Anti-phospho-p38 alpha (Thr180 Tyr182)(M39-652R)

Anti-phospho-p38 alpha (Thr180 Tyr182)(M39-652R)

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Description :Rabbit Polyclonal Antibody

Species :Rabbit

Tag :

Expression System:

Sequence :

Specificity :Recognizes the p38 alpha protein phosphorylated at threonine 180 and tyrosine 182

Cited Applications :WB, IHC

Cross Reactivity :Human, Mouse, Rat, Bovine, Canine, Chicken, non-Human Primate and Zebrafish

Host :Rabbit, IgG

Immunogen :Synthetic phospho-peptide corresponding to amino acid residues surrounding Thr180/Tyr182 conjugated to KLH

Purification :Affinity Chromatography

Stability :Store at 4oC (add 0.1% NaN3) for several months, and at -20oC for longer periods. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.

Sample Data :Western blot of HeLa cell lysates that had been treated with UV or untreated (Control) showing specific immunolabeling of the ~39kDa p38 alpha protein phosphorylated at Thr180/Tyr182.

Sample Data :Immunostaining of human breast cancer tissue showing p38 alpha protein when phosphorylated at Thr180/Tyr182 in red. Photo courtesy of Patsy Ruegg.

Scientific Background :p38alpha (a.k.a. SAPK2A) is a member of the p38 MAPK family, which are activated by various environmental stresses and proinflammatory cytokines (1). The activation of p38 requires its phosphorylation by MAP kinase kinases (MKKs) or by autophosphorylation triggered by the interaction of MAP3K7IP1/TAB1 protein with this kinase (2). The substrates of p38 include the transcriptional regulators ATF2, MEF2C, MAX, the cell cycle regulator CDC25B, and the tumor suppressor p53. Its wide range of targets suggest that p38 has roles in stress related transcription, cell cycle regulation and genotoxic stress response. Like the other MAPKs, p38 is activated by a dual specificity kinase that phosphorylates Thr180 and Tyr182 (3).

References :
1. Han, J. et al: A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. Science 265: 808-811, 1994.

2. Ge, B. et al: MAPKK-independent activation of p38-alpha mediated by TAB1-dependent autophosphorylation of p38-alpha. Science 295: 1291-1294, 2002.

3. Lin A. et al: Identification of a dual specificity kinase that activates the Jun kinases and p38-Mpk2. Science 268:286-290, 1995.

Product Sheets (By Lot #) :

J1274-25.pdf

Research Areas :Angiogenesis, Apoptosis/Autophagy, Cardiovascular Disease, Cellular Stress, Inflammation, Metabolic Disorder, Neurobiology, NfkB Pathway, p38 Pathway, Ser/Thr Kinases, Neurobiology, Inflammation, Metabolic Disorder, Cardiovascular Disease, p38 Pathway, NfkB Pathway, Apoptosis/Autophagy, Cellular Stress, Angiogenesis, Ser/Thr Kinases