Analytical Data
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Gene name
RPIA
- Application
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Alternative Names
RPIA;RPI;Ribose-5-phosphate isomerase
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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
P49247
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Expression Region
1-311aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMQRPGPFSTLYGRVLAPLPGRAGGAASGGG GNSWDLPGSHVRLPGRAQSGTRGGAGNTSTSCGDSNSICPAPSTMSKAEE AKKLAGRAAVENHVRNNQVLGIGSGSTIVHAVQRIAERVKQENLNLVCIP TSFQARQLILQYGLTLSDLDRHPEIDLAIDGADEVDADLNLIKGGGGCLT QEKIVAGYASRFIVIADFRKDSKNLGDQWHKGIPIEVIPMAYVPVSRAVS QKFGGVVELRMAVNKAGPVVTDNGNFILDWKFDRVHKWSEVNTAIKMIPG VVDTGLFINMAERVYFGMQDGSVNMREKPFC
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Molecular Weight
35 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
Research into RPIA (Ribose-5-phosphate isomerase A) has gained significant attention due to its critical role in the pentose phosphate pathway (PPP), which is essential for cellular metabolism and biosynthesis. RPIA catalyzes the reversible isomerization of ribose-5-phosphate and ribulose-5-phosphate, thereby facilitating the generation of nucleotides and nucleic acids, crucial for cell growth and proliferation. Aberrant regulation of this enzyme has been implicated in various diseases, including cancer and metabolic disorders, making it a potential therapeutic target. Moreover, elucidating the structural and functional characteristics of RPIA can provide insights into its enzymatic mechanisms and the regulatory networks within the PPP. Recent advances in protein engineering and structural biology techniques have enabled researchers to study RPIA in greater detail, paving the way for the development of RPIA inhibitors that could modulate its activity for therapeutic benefits. Understanding the dynamics of RPIA also holds promise for enhancing the efficiency of biotechnological applications, such as improving the production of biofuels and biochemicals through engineered metabolic pathways. Overall, the comprehensive study of RPIA's structure-function relationship is vital for the development of novel strategies to combat diseases related to cellular metabolism and could have far-reaching implications in both health and industry.
