Analytical Data
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Gene name
CCDC23
- Application
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Alternative Names
CCDC23；CCDC23；Small vasohibin-binding Protein
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8N300
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Expression Region
1-66aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFMDPPA RKEKTKVKES VSRVEKAKQK SAQQELKQRQ RAEIYALNRV MTELEQQQFD EFCKQMQPPG E
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Molecular Weight
11 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
CCDC23 (Coiled-Coil Domain Containing 23) is a protein that plays a significant role in cellular processes, particularly in cilia formation and function, which are crucial for various signaling pathways and cellular motility. Dysregulation or mutations in CCDC23 have been associated with several ciliopathies, conditions that result from defects in cilia structure and function. Key research efforts have focused on understanding the structural and functional aspects of CCDC23, as well as its interactions with other proteins involved in ciliary assembly and maintenance. Recent studies have utilized recombinant protein techniques to produce CCDC23 in various expression systems, allowing for detailed biochemical and biophysical characterization. The analysis of the recombinant protein offers insights into its structural properties, interaction dynamics, and potential roles in disease mechanisms. Additionally, these studies pave the way for future therapeutic interventions aimed at correcting the dysfunctions associated with CCDC23-related disorders. Understanding the detailed mechanisms of CCDC23 function will not only enhance our knowledge of ciliogenesis but also contribute to the development of targeted strategies for dealing with the basic science and clinical implications of ciliopathies.
