Analytical Data
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Gene name
GLYCAM1
- Application
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Alternative Names
(GlyCAM-1)(Lactophorin)(Whey protein)
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Species
Lama glama
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Source
E. coli
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Tag
N- His-KSI
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P83315
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Expression Region
1-18aa
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Molecular Weight
17.4 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
GLYCAM1 is a critical glycoprotein that plays a significant role in cellular interactions, particularly in the adhesion and migration of immune cells. It serves as a ligand for specific receptors on leukocytes, influencing processes such as inflammation and immune response. The study of GLYCAM1 has gained prominence due to its implications in various diseases, including autoimmune disorders and cancer, where aberrant glycosylation patterns may contribute to disease progression. Recombinant GLYCAM1 protein has become a valuable tool for elucidating its biological functions and interactions at the molecular level. Researchers utilize recombinant techniques to produce GLYCAM1 in controlled settings, enabling detailed investigations into its structure-function relationships. This recombinant approach allows for the examination of glycosylation variants and their effects on cell signaling pathways. Understanding the precise mechanisms by which GLYCAM1 interacts with its receptors can provide insights into novel therapeutic targets and strategies in disease management. Overall, the research surrounding GLYCAM1 not only enhances our fundamental knowledge of glycoprotein biology but also holds promise for advancing medical interventions in glycan-related pathologies.
