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AB113188

Recombinant Human Heme Oxygenase 1 protein

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(1 Publication)

Recombinant Human Heme Oxygenase 1 protein is a Human Full Length protein, in the 1 to 288 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, WB, PepArr.

View Alternative Names

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

2 Images
Western blot - Recombinant Human Heme Oxygenase 1 protein (AB113188)
  • WB

Unknown

Western blot - Recombinant Human Heme Oxygenase 1 protein (AB113188)

All lanes:

anti-Heme Oxygenase 1 antibody at 1/1000 dilution

All lanes:

Western blot - Recombinant Human Heme Oxygenase 1 protein (ab113188) at 0.1 µg

false

SDS-PAGE - Recombinant Human Heme Oxygenase 1 protein (AB113188)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human Heme Oxygenase 1 protein (AB113188)

SDS-PAGE showing ab113188 stained with Coomassie stain.
Lane 1 : 0.5μg protein
Lane 2 : 1.0μg protein
Lane 3 : 2.0μg protein
Lane 4 : 5.0μg protein

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

PepArr, WB, SDS-PAGE

applications

Biologically active

No

Accession

P09601

Animal free

No

Carrier free

No

Species

Human

Storage buffer

Constituents: 2.63% Sodium chloride, 2% Glycerol (glycerin, glycerine), 0.79% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.002% PMSF

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "PepArr": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVALEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRASNKVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM","proteinLength":"Full Length","predictedMolecularWeight":"32 kDa","actualMolecularWeight":null,"aminoAcidEnd":288,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P09601","tags":[]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

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.

Specifications

Form

Liquid

Additional notes

ab113188 is purified by multi-step chromatography.

General info

Function

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.

Sequence similarities

Belongs to the heme oxygenase family.

Post-translational modifications

A soluble form arises by proteolytic removal of the membrane anchor.

Product protocols

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 (1)

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

Journal of the American Society of Nephrology : JA 23:1048-57 PubMed22440905

2012

Plasma and urinary heme oxygenase-1 in AKI.

Applications

Unspecified application

Species

Unspecified reactive species

Richard A Zager,Ali C M Johnson,Kirsten Becker
View all publications

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