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Recombinant human biotinylated MAP kinase 11 / p38 beta, unactive, 5 µg  

Recombinant human biotinylated MAP kinase 11 / p38 beta, unactive, 5 µg

Recombinant human biotinylated mitogen-activated protein kinase 11 / p38 beta / SAPK2, unactive enzyme

Alternate names: recombinant, human, protein kinase, SAPK2, Stress-activated protein kinase 2, MAPK11, mitogen-activated protein kinase 11, btnp38b

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Availability: on stock

295,00 €

The p38 MAPK (mitogen-activated protein kinase) pathway contains protein kinases which engage in respond to various extracellular stimuli an intracellular signalling cascade, coordinating the activation of gene transcription, protein synthesis, cell cycle machinery, cell death, and differentiation. The different p38 MAPK family members (p38α, p38β, p38γ, p38δencoded by different genes show an approximately 60% identical in their amino acid sequence but have different tissue expression patterns. p38 MAPKs being activated by dual phosphorylation of the Thr-Gly-Tyr in the activation loop sequence by MKKs/MAP2Ks (MKK6 and MKK3). Down-regulation of p38 MAPK is achieved for instance by Wip1, a phosphatase of the PP2C family that can be transcriptionally up-regulated by p53 or by MKPs, a family of dual-specificity protein phosphatases. Upon activation p38 MAP kinases can phosphorylate substrates on Ser-Pro or Thr-Pro motifs on MSK1 and 2, which directly phosphorylate the transcription factors CREB, ATF1, or cytosolic proteins such as phospholipase A2, Bcl-2 family proteins and cyclins. Because of the important role of p38α in inflammatory diseases it is also an interesting pharmaceutical target. Based on SB203580, one of the first discovered p38α inhibitors structurally diverse p38α and p38β inhibitors have been developed with both enhanced potency and specificity.

Biotinylated protein is not phosphorylated and activated by MKKs. Suitable for kinase molecule interaction analyses using SPR, as substrate for kinase activity assays and for western blot analyses.

Protein: Human recombinant p38 beta, biotinylated, full lenght, purified as N-His-fusion protein
Theoretical MW :42.7 kDa (fusion proteins)
Expression system: E.coli
Purification: Immobilized metal affinity chromatography (IMAC), gel filtration
Storage buffer: 20 mM Tris-HCl, 150 mM NaCl, 2 mM DTT, 20% glycerol, pH 8.0
Storage temperature: - 80°C (avoid repeated freeze-thaw cycles !)
Purity:>90 %
Protein concentration:0.42 mg/ml (Bradford method using BSA as standard protein)

Entrez Gene: ID 5600 
UniProtKB: Q15759

Ordering information: shipped on dry ice


Use the p38 MAPK - SPR Binding Assay of BIAFFIN for comprehensive kinetic characterization of your small molecule kinase inhibitors. 


Figure: Real-time kinetic analysis of kinase inhibitor SB203580 binding to p38β using surface plasmon resonance.

Please contact our application specialists to obtain more information and an individual quote tailored to your specific needs. 

We provide our Kinascreen services to kinetically characterize small molecule kinase inhibitors for all p38 isoforms (p38α, p38β, p38γ and p38δ) in their phosphorylated (activated) and unphosphorylated (non-activated) state. 

Product specific literature references:

Cuadrado A, Nebreda AR.  (2010) “Mechanisms and functions of p38 MAPK signalling.” Biochem J. 1;429(3):403-17.

Kyriakis JM, Avruch J. (2001) „Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation.“ Physiol Rev.81(2):807-69.

Roux PP, Blenis J.,(2004) “ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions.” Microbiol Mol Biol Rev. 68(2):320-44.

Shin J, Park B, Ahn K eta al. (2004) "Promyelocytic leukemia is a direct inhibitor of SAPK2/p38 mitogen-activated protein kinase" J Biol Chem. 279(39):40994-1003

Saklatvala J (2004) "The p38 MAP kinase pathway as a therapeutic target in inflammatory disease" Curr Opin Pharmacol. 4(4):372-7

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