Analytical Data
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Gene name
SLC22A5
- Application
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Alternative Names
High-affinity sodium-dependent carnitine cotransporter;Organic cation/carnitine transporter 2
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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
O76082
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Expression Region
42-142 aa
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AA Sequence
LIATPEHRCRVPDNLSSAWRNHTVPLRLRDGREVPHSCRRYRLATIANFSALGLEPGRDVDLGQLEQESCLDGWEFSQDVYLSTIVTEWNLVCEDDWKA
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Molecular Weight
18.4 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
Related Products
Protein Description
SLC22A5, also known as the carnitine transporter OCTN2, plays a crucial role in the cellular uptake of carnitine, a vital molecule for fatty acid oxidation and energy production. Mutations in the SLC22A5 gene can lead to primary carnitine deficiency, a metabolic disorder characterized by impaired fatty acid metabolism, muscle weakness, hypoglycemia, and cardiomyopathy. Given its significant impact on health, researchers have focused on characterizing and producing recombinant SLC22A5 protein to better understand its molecular structure, transport mechanisms, and interactions with substrates and inhibitors. The expression of SLC22A5 in heterologous systems, such as yeast or mammalian cells, allows for the generation of functionally active protein for detailed biochemical analyses. These studies not only enhance our comprehension of the physiological role of SLC22A5 in carnitine transport but also pave the way for potential therapeutic interventions in related metabolic disorders. Furthermore, understanding the structure-function relationship of SLC22A5 can aid in drug design to modulate its activity or to develop treatment strategies for individuals with SLC22A5-related conditions. Overall, research on recombinant SLC22A5 is pivotal for unraveling the complexities of carnitine transport and its implications for human health.
