Analytical Data
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Gene name
scaIM
- Application
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Alternative Names
N-4 cytosine-specific methyltransferase ScaI
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Species
Streptomyces caespitosus
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O52692
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Expression Region
1-304aa
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Molecular Weight
50.2 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
ScaIM (Scaffold Insulin-like Macromolecule) recombinant protein research has emerged as a significant area of interest in the field of biotechnology and therapeutic development. ScaIM proteins are designed to mimic insulin-like signaling pathways, playing crucial roles in cellular growth, metabolism, and maintenance of glucose homeostasis. Researchers are particularly focused on the potential applications of ScaIM in treating metabolic disorders such as diabetes and obesity, where insulin resistance is a prevalent issue. The development of recombinant ScaIM proteins not only enhances understanding of insulin-like mechanisms but also provides a platform for creating novel therapeutic agents with improved efficacy and safety profiles. Additionally, the production of these proteins through recombinant DNA technology allows for high yields and more consistent biological activity compared to traditional methods. As such, studies investigating the structure, function, and metabolic impacts of ScaIM proteins are critical for advancing our knowledge and developing innovative solutions for managing chronic metabolic conditions. With ongoing research exploring various modifications to enhance the stability and receptor affinity of these proteins, the potential for ScaIM as a groundbreaking treatment modality continues to expand, marking a promising frontier in the realm of metabolic disease management.
