Analytical Data
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Gene name
IGFALS
- Application
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Alternative Names
ALS
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P35858
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Expression Region
Ala28~Cys605
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Molecular Weight
60kDa
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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
IGFALS (Insulin-like Growth Factor Acid-Labile Subunit) is a crucial component of the insulin-like growth factor (IGF) system, which plays a significant role in cell growth, development, and metabolism. It primarily functions by stabilizing the circulating IGF complex, thus prolonging the half-life of IGFs in the bloodstream. The investigation of IGFALS recombinant protein has gained considerable attention in the context of understanding its physiological and pathological roles, particularly in growth disorders, metabolic syndromes, and certain cancers. Given its intricate involvement in the endocrine regulation of growth and its interactions with other IGF-binding proteins, researchers are exploring the potential of IGFALS as a therapeutic target. Furthermore, the generation of recombinant IGFALS provides valuable tools for studying its structure-function relationships and its impacts on IGF signaling pathways. Advances in recombinant DNA technology have enabled the production of IGFALS with enhanced purity and activity, facilitating in vitro and in vivo studies. This research not only contributes to elucidating the fundamental mechanisms underlying growth regulation but also paves the way for potential clinical applications in treating diseases associated with IGF dysregulation. Overall, the exploration of IGFALS recombinant protein holds promise for advancing our understanding of growth biology and developing novel therapeutic strategies.
