Analytical Data
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Gene name
KNCN
- Application
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Alternative Names
KNCN; Kinocilin
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A6PVL3
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Expression Region
1-136aa
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AA Sequence
MLRQSLSGCPCPALPSCLLPLCQCPPGLGDPDRRQARPCRPQSGWEQCLEWGLLHSPGQASPKWIPLVWAGTWSKVSPDAPTGFPCFRLLPWPFFLDCSSALLPVQSTDLFLWNLGSRALTMTRMPQSLALTRLQK
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Molecular Weight
41.5 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
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Protein Description
KNCN (K+ channel-interacting protein C-novel) is a member of the K+ channel-interacting protein family, which plays a crucial role in modulating the activity of voltage-gated K+ channels. In recent years, KNCN has garnered attention for its potential involvement in various physiological and pathological processes, including neuronal excitability, cardiac function, and tumor biology. Research indicates that KNCN may interact with specific K+ channels, influencing their gating and localization, which could have significant implications for understanding diseases such as arrhythmias, epilepsy, and cancer. By exploring the structural and functional characteristics of KNCN through recombinant protein studies, scientists aim to elucidate its role in these processes. The generation of recombinant KNCN protein allows for detailed investigation of its interactions with K+ channels and other cellular partners, paving the way for potential therapeutic applications. Furthermore, understanding KNCN's structure-function relationship may provide insights into its regulatory mechanisms and open new avenues for drug discovery. This research is essential not only for basic scientific knowledge but also for developing targeted treatments for diseases linked to dysregulated K+ channel activity.
