Analytical Data
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Gene name
Glxr
- Application
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Alternative Names
Glxr;GLXR;Glyoxylate reductase/hydroxypyruvate reductase
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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
Q9UBQ7
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Expression Region
1-328aa
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AA Sequence
MRPVRLMKVF VTRRIPAEGR VALARAADCE VEQWDSDEPI PAKELERGVA GAHGLLCLLS DHVDKRILDA AGANLKVIST MSVGIDHLAL DEIKKRGIRV GYTPDVLTDT TAELAVSLLL TTCRRLPEAI EEVKNGGWTS WKPLWLCGYG LTQSTVGIIG LGRIGQAIAR RLKPFGVQRF LYTGRQPRPE EAAEFQAEFV STPELAAQSD FIVVACSLTP ATEGLCNKDF FQKMKETAVF INISRGDVVN QDDLYQALAS GKIAAAGLDV TSPEPLPTNH PLLTLKNCVI LPHIGSATHR TRNTMSLLAA NNLLAGLRGE PMPSELKL
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Molecular Weight
35.6 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
GLXR (glutathione-dependent peroxidase-like protein) is a novel protein that has garnered significant attention in the field of molecular biology and biochemistry due to its potential role in oxidative stress response and cellular signaling pathways. Research indicates that GLXR, similar to glutathione peroxidases, may help in the detoxification of reactive oxygen species (ROS), which are implicated in various pathological conditions, including cancer, neurodegenerative diseases, and aging. The re-structuring of GLXR through recombinant DNA technology has enabled scientists to produce this protein in host systems, allowing for detailed studies of its structure-function relationships, enzymatic activity, and interactions with other cellular components. Understanding the molecular mechanisms by which GLXR operates could provide new insights into its physiological and pathological roles, further establishing its potential as a therapeutic target. The ongoing research aims to elucidate the regulatory mechanisms of GLXR expression and activity, along with its implications in disease contexts, paving the way for innovative approaches in disease prevention and treatment.











