MYLK Blocking Peptide peptide (STJ505395)

SKU:
STJ505395-250

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Applications: Immunodepletion/Immunocompetition
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: MYLK Blocking Peptide is synthetically produced from the 1870-1917 sequence and is suitable for use in western blot applications.
Formulation: Liquid form at 2.5mg/ml concentration in PBS. Up to 5% DMSO can be added. Orders with >1mg can be supplied in lyophilized powder form, or in buffer of choice.
Storage Instruction: Store at-20°C for long term storage. Avoid freeze-thaw cycles.
Gene Symbol: MYLK
Gene ID: 4638
Uniprot ID: MYLK_HUMAN
Immunogen Region: 1870-1917
Immunogen: Synthetic peptide taken within amino acid region 1870-1917 on human Myosin light chain kinase, smooth muscle isoform 1 protein.
Tissue Specificity 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).
Post Translational Modifications 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. Acetylated at Lys-608 by NAA10/ARD1 via a calcium-dependent signaling.this acetylation represses kinase activity and reduces tumor cell migration.
Function Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. 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. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury.triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca(2+) entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells. Responsible for high proliferative ability of breast cancer cells through anti-apoptosis.
Peptide Name Myosin Light Chain Kinase - Smooth Muscle
Mlck
Smmlck
Kinase-Related Protein
Krp
Telokin Cleaved Into - Myosin Light Chain Kinase - Smooth Muscle - Deglutamylated Form
Database Links Reactome: R-HSA-445355
Reactome: R-HSA-5627123
Cellular Localisation Cytoplasm
Cell Projection
Lamellipodium
Cleavage Furrow
Cytoskeleton
Stress Fiber
Localized To Stress Fibers During Interphase And To The Cleavage Furrow During Mitosis
Alternative Peptide Names Myosin Light Chain Kinase - Smooth Muscle protein
Mlck protein
Smmlck protein
Kinase-Related Protein protein
Krp protein
Telokin Cleaved Into - Myosin Light Chain Kinase - Smooth Muscle - Deglutamylated Form protein
MYLK protein
MLCK protein
MLCK1 protein
MYLK1 protein

Information sourced from Uniprot.org

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