This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Lagerung
4 °C,-20 °C
Informationen zur Lagerung
Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles.
Haase, Dobbernack, Tünnemann, Karczewski, Cardoso, Petzhold, Schlegel, Lutter, Pierschalek, Behlke, Morano: "Minigenes encoding N-terminal domains of human cardiac myosin light chain-1 improve heart function of transgenic rats." in: FASEB journal : official publication of the Federation of American Societies for Experimental Biology, Vol. 20, Issue 7, pp. 865-73, (2006) (PubMed).
Xie, Huang, Huang, Zhou, Gong: "The functional domains of human ventricular myosin light chain 1." in: Biophysical chemistry, Vol. 106, Issue 1, pp. 57-66, (2003) (PubMed).
Myosins are a large superfamily of motor proteins that move along actin filaments, while hydrolyzing ATP. Myosin is the major component of thick muscle filaments, and is a long asymmetric molecule containing a globular head and a long tail. The molecule consists of two heavy chains and four light chains. Activation of smooth and cardiac muscle primarily involves pathways which increase calcium and myosin phosphorylation resulting in contraction. Myosin light chain phosphatase acts to regulate muscle contraction by dephosphorylating activated myosin light chain. MYL3 encodes myosin light chain 3, an alkali light chain also referred to in the literature as both the ventricular isoform and the slow skeletal muscle isoform. Human myosin light chain has clinical application as a cardiac marker. Mutations in MYL3 have been identified as a cause of mid-left ventricular chamber type hypertrophic cardiomyopathy.