M5566
Anti-Myosin IX/Myr5 antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
Synonym(s):
Anti-CELIAC4, Anti-MYR5
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About This Item
Recommended Products
biological source
rabbit
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 230 kDa
species reactivity
rat
technique(s)
microarray: suitable
western blot: 1:1,000 using rat embryonic brain extract.
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
rat ... Myo9b(25486)
General description
Myosin IX belongs to the family of unconventional myosins. The tail region of these myosins contains a GTPase-activating protein (GAP) domain. It is expressed at higher levels in the embryonic brain than in the adult brain. In the adult rat, it is highly expressed in the lung, liver, spleen, and testis. The subcellular localization of class IX myosins appears to be partly cytoplasmic and partly associated with membranes and the actin cytoskeleton. The tail domain of myosin IX/Myr5 contains a region that coordinates two atoms of zinc. Myosin IX is thought to be involved in signal transduction and leukocyte differentiation.
Myosin IX/Myr5 is a single headed myosin which possesses an N-terminal extension and a large loop 2 insertion.
Specificity
Anti-Myosin IX/Myr5 recognizes rat myosin IX/Myr5 (230 kDa).
Immunogen
synthetic peptide corresponding to the C-terminal region of rat myosin IX/Myr5 (amino acids 1960-1980).
Application
Anti-Myosin IX/Myr5 antibody produced in rabbit may be used in immunoblotting.
Biochem/physiol Actions
Myosin IX expression level may vary during development and differentiation. The tail domain of myosin IX/Myr5 and the GTPase-activating protein (GAP) domain stimulates GTP hydrolysis. It is implicated in the regulation of actin organization, and the actin cytoskeleton. Overexpression of both Myr5 and Myr7 in cultured cells results in inactivation of Rho, loss of actin stress fibers, and focal contacts, leading to changes in cell morphology.
Myosin IX/Myr5 moves along the actin filaments for long distances and is mostly present in its ATP-bound state. It has been studied as a negative regulator of RhoC which is a G-protein.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Storage and Stability
For continuous use, store at 2-8 °C for up to one month. For prolonged storage, freeze in working aliquots at −20 °C. Repeated freezing and thawing is not recom-mended. Storage in frost-free freezers is also not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Wanqin Liao et al.
The Journal of biological chemistry, 285(32), 24933-24942 (2010-06-12)
Mammalian myosin IXb (Myo9b) has been shown to exhibit unique motor properties in that it is a single-headed processive motor and the rate-limiting step in its chemical cycle is ATP hydrolysis. Furthermore, it has been reported to move toward the
Sandra Struchholz et al.
The Journal of biological chemistry, 284(6), 3663-3671 (2008-12-09)
The mammalian class IX myosin Myo9b can move considerable distances along actin filaments before it dissociates. This is remarkable, because it is single headed and because the rate-limiting step in its ATPase cycle is ATP hydrolysis. Thus, it spends most
Vijayalaxmi Nalavadi et al.
The Journal of biological chemistry, 280(47), 38957-38968 (2005-09-24)
Myosin IXb (Myo9b) was reported to be a single-headed, processive myosin. In its head domain it contains an N-terminal extension and a large loop 2 insertion that are specific for class IX myosins. We characterized the kinetic properties of purified
Arturo Raya-Sandino et al.
Biochimica et biophysica acta. Molecular cell research, 1864(10), 1714-1733 (2017-05-31)
Silencing Zonula occludens 2 (ZO-2), a tight junctions (TJ) scaffold protein, in epithelial cells (MDCK ZO-2 KD) triggers: 1) Decreased cell to substratum attachment, accompanied by reduced expression of claudin-7 and integrin β1, and increased vinculin recruitment to focal adhesions
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