Analytical Data
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Gene name
DDH2
- Application
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Alternative Names
AKR1C2; DD; BABP; DD2; HAKRD; MCDR2; Aldo-Keto Reductase Family 1,Member C2; Bile Acid Binding Protein; 3-Alpha Hydroxysteroid Dehydrogenase Type III
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Species
Human
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Source
E. coli
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Tag
N-6His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P52895
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Expression Region
1~323aa
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Molecular Weight
42kDa
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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
Identification
Protein Description
DDH2, also known as delta-1-pyrroline-5-carboxylate dehydrogenase 2, is an enzyme implicated in proline metabolism, which plays a crucial role in cellular responses to stress and regulation of osmotic homeostasis. Research on DDH2 recombinantly expressed proteins has garnered attention due to their potential applications in various fields, including agriculture, biotechnology, and medicine. Understanding the structure and function of DDH2 is vital for elucidating its role in stress responses, particularly in plants and mammalian systems. Recombinant DDH2 proteins can be engineered to enhance their catalytic efficiency or stability, making them valuable for experimental studies that aim to investigate metabolic pathways involving proline and its derivatives. Furthermore, insights gained from this research could contribute to developing crops with improved resilience to environmental stressors, addressing food security issues exacerbated by climate change. Additionally, by exploring DDH2's involvement in human diseases, such as neurodegenerative disorders, researchers can pave the way for novel therapeutic strategies. Thus, the study of DDH2 recombinant proteins not only enhances our fundamental understanding of metabolic processes but also opens up new avenues for practical applications in improving health and environmental resilience.
