Analytical Data
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Gene name
GLYCAM1
- Application
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Alternative Names
GLYCAM1；Carbohydrate sulfotransferase 4
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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
Q8IVK1
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Expression Region
1-47aa
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AA Sequence
MKFFMVLLPASLASTSLAILDVESGLLPQLSVLLSNRLRGKTCQTGP
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Molecular Weight
5.1kDa
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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, a member of the Glycosylation-Associated Protein family, plays a crucial role in the immune system and cellular processes. It is primarily expressed in various tissues, including the brain and immune cells, and has been implicated in modulating cell signaling, adhesion, and migration. The protein's structure features unique glycosylation patterns that influence its function and interactions with other biomolecules. Research has shown that GLYCAM1 is involved in various pathological conditions, including autoimmune diseases and cancer, highlighting its potential as a therapeutic target. Understanding the molecular mechanisms underpinning GLYCAM1's role is essential for developing new diagnostic and treatment strategies. Recent advancements in recombinant protein technologies have enabled the production of GLYCAM1 in significant quantities, allowing for detailed studies of its biochemical properties and interactions. This research aims not only to unravel the complexities of GLYCAM1's functions but also to explore its implications in health and disease, paving the way for innovative approaches in targeted therapies. The ongoing exploration of GLYCAM1 holds promise for enhancing our understanding of glycosylation in biological processes and its potential impact on human health.
