Analytical Data
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Gene name
NLK
- Application
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Alternative Names
(Nemo-like kinase)(Protein LAK1)
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UBE8
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Expression Region
1-527aa
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Molecular Weight
63.3 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
Related Products
Protein Description
NLK (Nemo-like kinase) is a member of the mitogen-activated protein kinase (MAPK) family, primarily involved in various signaling pathways that regulate cellular processes such as growth, differentiation, and apoptosis. Its aberrant expression has been implicated in several cancers, highlighting its potential as a therapeutic target. Research on NLK has gained traction due to its critical role in modulating key downstream effects of the Wnt and Notch signaling pathways, both of which are essential for normal developmental processes and cellular homeostasis. The study of NLK's structure and function has revealed its capability to phosphorylate specific substrates, leading to alterations in gene expression and cellular behavior. Recombining NLK proteins for experimental purposes has allowed researchers to investigate their biochemical characteristics and interaction networks in detail, thus providing insights into the mechanisms underlying tumorigenesis and other diseases. Furthermore, understanding the regulation of NLK activity may unveil novel strategies for targeted therapies, making it a promising focus in cancer research and molecular biology. The ongoing studies aim to elucidate the precise physiological roles of NLK in various contexts, paving the way for potential applications in regenerative medicine and targeted cancer therapies.
