Analytical Data
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Gene name
GML
- Application
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Alternative Names
LY6DL; GPI Anchored Molecule Like Protein
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q99445
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Expression Region
Met21~Pro158
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Molecular Weight
46kDa
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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
Related Products
Protein Description
GML (Glycoprotein Murine Leukemia) recombinant protein research has gained significant attention in recent years due to its potential implications in immunology and cancer therapy. GML is a glycoprotein derived from murine leukemia virus, which exhibits unique biological properties, including the ability to activate immune responses. Researchers have identified that GML can enhance the activity of various immune cells, making it a promising candidate for developing novel immunotherapeutic strategies. The recombinant production of GML enables detailed studies into its structure-function relationships and facilitates the exploration of its mechanisms in modulating immune responses. Moreover, as cancer cells often express aberrant glycoproteins, the characterization of GML can provide insights into tumor immunology and help design targeted therapies aimed at harnessing the immune system to eliminate cancer cells. Overall, the study of GML recombinant protein is poised to contribute significantly to the fields of vaccine development, cancer immunotherapy, and understanding immune system dynamics, making it a focal point for ongoing research and clinical applications.
