Analytical Data
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Gene name
SPR
- Application
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Alternative Names
SPR;Sepiapterin 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
P35270
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Expression Region
1-261aa
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AA Sequence
MEGGLGRAVCLLTGASRGFGRTLAPLLASLLSPGSVLVLSARNDEALRQLEAELGAERSGLRVVRVPADLGAEAGLQQLLGALRELPRPKGLQRLLLINNAGSLGDVSKGFVDLSDSTQVNNYWALNLTSMLCLTSSVLKAFPDSPGLNRTVVNISSLCALQPFKGWALYCAGKAARDMLFQVLALEEPNVRVLNYAPGPLDTDMQQLARETSVDPDMRKGLQELKAKGKLVDCKVSAQKLLSLLEKDEFKSGAHVDFYDK
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Molecular Weight
75.8 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
SPR (Surface Plasmon Resonance) has emerged as a pivotal technology in the study of biomolecular interactions, particularly for recombinant proteins. Recombinant proteins, produced through genetic engineering techniques, are fundamental in various applications including therapeutics, diagnostics, and research. The ability to analyze the real-time interaction dynamics of these proteins with other biomolecules is crucial for understanding their functional mechanisms. SPR provides a label-free, sensitive method for monitoring these interactions by measuring changes in refractive index near a sensor surface, enabling the determination of binding kinetics and affinities. This technology facilitates the screening of protein-protein, protein-ligand, and protein-DNA interactions, paving the way for drug discovery and design. Recent advancements in SPR instrumentation, such as enhanced sensitivity and multiplexing capabilities, have further expanded its application spectrum. Understanding how recombinant proteins interact within biological systems not only informs the development of novel therapeutics but also aids in the design of protein-based biosensors and biomaterials. As such, the integration of SPR in recombinant protein research represents a significant advancement in the field of molecular biology and biochemistry, contributing to innovative solutions for contemporary health and scientific challenges.
