Analytical Data
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Gene name
PRXL2A
- Application
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Alternative Names
Peroxiredoxin-like 2 activated in M-CSF stimulated monocytes (Protein PAMM) (Redox-regulatory protein FAM213A) (C10orf58) (FAM213A) (PAMM)
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9BRX8
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Expression Region
1-229aa
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Molecular Weight
33.2 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
PRXL2A is a member of the pyridoxal phosphate-dependent enzyme family that has garnered interest in both basic research and potential therapeutic applications due to its role in cellular processes. Research indicates that PRXL2A is involved in various biological functions, including the regulation of oxidative stress, modulating cellular responses to inflammatory signals, and influencing metabolic pathways. The protein’s unique structure, characterized by its conserved domains, suggests a mechanism that may be crucial in maintaining cellular homeostasis. Moreover, abnormalities in PRXL2A expression or function have been associated with several diseases, including neurodegenerative disorders and cancer, highlighting its potential as a biomarker or therapeutic target. The study of recombinant PRXL2A protein allows researchers to better understand its biochemical properties and interactions within the cell, facilitating the exploration of its physiological roles. By producing this protein in a recombinant system, scientists can perform detailed analyses, including enzymatic activity, binding affinity, and structural studies, to elucidate the underlying mechanisms by which PRXL2A exerts its effects. Understanding these mechanisms is essential for developing strategies to modulate PRXL2A activity, which could lead to novel interventions in diseases linked to its dysfunction. Continued research into PRXL2A and its recombinant form may unlock new insights into its biological significance and therapeutic potential in health and disease.
