Lane 1: human lung tissue lysate
Lane 2: mouse lung tissue lysate
Lane 2: rat lung tissue lysate
Recombinant Rabbit monoclonal primary
Recombinant Myosin light-chain kinase Monoclonal Antibody (ET1608-68)
Human lung tissue lysate, mouse lung tissue lysate, rat lung tissue lysate, Hela, L6, NIH/3T3, SH-SY5Y, rat smooth muscle tissue, human colon carcinoma tissue, mouse smooth muscle tissue.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A affinity purified.
Myosin light chain kinase
deglutamylated form antibody; DKFZp686I10125 antibody; EC 18.104.22.168 antibody; FLJ12216 antibody; Kinase related protein antibody; Kinase-related protein antibody; KRP antibody; MLCK antibody; MLCK1 antibody; MLCK108 antibody; MLCK210 antibody; MSTP083 antibody; MYLK antibody; MYLK_HUMAN antibody; MYLK1 antibody; Myosin light chain kinase antibody; Myosin light polypeptide kinase antibody; OTTHUMP00000180642 antibody; OTTHUMP00000180643 antibody; smMLCK antibody; smooth muscle antibody; Smooth muscle myosin light chain kinase antibody; Telokin antibody
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.
Smooth muscle and non-muscle isozymes are expressed in a wide variety of adult and fetal tissues and in cultured endothelium with qualitative expression appearing to be neither tissue- nor development-specific. Non-muscle isoform 2 is the dominant splice variant expressed in various tissues. Telokin has been found in a wide variety of adult and fetal tissues. Accumulates in well differentiated enterocytes of the intestinal epithelium in response to tumor necrosis factor (TNF).
Can probably be down-regulated by phosphorylation. Tyrosine phosphorylation by ABL1 increases kinase activity, reverses MLCK-mediated inhibition of Arp2/3-mediated actin polymerization, and enhances CTTN-binding. Phosphorylation by SRC at Tyr-464 and Tyr-471 promotes CTTN binding.; The C-terminus is deglutamylated by AGTPBP1/CCP1, AGBL1/CCP4 and AGBL4/CCP6, leading to the formation of Myosin light chain kinase, smooth muscle, deglutamylated form. The consequences of C-terminal deglutamylation are unknown (By similarity).; Acetylated at Lys-608 by NAA10/ARD1 via a calcium-dependent signaling; this acetylation represses kinase activity and reduces tumor cell migration.
Cytoplasm, Cell projection, Cleavage furrow.
MLCK, a member of the Ser/Thr protein kinase family, is a calcium/calmodulin-dependent enzyme responsible for smooth muscle contraction via phosphorylation of a specific serine in the N-terminus of myosin light chains (MLC), an event that facilitates myosin interaction with actin filaments. It is a central determinant in the development of vascular permeability and tissue edema formation. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. MLCK acts as a critical participant in signaling sequences that result in fibroblast apoptosis. Smooth muscle and non-muscle isozymes are expressed in a wide variety of adult and fetal tissues and in cultured endothelium with qualitative expression appearing to be neither tissue- nor development-specific. Non-muscle isoform 2 is the dominant splice variant expressed in various tissues. The Telokin isoform, which binds calmodulin, has been found in a wide variety of adult and fetal tissues. MLCK is probably down-regulated by phosphorylation. The protein contains 1 fibronectin type III domain and 9 immunoglobulin-like C2-type domains.