Recombinant Human Ferrochelatase, Mitochondrial (FECH) Protein (His&Myc)

Name: Recombinant Human Ferrochelatase, Mitochondrial (FECH) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-00801P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Ferrochelatase, Mitochondrial (FECH) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P22830
Target Symbol	FECH
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	GAKPQVQPQKRKPKTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKRRTPKIQEQYRRIGGGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFRYVHPLTEEAIEEMERDGLERAIAFTQYPQYSCSTTGSSLNAIYRYYNQVGRKPTMKWSTIDRWPTHHLLIQCFADHILKELDHFPLEKRSEVVILFSAHSLPMSVVNRGDPYPQEVSATVQKVMERLEYCNPYRLVWQSKVGPMPWLGPQTDESIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAKECGVENIRRAESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRETKSFFTSQQL
Expression Range	55-423aa
Protein Length	Full Length of Mature Protein
Mol. Weight	49.6 kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Catalyzes the ferrous insertion into protoporphyrin IX.
Subcellular Location	Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Protein Families	Ferrochelatase family
Database References	HGNC: 3647 OMIM: 177000 KEGG: hsa:2235 STRING: 9606.ENSP00000372326 UniGene: Hs.365365
Associated Diseases	Erythropoietic protoporphyria (EPP)

Gene Functions References

FECH mRNA was largely significantly decreased in colon adenocarcinomas relative to normal colon tissues. PMID: 28075030
Using a forward chemical genetic approach, the authors identified the heme synthesis enzyme ferrochelatase (FECH) as necessary for angiogenesis in vitro and in vivo FECH is overexpressed in wet age-related macular degeneration eyes and murine choroidal neovascularization. PMID: 28377496
In this study, QM/MM and quantum mechanical thermodynamic cycle perturbation free energy calculations were performed to investigate the porphyrin metalation in human ferrochelatase. It suggests a most reasonable pathway including the steps of the ferrous iron approaching from the site with Met76 coordinated and His263 playing the role of accepting proton. PMID: 27801584
These findings suggest that homozygous polymorphism of the FECH gene is associated with a slight elevation of the protoporphyrin level in erythrocytes, resulting in a mild EPP phenotype PMID: 26280465
a novel mutation, c.84G >A, in the FECH gene in four individuals with Erythropoietic Protoporphyria, is reported. PMID: 26789144
High ferrochelatase expression is associated with growth of malarial parasites in erythropoietic protoporphyria patients. PMID: 25414439
of ASO-V1 into developing human erythroblasts from an overtly EPP subject markedly increased the production of WT FECH mRNA and reduced the accumulation of PPIX to a level similar to that measured in asymptomatic EPP subjects PMID: 24680888
Sequence analysis of the FECH gene identified a novel missense mutation in exon 4 (c.418>A, G140R) of the FECH gene, as well as the common FECH IVS3-48 polymorphism in erythropoietic protoporphyria. PMID: 23600449
Loss-of-function FECH and gain-of-function erythroid-specific ALAS2 mutations causing erythropoietic protoporphyria and x-linked protoporphyria in North American patients reveal novel mutations and a high prevalence of X-linked protoporphyria. PMID: 23364466
The mutation analysis in the FECH gene identified different genotypes with the t/t genotype, 7 with the t/M genotype, 14 with the c/t genotype and 10 with c/M genotype from different EPP families. PMID: 19656458
Sequencing of the ferrochelatase gene did not show a mutation in any of the patients studied. Furthermore, the hypomorphic allele IVS3-48C was absent in all individuals. PMID: 19656459
Molecular dynamic simulations provided insight into the conformational movements and function of the active site residues of human ferrochelatase. PMID: 23446439
function of solvent-filled channels in human ferrochelatase PMID: 22712763
Report ferrochelatase functional variants resulting in erythropoietic protoporphyria in an Ashkenazi Jewish family. PMID: 18758989
Erythropoietic protoporphyria patients and their mother revealed heterozygosity for a novel mutation (c.1052delA) in FECH gene of both children, and heterozygosity for the hypomorphic allele IVS3-48T>C in all of them. PMID: 21659066
role of IVS3-48C allele in erythropoietic protoporphyria PMID: 21132468
A novel homoallelic missense mutation (p.Ser318Tyr) was identified in the FECH gene in erythropoietic protoporphyria and palmar keratoderma PMID: 20337824
More than 96% of unrelated EPP patients have ferrochelatase deficiency (MIM 177000). Inheritance of a common hypomorphic IVS3-48C FECH allele trans to a deleterious FECH mutation reduces FECH activity below a critical threshold. Review. PMID: 20850938
