Analytical Data
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Gene name
IK
- Application
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Alternative Names
RED; RER; IK factor
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13123
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Expression Region
Met1~Pro192
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Molecular Weight
62kDa
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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
The study of the IK (intermediate filament keratin) protein family has garnered significant attention due to their crucial roles in cellular structure and function. Intermediate filaments, which include keratins, are integral components of the cytoskeletal framework, providing mechanical stability and contributing to the integrity of epithelial cells. The IK proteins are particularly interesting because they are involved in various biological processes, including cell differentiation, proliferation, and response to stress. Dysregulation of these proteins has been linked to a range of diseases, including cancer and skin disorders, capturing the interest of researchers aiming to understand their function and potential therapeutic applications. Furthermore, advancements in molecular biology techniques have enabled the exploration of IK protein expression patterns and interactions within cellular networks. Investigating the structure-function relationship of IK proteins may reveal insights into their role in disease pathology and highlight potential targets for pharmacological intervention. Overall, the study of IK proteins is a rapidly evolving field that holds promise for enhancing our understanding of cellular mechanics and developing novel strategies for disease management.
