Recombinant Human MYL9 protein (His tag N-Terminus)
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Recombinant Human MYL9 protein (His tag N-Terminus) is a Human Full Length protein, in the 1 to 172 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec, WB.
View Alternative Names
MLC2, MRLC1, MYRL2, MYL9, Myosin regulatory light polypeptide 9, 20 kDa myosin light chain, MLC-2C, Myosin RLC, Myosin regulatory light chain 9, Myosin regulatory light chain MRLC1, LC20
- WB
Unknown
Western blot - Recombinant Human MYL9 protein (His tag N-Terminus) (AB104014)
All lanes:
Western blot - Anti-MYL9 antibody (<a href='/en-us/products/primary-antibodies/myl9-antibody-ab64161'>ab64161</a>) at 1/2000 dilution
All lanes:
Western blot - Recombinant Human MYL9 protein (His tag N-Terminus) (ab104014) at 0.1 µg
Secondary
All lanes:
Western blot - Goat Anti-Rabbit IgG H&L (HRP) preadsorbed (<a href='/en-us/products/secondary-antibodies/goat-rabbit-igg-h-l-hrp-preadsorbed-ab97080'>ab97080</a>) at 1/5000 dilution
Predicted band size: 20 kDa
true
Exposure time: 4min
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human MYL9 protein (His tag N-Terminus) (AB104014)
15% SDS-PAGE analysis of ab104014 (3 μg)
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Specifications
Form
Liquid
Additional notes
Purified by using anion-exchange chromatography (DEAE sepharose resin) and gel-filtration chromatography (Sephacryl S-200) with 20mM Tris pH 7.5, 2mM EDTA.
General info
Function
Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion (PubMed : 11942626, PubMed : 2526655). In myoblasts, may regulate PIEZO1-dependent cortical actomyosin assembly involved in myotube formation (By similarity).
Post-translational modifications
Phosphorylation increases the actin-activated myosin ATPase activity and thereby regulates the contractile activity. It is required to generate the driving force in the migration of the cells but not necessary for localization of myosin-2 at the leading edge. Phosphorylation is required for myotube formation.
Subcellular localisation
Cytoskeleton
Target data
Product promise
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