Analytical Data
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Gene name
IMPDH2
- Application
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Alternative Names
IMP dehydrogenase 2; IMPD 2; IMPDH 2
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Species
Human
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Source
E. coli
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Tag
C-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P12268
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Expression Region
L5-F514
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Protein Length
Partial
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Molecular Weight
62 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
IMPDH2 (Inosine Monophosphate Dehydrogenase 2) is a crucial enzyme involved in the de novo synthesis of purine nucleotides, playing a significant role in cellular proliferation and immune responses. Its importance is underscored by its involvement in various physiological and pathological processes, including cancer, where its overexpression can lead to uncontrolled cell growth. The interest in IMPDH2 has surged due to its potential as a therapeutic target, particularly in the development of immunosuppressive drugs for organ transplantation and treatments for autoimmune diseases. Additionally, scientists have been exploring its structure and function through recombinant protein studies to better understand its enzymatic mechanisms and interaction with potential inhibitors. The expression of recombinant IMPDH2 facilitates high-throughput screening of small molecules that may serve as effective inhibitors, ultimately aiming to provide new avenues for therapeutic interventions. Understanding the biochemistry of IMPDH2 at the molecular level can pave the way for novel drug designs and strategies to combat conditions linked with abnormal purine metabolism, making it a focal point of research in both biochemistry and pharmacology.











