Analytical Data
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Gene name
GML
- Application
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Alternative Names
GML；LY6DL；Glycosyl-phosphatidylinositol-anchored molecule-like Protein
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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
Q99445
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Expression Region
18-158aa
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AA Sequence
SAT MRAQWTYSLR CHDCAVINDF NCPNIRVCPY HIRRCMTISI RINSRELLVY KNCTNNCTFV YAAEQPPEAP GKIFKTNSFY WVCCCNSMVC NAGGPTNLER DMLPDEVTEE ELPEGTVRLG VSKLLLSFAS IIVSNILP
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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
The study of GML (Glycosylation-Mediated Ligands) recombination proteins arises from the growing interest in glycosylation's role in various biological processes, including cell signaling, immune response, and protein stability. Glycosylation is a post-translational modification where carbohydrates are added to proteins, significantly influencing their structure and function. Research has shown that glycosylation can affect protein folding, enhance stability, and influence interactions with other biomolecules, making it critical in biopharmaceutical development and therapeutic applications. The employment of recombinant DNA technology allows for the production of GML proteins with specific glycosylation patterns, facilitating detailed studies into their functional implications. By examining the effects of glycosylation on protein activity, researchers aim to design more effective drugs and biomolecules tailored to overcome challenges in treatment efficacy and specificity. This field of study also holds promise for advancements in vaccine development, where glycosylated antigens could enhance immunogenicity. As our understanding of GML recombination proteins advances, we foresee significant contributions to biotechnology and medicine, including improved diagnostic tools and novel therapeutic strategies aimed at combating various diseases.