analysis of the inhibitory metal ion-binding site in ferrochelatase PMID: 20966079
A novel splicing FECH mutation in a Chinese erythropoietic protoporphyria family is believed to be responsible for generating the phenotypic symptoms in this family. PMID: 19888946
the stability of newly formed ferrochelatase protein was dramatically decreased during iron deficiency PMID: 19965627
analysis of skin ferrochelatase and photosensitivity in mice and man PMID: 19657351
Mutations in the FECH gene could not account the development of liver disease in the severe phenotype of erythropoietic protoporphyria(EPP). PMID: 11929052
Data indicate a significant genotype-phenotype correlation between "null allele" mutation and protoporphyrin related liver disease in erythropoietic protoporphyria. PMID: 11929053
Modulation of penetrance by the wild-type allele in dominantly inherited erythrohepatic and acute hepatic porphyrias was studied using FECH. PMID: 14669009
Mutation in ferrochelatase is associated with erythropoietic porphyria. PMID: 15046047
analysis of frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis PMID: 15123683
Identification of autosomal recessive FECH mutations in erythropoietic protoporphyria patients with higher risk of severe liver disease in the United Kingdom. PMID: 15286165
data for 12 ferrochelatase wild-type/EPP mutant heterodimers show that some mutations result in heterodimers with the residual activity anticipated, whereas others result in heterodimers with significantly lower activity than would be predicted PMID: 15831704
mutation in promoter affects binding of a transcription factor and causes erythropoietic protoporphyria phenotype PMID: 15850836
A common single-nucleotide polymorphism of FECH gene contributes to the genetic predisposition for erythropoietic protoporphyria. PMID: 16385445
Patients with erythropoietic protoporphyria usually have a mutation in 1 Ferrochelatase allele that alters enzyme structure/function, together with a polymorphism in the nonmutant allele that causes low gene expression. PMID: 16819399
These data suggest that the first 62 amino acids of ferrochelatase allow targeting to mitochondria but do not contain sufficient information for efficient processing of the protein. PMID: 16844398
Mutations and a low-expressed allele IVS3-48c (in trans to the mutation) of the ferrochelatase (FECH) gene are responsible for erythropoietic protoporphyria (EPP) which is characterized clinically by cutaneous photosensitivity. PMID: 17196862
Substrate is bound deep within an enclosed pocket, and the binding sites with protoporphyrin IX are mapped in detail. PMID: 17261801
results highlight a novel, profilin2-dependent pathway, regulating synaptic physiology, neuronal excitability, and complex behavior PMID: 17566985
It was found that in the H263C and H341C variants, but not the F337A variant enzymes, the side chains of N75, M76, R164, H263, F337, H341, and E343 are oriented in a fashion similar to what is found in ferrochelatase with the bound porphyrin substrate PMID: 17567154
large deletions of the FECH gene are an important cause of erythropoietic protoporphyria PMID: 17597821
mutation associated with erythropoietic protoporphyria in Chinese family PMID: 17723290
show that in malignant tissue a transcriptional down-regulation of FECH occurs, which causes endogenous protoporphyrin-IX accumulation PMID: 17875605
most cases of EPP result from the coinheritance of IVS3-48C and a mutation in the FECH gene, and also document the existence of patients with mutations in homozygosity that may present a more severe form of the disease. PMID: 17875872
Data shows ferrochelatase undergoes significant changes in secondary structure during the catalytic cycle. PMID: 17884090
a ferrochelatase mutation in a Chinese family with erythropoietic protoporphyria. PMID: 18160121
analysis of FECH mutations in patients with seasonal palmar keratoderma in erythropoietic protoporphyria PMID: 18787536
ferrochelatase localizes to both the mitochondrial outer and inner membranes, and the change in the equilibrium position of the forward and reverse activities may be regulated by the phosphorylation of ferrochelatase PMID: 19691493
The findings show that at least in the cases of Mn, Pb, Cd, and Hg, metal "inhibition" of ferrochelatase occurs after metal insertion and results from poor or diminished product release. PMID: 19703464
analysis of ion selectivity and substrate inhibition in the metal ion chelation catalyzed by human ferrochelatase PMID: 19767646

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