Analytical Data
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Gene name
PECR
- Application
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Alternative Names
PECR;SDR29C1;Peroxisomal trans-2-enoyl-CoA reductase
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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
Q9BY49
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Expression Region
1-303aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSHMASWAKGRSYLAPGLLQGQVAIVTGG ATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPPTKQARVIP IQCNIRNEEEVNNLVKSTLDTFGKINFLVNNGGGQFLSPAEHISSKGWHA VLETNLTGTFYMCKAVYSSWMKEHGGSIVNIIVPTKAGFPLAVHSGAARA GVYNLTKSLALEWACSGIRINCVAPGVIYSQTAVENYGSWGQSFFEGSFQ KIPAKRIGVPEEVSSVVCFLLSPAASFITGQSVDVDGGRSLYTHSYEVPD HDNWPKGAGDLSVVKKMKETFKEKAKL
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Molecular Weight
35 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
PECR (Peroxisomal-EVA1-Like Protein) is a member of the electron transport chain involved in the fatty acid oxidation process within peroxisomes. Its role is crucial for maintaining cellular energy homeostasis and lipid metabolism. Recent studies have highlighted PECR's potential involvement in various metabolic disorders, including obesity and diabetes, as well as its implications in neurodegenerative diseases. Given its pivotal functions, researchers have focused on characterizing the protein's structure, function, and regulatory mechanisms. Recombinant PECR proteins are being developed to explore their biochemical properties and interactions with other cellular components. These studies are significant for understanding how PECR contributes to overall metabolic regulation and for identifying potential therapeutic targets for conditions linked to peroxisomal dysfunction. Moreover, recombinant PECR can be used in high-throughput screening assays to discover small molecules that modulate its activity, providing insights into the development of innovative treatments for metabolic diseases. The ongoing research around PECR not only aims to elucidate its functional role but also emphasizes the broader implications of peroxisomal proteins in health and disease. As advancements in molecular biology tools continue, the production and analysis of PECR in various model systems will further illuminate its pathophysiological relevance, potentially leading to breakthroughs in clinical applications.
