Analytical Data
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Gene name
PNCK
- Application
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Alternative Names
PNCK；Calcium/calmodulin-dependent Protein kinase type 1B
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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
Q6P2M8
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Expression Region
1-343aa
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AA Sequence
MLLLKKHTED ISSVYEIRER LGSGAFSEVV LAQERGSAHL VALKCIPKKA LRGKEALVEN EIAVLRRISH PNIVALEDVH ESPSHLYLAM ELVTGGELFD RIMERGSYTE KDASHLVGQV LGAVSYLHSL GIVHRDLKPE NLLYATPFED SKIMVSDFGL SKIQAGNMLG TACGTPGYVA PELLEQKPYG KAVDVWALGV ISYILLCGYP PFYDESDPEL FSQILRASYE FDSPFWDDIS ESAKDFIRHL LERDPQKRFT CQQALRHLWI SGDTAFDRDI LGSVSEQIRK NFARTHWKRA FNATSFLRHI RKLGQIPEGE GASEQGMARH SHSGLRAGQP PKW
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Molecular Weight
38 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
PNCK (p50nck) is a member of the non-receptor tyrosine kinase family and has garnered increasing attention due to its crucial role in various cellular processes, including cell proliferation, differentiation, and survival. Research has shown that PNCK is involved in multiple signaling pathways, particularly those related to cancer and neurodegeneration, which positions it as a potential therapeutic target. The understanding of PNCK's function has been facilitated by advances in recombinant protein technology, allowing researchers to produce and purify PNCK in sufficient quantities for in vitro studies. By generating PNCK recombined proteins, scientists can investigate its structural properties and enzymatic activity, providing insights into its molecular mechanisms. Furthermore, the exploration of PNCK interactions with other proteins may reveal novel pathways that contribute to disease progression. Thus, the research surrounding recombinant PNCK not only aims to elucidate its fundamental biological roles but also to facilitate the development of targeted therapies for malignancies and neurological disorders associated with dysregulation of its signaling. The ongoing studies leverage sophisticated techniques including CRISPR, mass spectrometry, and cryo-electron microscopy, emphasizing the significance of PNCK in modern biomedical research. Through these efforts, the PNCK protein stands to offer valuable contributions to our comprehension of complex human diseases, paving the way for innovative treatment strategies.
