Analytical Data
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Gene name
GNL2
- Application
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Alternative Names
Autoantigen NGP-1
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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
Q13823
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Expression Region
1-731aa
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Molecular Weight
99.7 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
GNL2, or Guanine nucleotide-binding protein-like 2, is a member of the GTPase family and plays a vital role in various cellular processes, including ribosome biogenesis, cellular proliferation, and stress response. Its involvement in multiple biological pathways makes GNL2 a key player in cellular homeostasis. Recent studies have indicated that GNL2 is overexpressed in several types of cancers, suggesting a potential link to tumorigenesis and making it a promising target for cancer research. The functional characterization of GNL2, particularly through the study of its recombinant protein, is essential to elucidate its specific roles within the cell and its mechanisms of action. By producing and analyzing GNL2 recombinant proteins, researchers aim to gain insights into its biochemical properties, interacting partners, and regulatory mechanisms, which could potentially open avenues for therapeutic interventions in cancer and other diseases associated with GNL2 dysregulation. Given the rising interest in targeting GTPases in cancer treatment, understanding GNL2 through recombinant protein studies could contribute significantly to the field of cancer biology and targeted therapy.
