Analytical Data
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Gene name
prpL
- Application
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Alternative Names
prpL；WASPIP；WIP；WAS/WASL-interacting Protein family member 1
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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
Q9HWK6
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Expression Region
212-462aa
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AA Sequence
AGYRDGFGASGSCEVDAVCATQSGTRAYDNATAAVAKMVFTSSADGGSYICTGTLLNNGNSPKRQLFWSAAHCIEDQATAATLQTIWFYNTTQCYGDASTINQSVTVLTGGANILHRDAKRDTLLLELKRTPPAGVFYQGWSATPIANGSLGHDIHHPRGDAKKYSQGNVSAVGVTYDGHTALTRVDWPSAVVEGGSSGSGLLTVAGDGSYQLRGGLYGGPSYCGAPTSQRNDYFSDFSGVYSQISRYFAP
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Molecular Weight
42.4 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
PRPL (phosphoribulokinase-like) recombinant proteins have gained significant attention in recent years due to their potential applications in various fields, including biotechnology, agriculture, and medicine. The PRPL gene family, primarily known for its role in photosynthesis, encodes enzymes that catalyze essential biochemical reactions. Researchers have been particularly interested in characterizing PRPL proteins due to their unique structural and functional properties, which may provide insights into the regulation of metabolic pathways in plants. Moreover, the reconstitution of these proteins through recombinant DNA technology allows for the production of large quantities of PRPL for detailed biochemical studies and potential commercial applications. Advances in genetic engineering techniques, combined with a deeper understanding of plant metabolic functions, have led to intensified research efforts aimed at exploring the functional attributes of PRPL proteins, including their influence on plant growth, stress responses, and overall productivity. With the increasing demand for sustainable agricultural practices and high-yield crop varieties, the investigation of PRPL proteins could pave the way for innovative solutions to enhance plant performance under varying environmental conditions. Overall, the study of PRPL recombinant proteins represents a promising frontier in biological research, with implications that extend beyond basic science into practical agricultural advancements.
