Analytical Data
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Gene name
SLC35F3
- Application
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Alternative Names
(Solute carrier family 35 member F3)
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8IY50
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Expression Region
1-66aa
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Molecular Weight
14.5 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
SLC35F3 is a member of the solute carrier (SLC) family, which is known for its role in the transport of various substrates across cellular membranes. This particular protein has garnered attention due to its potential involvement in important biological processes, such as nucleotide sugar transport, which is crucial for glycosylation—the modification of proteins and lipids by carbohydrate additions. Aberrations in glycosylation are linked to various diseases, including cancer and genetic disorders. Initial studies indicate that SLC35F3 might play a role in cellular stress responses and the maintenance of cellular homeostasis, further highlighting its significance in modeling cellular function. Furthermore, the exploration of SLC35F3 as a recombinant protein offers the potential for understanding its structure-function relationships, which could illuminate its mechanistic roles in human health and disease. Research into SLC35F3 may provide insights into novel therapeutic targets and strategies, particularly in diseases that exhibit altered glycosylation patterns. Understanding the biochemical pathways involving SLC35F3 could lead to advancements in drug design and the development of biomolecular tools, thereby underscoring the importance of this protein in both basic and applied biomedical research.
