Analytical Data
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Gene name
SLC30A8
- Application
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Alternative Names
Solute carrier family 30 member 8 (ZNT8)
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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
Q8IWU4
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Expression Region
267-369aa
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Molecular Weight
18.8 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
SLC30A8, a member of the SLC (solute carrier) family, encodes a zinc transporter predominantly expressed in pancreatic beta cells, where it plays a crucial role in insulin secretion and glucose homeostasis. Genetic studies have identified SLC30A8 as a significant risk factor for type 2 diabetes, with certain polymorphisms associated with increased susceptibility to the disease. The protein facilitates the transport of zinc ions, which are essential for insulin crystallization and storage within secretory granules. Understanding the functional mechanisms of SLC30A8 and its influence on beta-cell function is vital for elucidating the pathophysiology of diabetes. Research has increasingly focused on the recombinant expression of SLC30A8 to explore its structure-function relationships, enabling the investigation of how specific mutations might affect protein activity. Recent advances in techniques such as X-ray crystallography and cryo-electron microscopy have provided insights into its molecular architecture, further guiding therapeutic interventions. By studying the recombinant protein in various cellular contexts, researchers aim to identify potential targets for drug development, paving the way for novel strategies to combat type 2 diabetes.
