Analytical Data
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Gene name
KLP1
- Application
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Alternative Names
NAT14; KLP1; Probable N-acetyltransferase 14; K562 cell-derived leucine-zipper-like protein 1
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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
Q8WUY8
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Expression Region
1-206aa
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AA Sequence
MAPSHLSVREMREDEKPLVLEMLKAGVKDTENRVALHALTRPPALLLLAAASSGLRFVLASFALALLLPVFLAVAAVKLGLRARWGSLPPPGGLGGPWVAVRGSGDVCGVLALAPGTNAGDGARVTRLSVSRWHRRRGVGRRLLAFAEARARAWAGGMGEPRARLVVPVAVAAWGVGGMLEGCGYQAEGGWGCLGYTLVREFSKDL
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Molecular Weight
48.1 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
KLP1, a member of the kinesin superfamily, is a motor protein known for its role in cellular transport processes, particularly in the movement of organelles along microtubules. The interest in KLP1 research stems from its essential functions in mitosis and intracellular trafficking, which are critical for maintaining cellular homeostasis and proper cell division. Dysregulation of kinesins like KLP1 has been linked to various diseases, including cancer and neurodegenerative disorders, highlighting the importance of understanding its molecular mechanisms. Researchers have been investigating the structure, function, and regulatory mechanisms of KLP1 through recombinant protein technology. This approach enables the production of KLP1 in a controlled manner, allowing for detailed studies of its interactions with microtubules and other cellular components. Additionally, studying KLP1's dynamic behavior can provide insights into its role during cell division and its involvement in cellular responses to stress. The findings could pave the way for therapeutic strategies targeting KLP1-related pathways in diseases characterized by disturbed motor protein function, thereby contributing to the development of novel treatments and improving our understanding of fundamental cellular processes.
