Analytical Data
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Gene name
CYP4F11
- Application
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Alternative Names
CYP4F11；Cytochrome P450 4F11
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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
Q9HBI6
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Expression Region
38-524aa
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AA Sequence
TYTFYDNCRRLQCFPQPPKQNWFWGHQGLVTPTEEGMKTLTQLVTTYPQGFKLWLGPTFPLLILCHPDIIRPITSASAAVAPKDMIFYGFLKPWLGDGLLLSGGDKWSRHRRMLTPAFHFNILKPYMKIFNKSVNIMHDKWQRLASEGSARLDMFEHISLMTLDSLQKCVFSFESNCQEKPSEYIAAILELSAFVEKRNQQILLHTDFLYYLTPDGQRFRRACHLVHDFTDAVIQERRCTLPTQGIDDFLKNKAKSKTLDFIDVLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEIEWDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLPDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPTHTEPRRKPELILRAEGGLWLRVEPLGANSQ
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Molecular Weight
72.2 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
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Protein Description
CYP4F11, a member of the cytochrome P450 family of enzymes, plays a critical role in the metabolism of fatty acids and other endogenous compounds, influencing various physiological processes and disease mechanisms. This enzyme is primarily expressed in the liver and has been implicated in the metabolism of leukotrienes and other bioactive lipids, which are essential for inflammatory responses and cardiovascular health. Research into CYP4F11 has gained traction due to its potential involvement in diseases such as asthma, atherosclerosis, and cancer. Given the enzyme's complex regulatory mechanisms and its interactions with various substrates, generating recombinant CYP4F11 protein has become a significant focus for researchers. The recombinant protein can be used for in vitro studies to elucidate its enzymatic functions, substrate specificity, and interaction with pharmacological agents. Understanding CYP4F11's structure-function relationship is crucial for developing targeted therapies that modulate its activity, which could lead to innovative treatments for conditions linked to lipid metabolism and inflammation. Furthermore, the characterization of recombinant CYP4F11 enhances our understanding of its evolutionary adaptations and physiological roles, providing insights into the broader implications of cytochrome P450 enzymes in human health. As such, the study of CYP4F11 not only contributes to our fundamental understanding of metabolic pathways but also holds promise for the development of therapeutic strategies aimed at modulating its function in disease contexts.
