Analytical Data
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Gene name
UGDH
- Application
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Alternative Names
GDH; UDP Glc dehydrogenase; UDP GlcDH; UDP glucose 6 dehydrogenase; UDP glucose dehydrogenase; UDP-Glc dehydrogenase; UDP-GlcDH; UDP-glucose 6-dehydrogenase; UDP-glucose dehydrogenase; UDPGDH; UGD; Ugdh; UGDH_HUMAN; Uridine diphospho glucose dehydrogenase
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O60701
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Expression Region
1-494aa
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Molecular Weight
71 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
UGDH (UDP-glucose 6-dehydrogenase) is a pivotal enzyme in the uridine diphosphate (UDP)-glucuronate pathway, which plays a crucial role in the biosynthesis of glycosaminoglycans and proteoglycans. These macromolecules are fundamental for various biological processes, including cell signaling, differentiation, and maintenance of the extracellular matrix. Dysregulation of UGDH has been associated with several pathological conditions, such as congenital disorders and cancers, making it a target of interest in biomedical research. The study of recombinant UGDH protein allows for detailed investigation into its enzymatic mechanisms, structural properties, and potential regulatory roles in metabolic pathways. By employing techniques such as protein expression in heterologous systems and subsequent purification, researchers aim to elucidate the functional dynamics of UGDH. Additionally, understanding the enzyme's structure-function relationships could pave the way for the development of novel therapeutic strategies to modulate its activity in disease contexts. Current research endeavors also include exploring the potential of UGDH as a biomarker for specific diseases and its implications in drug development, highlighting its importance in both fundamental and applied biomedical research.
