Analytical Data
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Gene name
FECH
- Application
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Alternative Names
FECH；Ferrochelatase. mitochondrial
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P22830
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Expression Region
55-423aa
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AA Sequence
GAKPQVQPQKRKPKTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKRRTPKIQEQYRRIGGGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFRYVHPLTEEAIEEMERDGLERAIAFTQYPQYSCSTTGSSLNAIYRYYNQVGRKPTMKWSTIDRWPTHHLLIQCFADHILKELDHFPLEKRSEVVILFSAHSLPMSVVNRGDPYPQEVSATVQKVMERLEYCNPYRLVWQSKVGPMPWLGPQTDESIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAKECGVENIRRAESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRETKSFFTSQQL
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Molecular Weight
49.6 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Identification
Protein Description
FECH, or ferrochelatase, is a crucial enzyme in the heme biosynthesis pathway, responsible for catalyzing the insertion of ferrous iron into protoporphyrin IX to form heme. This process is vital for various biological functions, including oxygen transport, electron transfer, and catalysis in numerous metabolic pathways. Defects in FECH lead to disorders such as erythropoietic protoporphyria, characterized by increased levels of protoporphyrin and associated photosensitivity. Given the essential role of heme in cellular physiology, the study of FECH and its recombinant forms has gained significant attention. Researchers are keen to understand its structure-function relationships, the mechanisms of enzyme regulation, and how mutations affect its activity. Recombinant FECH proteins provide a powerful tool to investigate these aspects in vitro, facilitating the exploration of enzyme kinetics, substrate specificity, and interaction with potential therapeutic agents. Advances in recombinant protein technology, including expression systems and purification methods, have enabled the production of functional FECH for comprehensive studies. Furthermore, understanding FECH's role and regulation in heme metabolism is not only crucial for elucidating the pathophysiology of related disorders but also for developing novel therapeutic strategies aimed at modulating heme levels in various clinical conditions.
