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Merck

M7786

Sigma-Aldrich

Monoclonal Anti-Myosin (Smooth) antibody produced in mouse

clone hSM-V, ascites fluid

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

mouse

Qualitätsniveau

Konjugat

unconjugated

Antikörperform

ascites fluid

Antikörper-Produkttyp

primary antibodies

Klon

hSM-V, monoclonal

Mol-Gew.

antigen 200-204 kDa

Enthält

15 mM sodium azide

Speziesreaktivität

guinea pig, human, pig, canine, rabbit, chicken

Methode(n)

immunohistochemistry: 1:500 using and animal frozen section using acetone fixed human.
immunohistochemistry: suitable using using methacarn-fixed, paraffin-embedded sections of human and animal tissue
immunoprecipitation (IP): suitable
western blot: suitable

Isotyp

IgG1

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... MYH11(4629)

Allgemeine Beschreibung

Monoclonal Anti-Myosin (Smooth) (mouse IgG1 isotype) is derived from the hSM-V hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with human uterus smooth muscle extract. Myosin (~500 kDa) is a cytoskeletal protein containing two identical heavy chains (~200 kDa each) and four light chains (15-26 kDa). Myosin molecules consist of two major regions: tail (rod) and heads.

Spezifität

Mouse monoclonal clone hSM-V anti-Myosin (Smooth) antibody reacts in immunoblotting assays with myosin heavy chain polypeptides of 204 and 200 kDa (SM-1 and SM-2). It does not cross-react with skeletal, cardiac or non-muscle myosin. The antibody stains vascular and visceral smooth muscle cells, as well as cells that have smooth muscle-like characteristics (myofibroblasts and myoepithelial cells). It does not recognize epithelial, endothelial or connective tissue fibroblast cells. The product reacts with smooth muscle tissue from human, dog, rabbit, pig, guinea pig, and chicken.

Immunogen

human uterus smooth muscle extract.

Anwendung

The antibody may be used in:
  • immunoblotting
  • immunoprecipitation
  • immunohistochemistry
  • immunocytochemistry
  • flow cytometry
  • immunofluorescence

Biochem./physiol. Wirkung

Myosin implicated in cell motility. They aggregate into filaments through the tail region and interact with actin and with ATP through the head region. Myosin molecules spontaneously assemble into filaments in solutions of physiologic ionic strength and pH. In fact, the thick filament consists mainly of myosin molecules. The ATPase of myosin is activated by actin. This activation is the immediate source of the free energy that drives muscle contraction. It binds to the polymerized form of actin, the major constituent of the thin filament. Myosin is generally assumed to be a very specific and reliable smooth muscle marker, provided that the antibody used is specific for smooth muscle myosin and does not cross-react with skeletal, cardiac or non-muscle myosins.

Haftungsausschluss

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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Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 2

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

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In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

Phosphorylation of the regulatory light chain of myosin in striated muscle: methodological perspectives
Yu H, et al.
European Biophysics Journal, 45(8), 779-805 (2016)
Endothelial-to-mesenchymal transition drives atherosclerosis progression
Chen PY, et al.
The Journal of Clinical Investigation, 125(12), 4514-4528 (2015)
Human vascular model with defined stimulation medium - a characterization study
Huttala O, et al.
ALTEX, Citations(may), include-include (2015)
Myosin: The Actin Motor Protein
Molecular Cell Biology. 4th edition. (2000)
Direct measurements of local coupling between myosin molecules are consistent with a model of muscle activation
Walcott S and Kad NM
PLoS Computational Biology, 11(11), e1004599-e1004599 (2015)

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