Analytical Data
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Gene name
PYCR1
- Application
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Alternative Names
PYCR1;Pyrroline-5-carboxylate reductase 1. 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
P32322
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Expression Region
1-319aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMSVGFIGAGQLAFALAKGFTAAGVLAAHKI MASSPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD EIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPAPRVIRCMTNTPVVVRE GATVYATGTHAQVEDGRLMEQLLSSVGFCTEVEEDLIDAVTGLSGSGPAY AFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDN VSSPGGATIHALHVLESGGFRSLLINAVEASCIRTRELQSMADQEQVSPA AIKKTILDKVKLDSPAGTALSPSGHTKLLPRSLAPAGKD
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Molecular Weight
36 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
PYCR1, or pyrroline-5-carboxylate reductase 1, is an enzyme that plays a crucial role in the proline biosynthetic pathway, which is essential for maintaining cellular homeostasis, particularly under stress conditions. Research has indicated that PYCR1 is involved in the conversion of pyrroline-5-carboxylate to proline, an amino acid that serves as an important osmoprotectant, antioxidant, and regulator of cellular signaling. Dysregulation of PYCR1 has been linked to various pathological conditions, including metabolic disorders, neurodegenerative diseases, and cancer, highlighting its significance in cellular health and disease. The study of recombinant PYCR1 protein has gained traction as it provides insights into its biochemical properties, functional mechanisms, and potential therapeutic applications. Understanding the structure-function relationship of PYCR1 at a molecular level can unveil targets for drug development and interventions in related diseases. Moreover, recombinant PYCR1 can serve as a valuable tool in metabolic engineering and synthetic biology, allowing for the manipulation of proline metabolism in various organisms. Investigating this protein can therefore contribute to a broader understanding of metabolic pathways and their implications in health and disease management.
