Analytical Data
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Gene name
KLF2
- Application
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Alternative Names
LKLF; Lung krueppel-like factor
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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
Q9Y5W3
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Expression Region
Met1~Met355
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Molecular Weight
46kDa
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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
KLF2 (Krupple-like factor 2) is a transcription factor that plays a crucial role in various biological processes, including vascular development, endothelial function, and immune response regulation. Its significance in cellular differentiation and maintenance of pluripotency has prompted extensive research into its role in stem cell biology and tissue regeneration. Recombinant KLF2 proteins have emerged as valuable tools for studying the functional mechanisms and pathways in which KLF2 is involved. Researchers often utilize recombinant techniques to produce KLF2 proteins in bacterial or eukaryotic systems, allowing for the assessment of their biological activity and interaction with target genes. Given KLF2's implications in cardiovascular health and potential therapeutic applications, including regenerative medicine and cancer therapy, understanding its structural and functional properties at the protein level is essential. Additionally, the study of KLF2 recombinant proteins can provide insights into developing novel strategies to manipulate its expression or activity for potential clinical benefits. As researchers continue to explore the diverse roles of KLF2, the characterization of its recombinant protein forms stands as a critical component in deciphering its full biological impact.
