Analytical Data
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Gene name
gam
- Application
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Alternative Names
gam；AES；GRG；GRG5；TLE family member 5
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Species
E.coli
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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
P03702
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Expression Region
1-138aa
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AA Sequence
MDINTETEIKQKHSLTPFPVFLISPAFRGRYFHSYFRSSAMNAYYIQDRLEAQSWARHYQQLAREEKEAELADDMEKGLPQHLFESLCIDHLQRHGASKKSITRAFDDDVEFQERMAEHIRYMVETIAHHQVDIDSEV
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Molecular Weight
23.8 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 research on glycosylphosphatidylinositol (GPI)-anchored proteins, particularly GPI-anchored proteins like GnT1 and GPI-specific phospholipase D, has gained significant attention due to their critical roles in cell signaling, immune response, and development. These proteins are synthesized in the endoplasmic reticulum and are anchored to the cell membrane by a GPI moiety, which provides stability and facilitates interactions with various cellular components. In recent years, studies have increasingly focused on the functional mechanisms of GPI-anchored proteins, including their involvement in pathophysiological conditions such as cancer and infectious diseases. Their unique structural characteristics and dynamic roles in cellular processes make them attractive targets for therapeutic intervention. Researchers have also explored methods for isolating and characterizing these proteins, which has advanced our understanding of their biological significance and potential as biomarkers or therapeutic targets. As a result, ongoing investigations into GPI-anchored proteins aim to unravel their complex biological functions and therapeutic potential, paving the way for innovative strategies in disease diagnosis and treatment. Overall, the study of GPI-anchored proteins represents a promising frontier in biomedical research, with implications that extend from basic science to clinical applications.
