Analytical Data
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Gene name
GRHPR
- Application
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Alternative Names
GLXR; glycerate 2 dehydrogenase ; GLYD; Glyoxylate reductase/hydroxypyruvate reductase; Grhpr; GRHPR_HUMAN; OTTHUMP00000021379; OTTHUMP00000021380; OTTHUMP00000046131; PH 2; PH2; Primary hyperoxaluria type 2
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UBQ7
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Expression Region
1-328aa
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AA Sequence
MRPVRLMKVFVTRRIPAEGRVALARAADCEVEQWDSDEPIPAKELERGVAGAHGLLCLLSDHVDKRILDAAGANLKVISTMSVGIDHLALDEIKKRGIRVGYTPDVLTDTTAELAVSLLLTTCRRLPEAIEEVKNGGWTSWKPLWLCGYGLTQSTVGIIGLGRIGQAIARRLKPFGVQRFLYTGRQPRPEEAAEFQAEFVSTPELAAQSDFIVVACSLTPATEGLCNKDFFQKMKETAVFINISRGDVVNQDDLYQALASGKIAAAGLDVTSPEPLPTNHPLLTLKNCVILPHIGSATHRTRNTMSLLAANNLLAGLRGEPMPSELKL
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Molecular Weight
61.82 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
The GRHPR (Glyoxylate Reductase/Hydroxypyruvate Reductase) protein plays a crucial role in the metabolic pathways of glyoxylate and hydrogen peroxide, primarily functioning in the liver where it helps convert glyoxylate to glycolate and hydroxypyruvate to glycerate. Deficiencies in GRHPR have been linked to primary hyperoxaluria type II, a genetic disorder characterized by excessive oxalate production, leading to kidney damage and systemic complications. Understanding the structure and function of GRHPR is vital for developing therapeutic strategies for such conditions. Recent studies have concentrated on the recombinant expression of GRHPR, allowing for detailed analysis of its enzymatic properties, structural characteristics, and regulatory mechanisms. This research not only elucidates the enzyme's role in metabolic processes but also provides insights into potential interventions for managing hyperoxaluria and related disorders. By utilizing recombinant DNA technology, researchers can produce large quantities of functional GRHPR, facilitating experiments that explore enzyme kinetics, substrate specificity, and interaction with various cofactors. Moreover, insights gained from these studies could pave the way for gene therapy approaches or the development of small molecule drugs aimed at restoring GRHPR function in affected individuals. Thus, the recombinant GRHPR research represents a promising frontier in understanding metabolic diseases and enhancing therapeutic options for managing disorders associated with oxalate metabolism.
