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AB137042

Anti-FECH antibody [EPR8312]

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(6 Publications)

Rabbit Recombinant Monoclonal FECH antibody. Suitable for WB and reacts with Human samples. Cited in 6 publications.

View Alternative Names

Heme synthase, Protoheme ferro-lyase, FECH

1 Images
Western blot - Anti-FECH antibody [EPR8312] (AB137042)
  • WB

Unknown

Western blot - Anti-FECH antibody [EPR8312] (AB137042)

All lanes:

Western blot - Anti-FECH antibody [EPR8312] (ab137042) at 1/1000 dilution

Lane 1:

Human fetal liver lysate

Lane 2:

K562 cell lysate

Secondary

All lanes:

HRP labelled goat anti-rabbit at 1/2000 dilution

Predicted band size: 48 kDa

false

  • Carrier free

    Anti-FECH antibody [EPR8312] - BSA and Azide free

Key facts

Host species

Rabbit

Clonality

Monoclonal

Clone number

EPR8312

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

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

Reactivity data

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Product details

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

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.

Properties and storage information

Form
Liquid
Purity
Tissue culture supernatant
Storage buffer
pH: 7.2 - 7.4 Preservative: 0.01% Sodium azide Constituents: 50% Tissue culture supernatant, 40% Glycerol (glycerin, glycerine), 9% PBS, 0.05% BSA
Shipped at conditions
Blue Ice
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

Supplementary information

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

FECH also known as ferrochelatase is a mitochondrial enzyme responsible for catalyzing the final step of heme biosynthesis. It inserts ferrous iron into protoporphyrin IX to form heme an essential component of hemoglobin myoglobin and various cytochromes. FECH has a molecular weight of approximately 43 kDa and is expressed in tissues with high heme demand like bone marrow and liver. Alternative names for FECH include protoporphyrinogen IX ferrochelatase and protoporphyrin ferro-lyase.
Biological function summary

FECH plays an important role in the production of heme facilitating the incorporation of iron into protoporphyrin IX. This reaction is not operating alone; FECH functions as part of multienzyme complexes in the mitochondria tightly regulated to meet cellular heme requirements. The activity of FECH ensures the proper functioning of heme-dependent proteins impacting oxygen transport and cellular respiration.

Pathways

FECH significantly contributes to the heme biosynthesis pathway. It interacts closely with other enzymes in the pathway such as aminolevulinate synthase (ALAS) and porphobilinogen deaminase essential for the step-wise production of heme. FECH's interaction with these proteins ensures the efficient flow of intermediates throughout the heme biosynthesis pathway ultimately impacting the synthesis of important heme proteins like cytochromes.

FECH mutations lead to erythropoietic protoporphyria (EPP) a condition characterized by sensitivity to sunlight and liver complications. The defective FECH reduces heme production efficiency causing protoporphyrin accumulation in red blood cells. FECH also interacts with proteins involved in mitochondrial function affecting iron metabolism and potentially linking to disorders such as sideroblastic anemia where abnormal erythropoiesis occurs due to defects in iron incorporation.

Product protocols

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

Target data

Catalyzes the ferrous insertion into protoporphyrin IX.
See full target information FECH

Publications (6)

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

Translational psychiatry 13:269 PubMed37491335

2023

A role of splenic heme biosynthesis pathway in the persistent prophylactic actions of arketamine in lipopolysaccharide-treated mice.

Applications

Unspecified application

Species

Unspecified reactive species

Li Ma,Long Wang,Youge Qu,Xiayun Wan,Kenji Hashimoto

Nature communications 11:6310 PubMed33298951

2020

Heme biosynthesis depends on previously unrecognized acquisition of iron-sulfur cofactors in human amino-levulinic acid dehydratase.

Applications

Unspecified application

Species

Unspecified reactive species

Gang Liu,Debangsu Sil,Nunziata Maio,Wing-Hang Tong,J Martin Bollinger,Carsten Krebs,Tracey Ann Rouault

Redox biology 32:101483 PubMed32169822

2020

Identification of Frataxin as a regulator of ferroptosis.

Applications

Unspecified application

Species

Unspecified reactive species

Jing Du,Yi Zhou,Yanchun Li,Jun Xia,Yongjian Chen,Sufeng Chen,Xin Wang,Weidong Sun,Tongtong Wang,Xueying Ren,Xu Wang,Yihan An,Kang Lu,Wanye Hu,Siyuan Huang,Jianghui Li,Xiangmin Tong,Ying Wang

Acta pharmaceutica Sinica. B 9:937-951 PubMed31649844

2019

Synergistic antitumor activity of artesunate and HDAC inhibitors through elevating heme synthesis synergistic upregulation of ALAS1 expression.

Applications

Unspecified application

Species

Unspecified reactive species

Cai-Ping Chen,Kun Chen,Zhiqi Feng,Xiaoan Wen,Hongbin Sun

Photochemistry and photobiology 95:1052-1059 PubMed30767226

2019

Ferrochelatase Deficiency Abrogated the Enhancement of Aminolevulinic Acid-mediated Protoporphyrin IX by Iron Chelator Deferoxamine.

Applications

Unspecified application

Species

Unspecified reactive species

Pratheeba Palasuberniam,Daniel Kraus,Matthew Mansi,Alexander Braun,Richard Howley,Kenneth A Myers,Bin Chen

MedChemComm 10:209-220 PubMed30881609

2019

4'-Phosphopantetheine and long acyl chain-dependent interactions are integral to human mitochondrial acyl carrier protein function.

Applications

Unspecified application

Species

Unspecified reactive species

Jaimeen D Majmudar,Xidong Feng,Nicholas G Fox,Joseph F Nabhan,Theresa Towle,Tiffany Ma,Renea Gooch,Christine Bulawa,Wyatt W Yue,Alain Martelli
View all publications

Product promise

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