Analytical Data
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Gene name
SORD
- Application
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Alternative Names
SORD;Sorbitol dehydrogenase
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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
Q00796
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Expression Region
2-357aa
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AA Sequence
AAAAKPNNL SLVVHGPGDL RLENYPIPEP GPNEVLLRMH SVGICGSDVH YWEYGRIGNF IVKKPMVLGH EASGTVEKVG SSVKHLKPGD RVAIEPGAPR ENDEFCKMGR YNLSPSIFFC ATPPDDGNLC RFYKHNAAFC YKLPDNVTFE EGALIEPLSV GIHACRRGGV TLGHKVLVCG AGPIGMVTLL VAKAMGAAQV VVTDLSATRL SKAKEIGADL VLQISKESPQ EIARKVEGQL GCKPEVTIEC TGAEASIQAG IYATRSGGNL VLVGLGSEMT TVPLLHAAIR EVDIKGVFRY CNTWPVAISM LASKSVNVKP LVTHRFPLEK ALEAFETFKK GLGLKIMLKC DPSDQNP
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Molecular Weight
40 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
SORD (sorbitol dehydrogenase) is an important enzyme involved in the polyol pathway, which is critical for maintaining carbohydrate metabolism, particularly in tissues that are sensitive to changes in glucose levels, such as the retina, kidneys, and nerves. The enzyme catalyzes the conversion of sorbitol to fructose, playing a key role in regulating osmotic pressure and preventing cellular damage due to hyperglycemia. Aberrant SORD activity has been linked to various diabetic complications, including diabetic retinopathy, neuropathy, and nephropathy, making it a target of interest for therapeutic interventions. Recent studies have focused on identifying the structure and function of SORD through recombinant protein technology, allowing researchers to produce purified SORD for biochemical characterization and drug discovery. Understanding the enzyme's structure-function relationship can provide insights into its catalytic mechanism and help in designing inhibitors or activators that regulate its activity. Additionally, research on SORD can contribute to biomarker discovery for early diagnosis of diabetes-related complications. Overall, the study of SORD and its recombinant protein form holds significant promise in enhancing our understanding of metabolic disorders and developing novel therapeutic strategies.
