Analytical Data
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Gene name
KIF23
- Application
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Alternative Names
KNSL5; MKLP1; Kinesin-Like 5; Mitotic Kinesin-Like Protein 1
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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
Q02241
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Expression Region
Leu794~Pro960
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Molecular Weight
22kDa
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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
KIF23, also known as MKLP1 (mitotic kinesin-like protein 1), is a member of the kinesin superfamily of motor proteins that play crucial roles in cellular processes, especially during mitosis and cytokinesis. It is predominantly involved in the transport of organelles and the segregation of chromosomes. The significance of KIF23 in cell division has attracted considerable attention, as its dysregulation can lead to aneuploidy and tumorigenesis. Recent research has focused on the structural and functional characterization of KIF23, with recombinant protein studies aimed at revealing its mechanistic functions. Understanding the interaction between KIF23 and its binding partners, such as microtubules, is essential for elucidating its role in the mitotic spindle assembly and disassembly. Moreover, the development of KIF23 as a potential therapeutic target is of great interest, as inhibiting its function could provide a novel approach to cancer treatment. By employing recombinant KIF23 proteins in biochemical assays and structural studies, researchers aim to clarify its motor activity, regulatory mechanisms, and interaction dynamics, paving the way for new insights into cellular division and potential interventions in oncogenesis. The ongoing exploration of KIF23 not only enhances our understanding of fundamental biological processes but also opens avenues for innovative therapies targeting cancer cell proliferation.
