Analytical Data
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Gene name
G537R
- Application
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Alternative Names
G537R
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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
P51654
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Expression Region
25-559aa
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AA Sequence
QPPPPPPDATCHQVRSFFQRLQPGLKWVPETPVPGSDLQVCLPKGPTCCSRKMEEKYQLTARLNMEQLLQSASMELKFLIIQNAAVFQEAFEIVVRHAKNYTNAMFKNNYPSLTPQAFEFVGEFFTDVSLYILGSDINVDDMVNELFDSLFPVIYTQLMNPGLPDSALDINECLRGARRDLKVFGNFPKLIMTQVSKSLQVTRIFLQALNLGIEVINTTDHLKFSKDCGRMLTRMWYCSYCQGLMMVKPCGGYCNVVMQGCMAGVVEIDKYWREYILSLEELVNGMYRIYDMENVLLGLFSTIHDSIQYVQKNAGKLTTTIGKLCAHSQQRQYRSAYYPEDLFIDKKVLKVAHVEHEETLSSRRRELIQKLKSFISFYSALPGYICSHSPVAENDTLCWNGQELVERYSQKAARNGMKNQFNLHELKMKGPEPVVSQIIDKLKHINQLLRTMSMPKGRVLDKNLDEEGFESGDCGDDEDECIGGSGDGMIKVKNQLRFLAELAYDLDVDDAPRNSQQATPKDNEISTFHNLGNVH
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Molecular Weight
65.0 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 G537R recombinant protein has garnered significant attention in the realm of molecular biology and biochemistry due to its implications in understanding various disease mechanisms and potential therapeutic applications. This variant, a mutation of a specific protein, has been associated with altered functionality that may contribute to the progression of certain pathologies, including neurodegenerative diseases and cancers. Research into the G537R mutation aims to elucidate the structural and functional consequences that arise from this alteration. By analyzing the properties of the G537R protein, scientists hope to uncover insights into its role in cellular processes, as well as to identify potential molecular targets for drug development. Moreover, generating this recombinant protein allows for detailed studies using various biophysical and biochemical techniques, enabling researchers to characterize its interaction with other biomolecules and to understand the downstream effects of its expression. This research is crucial not only for the fundamental understanding of protein dynamics and function but also for paving the way towards innovative therapeutic strategies that could mitigate the effects of diseases linked to the G537R mutation. As the field of protein engineering evolves, the study of such mutants becomes increasingly relevant, providing a clearer picture of how specific genetic variations impact health and disease at the molecular level. Overall, the exploration of G537R recombinant protein presents an exciting avenue for scientific inquiry, linking basic research to the potential for clinical advancements.
