SRP5244
MLK1 (1-433), active, GST tagged human
PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
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Synonym(s):
MAP3K9, MEKK9, PRKE1
UNSPSC Code:
12352200
NACRES:
NA.32
recombinant
expressed in baculovirus infected Sf9 cells
product line
PRECISIO® Kinase
Assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
specific activity
99-133 nmol/min·mg
mol wt
~77 kDa
NCBI accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... MAP3K9(4293)
General description
MLK1 or Mixed-Lineage Kinase 1 is a mitogen-activated protein kinase kinase kinase capable of activating the c-Jun NH(2)-terminal kinase (JNK) pathway. The catalytic domain of MLK1 has amino acid sequence similarity to both the tyr-specific and the ser/thr-specific kinase classes. In addition, MLK1 contain 2 leu/ile-zipper motifs and a basic sequence near its C-termini. MLK1 is threonine (and possibly serine) phosphorylated at multiple sites in the activation loop, with phosphorylation of Thr312 required for full activation.
Physical form
Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.
Preparation Note
after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles
Legal Information
PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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John T Durkin et al.
Biochemistry, 43(51), 16348-16355 (2004-12-22)
Mixed-lineage kinase 1 (MLK1) is a mitogen-activated protein kinase kinase kinase capable of activating the c-Jun NH(2)-terminal kinase (JNK) pathway. Full-length MLK1 has 1104 amino acids and a domain structure identical to MLK2 and MLK3. Immunoblot and mass spectrometry show
D S Dorow et al.
European journal of biochemistry, 213(2), 701-710 (1993-04-15)
Using the polymerase chain reaction to study mRNA expressed in human epithelial tumor cells, a member of a new family of protein kinases was identified. The catalytic domain of this kinase has amino-acid-sequence similarity to both the Tyr-specific and the
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