Peptide containing DpSMANpSF in which pS corresponds to phosphorylated amino acids 218 and 222 of human MEK1
Application
Detect phospho-MEK1 (Ser218/222)/MEK2 (Ser222/226) using this Anti-phospho-MEK1 (Ser218/222)/MEK2 (Ser222/226) Antibody validated for use in WB.
Research Category Signaling
Research Sub Category MAP Kinases
Quality
routinely evaluated by immunoblot on RIPA lysates from PC-12 cells that have been treated with B-Raf
Target description
45kDa
Linkage
Replaces: 04-1017
Physical form
0.1M Tris-glycine, pH 7.4, 0.15M NaCl, 0.05% sodium azide before the addition of glycerol to 30%
Format: Purified
Protein A purified
Storage and Stability
2 years at -20°C
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class
10 - Combustible liquids
wgk_germany
WGK 2
Certificates of Analysis (COA)
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Proceedings of the National Academy of Sciences of the United States of America, 118(36) (2021-09-03)
The RAF/MEK/ERK pathway is central to the control of cell physiology, and its dysregulation is associated with many cancers. Accordingly, the proteins constituting this pathway, including MEK1/2 (MEK), have been subject to intense drug discovery and development efforts. Allosteric MEK
Negative regulation of MAPKK by phosphorylation of a conserved serine residue equivalent to Ser212 of MEK1.
Gopalbhai, Kailesh, et al.
The Journal of Biological Chemistry, 278, 8118-8125 (2003)
Nature chemical biology, 9(5), 307-312 (2013-03-19)
Protein kinase clients are recruited to the Hsp90 molecular chaperone system via Cdc37, which simultaneously binds Hsp90 and kinases and regulates the Hsp90 chaperone cycle. Pharmacological inhibition of Hsp90 in vivo results in degradation of kinase clients, with a therapeutic
The kinome specific co-chaperone, CDC37 (cell division cycle 37), is responsible for delivering BRAF (B-Rapidly Accelerated Fibrosarcoma) to the Hsp90 (heat shock protein 90) complex, where it is then translocated to the RAS (protooncogene product p21) complex at the plasma
Chirality and morphology are essential factors for protein function and interactions with other biomacromolecules. Extracellular matrix (ECM) proteins are also similar to other proteins in this sense; however, the complexity of the natural ECM makes it difficult to study these
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