tosevska,René Zadnikar,Daniel Doberer,Rodrig Marculescu,Karl-Heinz Wagner

Endocrinology 153:4367-79 PubMed22733969

2012

Immunoregulatory natural killer cells suppress autoimmunity by down-regulating antigen-specific CD8+ T cells in mice.

Applications

Unspecified application

Species

Unspecified reactive species

Margret Ehlers,Claudia Papewalis,Wiebke Stenzel,Benedikt Jacobs,Klaus L Meyer,René Deenen,Holger S Willenberg,Sven Schinner,Annette Thiel,Werner A Scherbaum,Evelyn Ullrich,Laurence Zitvogel,Matthias Schott
View all publications

Product promise

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