A4861
p38α, active, GST tagged human
PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
Synonym(s):
CSBP1, CSBP2, CSPB1, MAPK14, PRKM14, PRKM15, SAPK2A
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About This Item
UNSPSC Code:
12352200
NACRES:
NA.32
Pricing and availability is not currently available.
recombinant
expressed in baculovirus infected Sf9 cells
Quality Level
product line
PRECISIO® Kinase
assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
specific activity
148-202 nmol/min·mg
mol wt
~67 kDa
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... MAPK14(1432)
Biochem/physiol Actions
p38α (SAPK2A) is a member of the p38 MAPK family which are activated by various environmental stresses and proinflammatory cytokines. The activation of p38 requires its phosphorylation by MAP kinase kinases (MKKs), or its autophosphorylation triggered by the interaction of MAP3K7IP1/TAB1 protein with this kinase. The substrates of p38 include transcription regulator ATF2, MEF2C, MAX, cell cycle regulator CDC25B, and tumor suppressor p53, which suggest the roles of this kinase in stress related transcription and cell cycle regulation, as well as in genotoxic stress response.
Physical form
Supplied in 50 mM Tris-HCl, pH 7.5, with 150 mM NaCl, 0.25 mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, and 25% glycerol.
Legal Information
PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany
Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha.
Baoxue Ge et al.
Science (New York, N.Y.), 295(5558), 1291-1294 (2002-02-16)
Phosphorylation of mitogen-activated protein kinases (MAPKs) on specific tyrosine and threonine sites by MAP kinase kinases (MAPKKs) is thought to be the sole activation mechanism. Here, we report an unexpected activation mechanism for p38alpha MAPK that does not involve the
J Han et al.
Science (New York, N.Y.), 265(5173), 808-811 (1994-08-05)
Mammalian cells respond to endotoxic lipopolysaccharide (LPS) by activation of protein kinase cascades that lead to new gene expression. A protein kinase, p38, that was tyrosine phosphorylated in response to LPS, was cloned. The p38 enzyme and the product of
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