Analytical Data
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Gene name
KLHL14
- Application
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Alternative Names
KIAA1384
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Species
Human
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Source
Baculovirus
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Tag
Strep;His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9P2G3-1
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Expression Region
S2-K628
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Protein Length
Partial
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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
KLHL14, a member of the Kelch-like (KLHL) protein family, plays a pivotal role in various cellular processes, including protein degradation, cellular signaling, and cytoskeletal organization. Its involvement in the regulation of the ubiquitin-proteasome system has garnered attention, particularly in the context of several human diseases, including cancer and neurodegenerative disorders. Recent studies have suggested that KLHL14 may function as a substrate adapter for Cullin-RING E3 ligases, contributing to the selective degradation of specific proteins and thereby influencing cellular homeostasis. Researchers have increasingly focused on the functional characterization of KLHL14 and its interactions with other cellular components to elucidate its biochemical pathways and regulatory roles. The exploration of KLHL14 as a recombinant protein provides insights into its structural properties and functional mechanisms, laying the groundwork for potential therapeutic applications. Understanding KLHL14's role could unveil new targets for drug development, particularly in the field of cancer therapy, where manipulating protein degradation pathways may offer novel strategies to combat tumor progression. Furthermore, the production and study of KLHL14 recombinant protein may also facilitate the discovery of small molecules or peptides that can modulate its activity, offering additional avenues for intervention in diseases associated with aberrant KLHL14 expression or function. Overall, KLHL14 represents a promising area of research that bridges molecular biology, biochemistry, and therapeutic development, highlighting the importance of investigating its roles in cellular physiology and pathology.











