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Filamin A/Filamin 1 [E3]
Product group: | Primary |
Monoclonal/ Polyclonal: | Monoclonal |
Clone: | E3 |
Host: | Mouse |
Isotype: | IgG2a |
Application: | Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) |
Application notes: | 50-200 |
Conjugation Type: | Unconjugated |
Lightchain type: | Kappa |
Reactivity: | Human, Mouse, Rat |
General notes: | Localization: cytoplasm. |
Buffer: | citrate PH6.0 or EDTA pH8.0 |
UNSPSC code: | 12352203 |
Caldesmon, Filamin A (or Filamin 1), Nebulin and Villin are differentially expressed and regulated actin binding proteins. Both muscular (CDh) and non-muscular (CDl) forms of Caldesmon have been identified and each has been shown to bind to Actin as well as to calmodulin and Myosin. CDh is expressed predominantly on thin filaments in smooth muscle, whereas CDl is widely expressed in nonmuscle tissues and cells. Filamin A functions as a crosslinking protein forming a flexible link between two actin filaments. It is composed of two identical polypeptide chains each joined to the other at one end, with an actin binding site at the other. It is present in human platelets, lymphocytes, fibroblasts and smooth muscle actin. Nebulin is a large filamentous protein specific to muscle tissue that may function as a ruler for filament length. Several isoforms of Nebulin are produced by alternative exon usage. Villin is Ca2+-regulated and is the major structural component of the brush border of abso
Filamin A/Filamin 1 [E3]
Caldesmon, Filamin A (or Filamin 1), Nebulin and Villin are differentially expressed and regulated actin binding proteins. Both muscular (CDh) and non-muscular (CDl) forms of Caldesmon have been identified and each has been shown to bind to Actin as well as to calmodulin and Myosin. CDh is expressed predominantly on thin filaments in smooth muscle, whereas CDl is widely expressed in nonmuscle tissues and cells. Filamin A functions as a crosslinking protein forming a flexible link between two actin filaments. It is composed of two identical polypeptide chains each joined to the other at one end, with an actin binding site at the other. It is present in human platelets, lymphocytes, fibroblasts and smooth muscle actin. Nebulin is a large filamentous protein specific to muscle tissue that may function as a ruler for filament length. Several isoforms of Nebulin are produced by alternative exon usage. Villin is Ca2+-regulated and is the major structural component of the brush border of absorptive cells.
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