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Mouse Anti-FECH Recombinant Antibody (3H3) (CBMAB-F2294-CQ)

This product is a mouse antibody that recognizes FECH. The antibody 3H3 can be used for immunoassay techniques such as: ELISA.
See all FECH antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
3H3
Antibody Isotype
IgG2b, κ
Application
ELISA

Basic Information

Specificity
Human
Antibody Isotype
IgG2b, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.2
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
ferrochelatase (protoporphyria)
Introduction
The protein encoded by this gene is localized to the mitochondrion, where it catalyzes the insertion of the ferrous form of iron into protoporphyrin IX in the heme synthesis pathway. Mutations in this gene are associated with erythropoietic protoporphyria. Two transcript variants encoding different isoforms have been found for this gene. A pseudogene of this gene is found on chromosome 3.
Entrez Gene ID
2235
UniProt ID
P22830
Alternative Names
Ferrochelatase; Protoheme Ferro-Lyase; Protoporphyria; Heme Synthase; EC 4.99.1.1; Ferrochelatase (Protoporphyria);
Research Area
Catalyzes the ferrous insertion into protoporphyrin IX.
Biological Process
Cellular response to dexamethasone stimulus Source: Ensembl
Generation of precursor metabolites and energy Source: ProtInc
Heme biosynthetic process Source: UniProtKB
Protoporphyrinogen IX metabolic process Source: BHF-UCL
Response to arsenic-containing substance Source: Ensembl
Response to drug Source: Ensembl
Response to ethanol Source: Ensembl
Response to insecticide Source: Ensembl
Response to lead ion Source: Ensembl
Response to light stimulus Source: ProtInc
Response to methylmercury Source: Ensembl
Response to platinum ion Source: Ensembl
Cellular Location
Mitochondrion inner membrane
Involvement in disease
Protoporphyria, erythropoietic, 1 (EPP1):
An autosomal recessive form of porphyria with onset usually before age 10 years. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. Erythropoietic protoporphyria is marked by excessive protoporphyrin in erythrocytes, plasma, liver and feces, and by widely varying photosensitive skin changes ranging from a burning or pruritic sensation to erythema, edema and wheals.

Sishtla, K., Lambert-Cheatham, N., Lee, B., Han, D. H., Park, J., Pasha, S. P. B. S., ... & Corson, T. W. (2022). Small-molecule inhibitors of ferrochelatase are antiangiogenic agents. Cell Chemical Biology.

Abril, B., Sanchez-Torres, E. A., Bou, R., Benedito, J., & Garcia-Perez, J. V. (2022). Influence of pork liver drying on ferrochelatase activity for zinc protoporphyrin formation. LWT, 171, 114128.

Pasha, S. S., Shetty, T., Lambert-Cheatham, N. A., Sishtla, K., Mathew, D., Muniyandi, A., ... & Corson, T. W. (2021). Retinal phenotyping of ferrochelatase mutant mice reveals protoporphyrin accumulation and reduced neovascular response. Investigative ophthalmology & visual science, 62(2), 36-36.

Abril, B., Sanchez-Torres, E. A., Bou, R., Garcia-Perez, J. V., & Benedito, J. (2021). Ultrasound intensification of Ferrochelatase extraction from pork liver as a strategy to improve ZINC-protoporphyrin formation. Ultrasonics Sonochemistry, 78, 105703.

Lanzafame, M., Branca, G., Landi, C., Qiang, M., Vaz, B., Nardo, T., ... & Orioli, D. (2021). Cockayne syndrome group A and ferrochelatase finely tune ribosomal gene transcription and its response to UV irradiation. Nucleic acids research, 49(19), 10911-10930.

Babu, S. P. S. P., White, D., & Corson, T. W. (2020). Ferrochelatase regulates retinal neovascularization. FASEB journal: official publication of the Federation of American Societies for Experimental Biology, 34(9), 12419.

Ershov, P. V., Veselovsky, A. V., Mezentsev, Y. V., Yablokov, E. O., Kaluzhskiy, L. A., Tumilovich, A. M., ... & Ivanov, A. S. (2020). Mechanism of the Affinity-Enhancing Effect of Isatin on Human Ferrochelatase and Adrenodoxin Reductase Complex Formation: Implication for Protein Interactome Regulation. International journal of molecular sciences, 21(20), 7605.

Pazderník, M., Mareš, J., Pilný, J., & Sobotka, R. (2019). The antenna-like domain of the cyanobacterial ferrochelatase can bind chlorophyll and carotenoids in an energy-dissipative configuration. Journal of Biological Chemistry, 294(29), 11131-11143.

Safi, R., Mohsen-Kanson, T., Nemer, G., Dekmak, B., Rubeiz, N., El-Sabban, M., ... & Kurban, M. (2019). Loss of ferrochelatase is protective against colon cancer cells: ferrochelatase a possible regulator of the long noncoding RNA H19. Journal of gastrointestinal oncology, 10(5), 859.

Palasuberniam, P., Kraus, D., Mansi, M., Braun, A., Howley, R., Myers, K. A., & Chen, B. (2019). Ferrochelatase deficiency abrogated the enhancement of aminolevulinic acid‐mediated protoporphyrin IX by iron chelator deferoxamine. Photochemistry and photobiology, 95(4), 1052-1059.

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For research use only. Not intended for any clinical use.

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