Analytical Data
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Gene name
CYP27B1
- Application
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Alternative Names
CYP27B1；CYP1ALPHA；CYP27B；25-hydroxyvitamin D-1 alpha hydroxylase. 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
O15528
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Expression Region
1-508aa
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AA Sequence
MTQTLKYASRVFHRVRWAPELGASLGYREYHSARRSLADIPGPSTPSFLAELFCKGGLSRLHELQVQGAAHFGPVWLASFGTVRTVYVAAPALVEELLRQEGPRPERCSFSPWTEHRRCRQRACGLLTAEGEEWQRLRSLLAPLLLRPQAAARYAGTLNNVVCDLVRRLRRQRGRGTGPPALVRDVAGEFYKFGLEGIAAVLLGSRLGCLEAQVPPDTETFIRAVGSVFVSTLLTMAMPHWLRHLVPGPWGRLCRDWDQMFAFAQRHVERREAEAAMRNGGQPEKDLESGAHLTHFLFREELPAQSILGNVTELLLAGVDTVSNTLSWALYELSRHPEVQTALHSEITAALSPGSSAYPSATVLSQLPLLKAVVKEVLRLYPVVPGNSRVPDKDIHVGDYIIPKNTLVTLCHYATSRDPAQFPEPNSFRPARWLGEGPTPHPFASLPFGFGKRSCMGRRLAELELQMALAQILTHFEVQPEPGAAPVRPKTRTVLVPERSINLQFLDR
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Molecular Weight
56.5 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
Protein Description
CYP27B1, a member of the cytochrome P450 superfamily, plays a crucial role in the hydroxylation of vitamin D metabolites, converting 25-hydroxyvitamin D to its active form, 1,25-dihydroxyvitamin D. This bioactive form is essential for calcium homeostasis, bone health, and immune function. Dysregulation of CYP27B1 is linked to various diseases, including rickets, osteomalacia, and certain autoimmune disorders. Research into recombinant CYP27B1 provides valuable insights into its enzymatic mechanisms and biological functions, with implications for understanding vitamin D metabolism and its therapeutic potential. Recombinant protein technology allows for the production of active CYP27B1 in heterologous systems, enabling high-throughput studies into its enzymatic activity and regulation. Furthermore, studying CYP27B1 can shed light on its role in various physiological and pathological contexts, paving the way for novel therapeutic strategies in diseases associated with vitamin D deficiency or resistance. The recombinant protein serves as a critical tool for drug development and understanding the pharmacogenomics of vitamin D metabolism, as well as the development of supplements that can better modulate its activity.
