Analytical Data
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Gene name
SLC16A1
- Application
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Alternative Names
MCT1; MCT; Monocarboxylate Transporter 1; Monocarboxylic Acid Transporter 1
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Species
Human
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Source
E. coli
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Tag
Two N- s, His- & SUMO-
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P53985
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Expression Region
Asn444~Val500
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Molecular Weight
20kDa
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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
SLC16A1, also known as monocarboxylate transporter 1 (MCT1), is a crucial membrane protein that facilitates the transport of monocarboxylates, such as lactate, pyruvate, and other metabolites, across cell membranes. Its role in cellular metabolism is vital for various physiological processes, including energy production, pH regulation, and cellular signaling. Recent research has highlighted the significance of SLC16A1 in multiple diseases, including cancers, where altered expression of this transporter contributes to the Warburg effect, enabling tumor cells to thrive in low-oxygen environments by favoring glycolysis and lactate production. Understanding the structural and functional characteristics of SLC16A1 through the study of recombinant protein is essential for elucidating its mechanisms of action and regulatory pathways. The development of recombinant SLC16A1 can pave the way for high-throughput screening of potential therapeutics, aimed at modulating its function to restore normal metabolic processes or inhibit tumor growth. Furthermore, investigating the interactions between SLC16A1 and its substrates can provide insights into its role in metabolic disorders and facilitate the identification of novel biomarkers for disease diagnosis and progression. The ongoing research into SLC16A1 not only enhances our understanding of its fundamental biological roles but also holds significant potential for therapeutic applications in metabolic diseases and cancer treatment.
