Analytical Data
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Gene name
PYCRL
- Application
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Alternative Names
PYCR3;PYCRL;Pyrroline-5-carboxylate reductase 3
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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
Q53H96
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Expression Region
1-274aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAAAEPS PRRVGFVGAG RMAGAIAQGL IRAGKVEAQH ILASAPTDRN LCHFQALGCR TTHSNQEVLQ SCLLVIFATK PHVLPAVLAE VAPVVTTEHI LVSVAAGVSL STLEELLPPN TRVLRVLPNL PCVVQEGAIV MARGRHVGSS ETNLLQHLLE ACGRCEEVPE AYVDIHTGLS GSGVAFVCAF SEALAEGAVK MGMPSSLAHR IAAQTLLGTA KMLLHEGQHP AQLRSDVCTP GGTTIYGLHA LEQGGLRAAT MSAVEAATCR AKELSRK
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Molecular Weight
31 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
PYCRL, or Pyrroline-5-carboxylate reductase-like protein, is a member of the pyrroline-5-carboxylate reductase family, which plays a crucial role in proline metabolism. This protein is believed to be involved in various physiological processes, including cellular stress responses and nitric oxide signaling. The study of PYCRL has gained attention due to its potential implications in several pathological conditions, such as neurodegenerative diseases and cancer, where proline metabolism is often dysregulated. Understanding the structure and function of PYCRL could provide insights into its role in cellular homeostasis and vulnerability to oxidative stress. Furthermore, the recombinant expression of PYCRL allows for detailed biochemical characterization, which can elucidate its enzymatic properties and regulatory mechanisms. These studies are essential for exploring PYCRL as a potential therapeutic target or biomarker in diseases linked to metabolic dysregulation, highlighting the importance of this protein in both basic and applied biomedical research.
