Product namep38 peptide
See all p38 proteins and peptides
Purity> 90 % SDS-PAGE.
Our Abpromise guarantee covers the use of ab53314 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Blocking - Blocking peptide for Anti-p38 antibody (ab27986)
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Preparation and Storage
Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Preservative: 0.02% Thimerosal (merthiolate)
Constituents: PBS, 0.1% BSA
- CSAID binding protein
- CSAID Binding Protein 1
- CSAID-binding protein
FunctionResponds to activation by environmental stress, pro-inflammatory cytokines and lipopolysaccharide (LPS) by phosphorylating a number of transcription factors, such as ELK1 and ATF2 and several downstream kinases, such as MAPKAPK2 and MAPKAPK5. Plays a critical role in the production of some cytokines, for example IL-6. May play a role in stabilization of EPO mRNA during hypoxic stress. Isoform Mxi2 activation is stimulated by mitogens and oxidative stress and only poorly phosphorylates ELK1 and ATF2. Isoform Exip may play a role in the early onset of apoptosis.
Tissue specificityBrain, heart, placenta, pancreas and skeletal muscle. Expressed to a lesser extent in lung, liver and kidney.
Sequence similaritiesBelongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.
Contains 1 protein kinase domain.
DomainThe TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
modificationsDually phosphorylated on Thr-180 and Tyr-182, which activates the enzyme.
Phosphorylated upon DNA damage, probably by ATM or ATR.
Cellular localizationCytoplasm. Nucleus.
- Information by UniProt
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab53314 has not yet been referenced specifically in any publications.