Analytical Data
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Gene name
SEPP1
- Application
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Alternative Names
SEPP1；SELP；SEPP1；SelenoProtein P
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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
P49908
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Expression Region
20-381aa
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AA Sequence
ESQDQSSLCKQPPAWSIRDQDPMLNSNGSVTVVALLQASSYLCILQASKL EDLRVKLKKEGYSNISYIVVNHQGISSRLKYTHLKNKVSEHIPVYQQEEN QTDVWTLLNGSKDDFLIYDRCGRLVYHLGLPFSFLTFPYVEEAIKIAYCE KKCGNCSLTTLKDEDFCKRVSLATVDKTVETPSPHYHHEHHHNHGHQHLG SSELSENQQPGAPNAPTHPAPPGLHHHHKHKGQHRQGHPENRDMPASEDL QDLQKKLCRKRCINQLLCKLPTDSELAPRSSCCHCRHLIFEKTGSAITSQ CKENLPSLCSSQGLRAEENITESCQSRLPPAASQISQQLIPTEASASSRS KNQAKKSESPSN
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Molecular Weight
45 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
SEPP1, or Selenoprotein P, is a unique protein primarily characterized by its selenium content, playing a crucial role in selenium transport and homeostasis within the body. Its research background dates back to the recognition of selenium as an essential micronutrient with antioxidant properties, integral to various biological functions. SEPP1 is primarily produced in the liver and is secreted into the bloodstream, where it transports selenium to various tissues, thus influencing antioxidant defense systems and promoting overall health. Studies have indicated that SEPP1 may also be linked to various diseases, including cardiovascular disorders, neurodegenerative conditions, and cancer, highlighting its potential as a biomarker for these diseases. Furthermore, SEPP1 has garnered attention in the context of selenium deficiency, which has been associated with adverse health outcomes. Recent advancements in recombinant DNA technology have enabled the production of SEPP1 in a laboratory setting, thereby facilitating more in-depth studies into its structure, function, and therapeutic potential. Understanding the mechanisms behind SEPP1's actions could lead to novel approaches in treating diseases related to oxidative stress and selenium dysregulation. This growing interest in SEPP1 underscores its importance not only as a vital protein in human physiology but also as a promising target for future biomedical research and therapeutic interventions.
