Analytical Data
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Gene name
SLC7A7-SLC3A2
- Application
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Alternative Names
SLC3A2; CD98HC; 4F2; 4F2HC; 4T2HC; MDU1; NACAE; Activators Of Dibasic And Neutral Amino Acid Transport; Antigen Identified By Monoclonal Antibodies 4F2; CD98 Heavy Chain
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Species
Mouse
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P10852
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Expression Region
Ile285~Gln521
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Molecular Weight
56kDa
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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
SLC7A7 (System L Amino Acid Transporter 7) and SLC3A2 (a heavy chain subunit of the heterodimeric amino acid transporter) play pivotal roles in amino acid transport across cell membranes, which is essential for various cellular processes, including protein synthesis, cell signaling, and metabolic regulation. Mutations in SLC7A7 are linked to the genetic disorder lysinuric protein intolerance (LPI), characterized by impaired transport of basic amino acids, leading to severe metabolic disturbances. Understanding the functional dynamics of the SLC7A7-SLC3A2 complex is crucial for elucidating the mechanisms underlying amino acid transport and its implications for human health. The generation of recombinant proteins for these transporters provides a valuable tool for in-depth biochemical and structural studies, allowing researchers to dissect the intricate interactions and transport mechanisms involved. Utilizing such recombinant proteins could pave the way for novel therapeutic strategies targeting amino acid transport disorders, enhancing our understanding of metabolic diseases and contributing to the development of effective treatment options. Overall, the study of SLC7A7-SLC3A2 recombinant proteins serves as a critical foundation for advancing our knowledge in both basic and applied biomedical research.
