C6542
Monoclonal Anti-Caldesmon antibody produced in mouse
clone CALD-5, ascites fluid
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About This Item
UNSPSC Code:
12352203
MDL number:
biological source
mouse
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
CALD-5, monoclonal
contains
15 mM sodium azide
species reactivity
human, chicken
technique(s)
indirect immunofluorescence: suitable using frozen human tissue sections, microarray: suitable, western blot: 1:100 using chicken gizzard extract
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... CALD1(800)
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Immunogen
caldesmon from turkey gizzard
Biochem/physiol Actions
The antibody localizes the high molecular weight form of caldesmon in chicken or turkey gizzard and the low molecular weight form of caldesmon in chicken fibroblasts by immunoblotting. CALD-5 localizes both the high and low molecular weight caldesmons in cultured human smooth muscle cells. The antibody reacts with epitopes located on the N-terminal, non-calmodulin-binding part of caldesmon.
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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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W Durand-Arczynska et al.
Histochemistry, 100(6), 465-471 (1993-12-01)
Calponin and caldesmon are two proteins considered to play a regulatory role in smooth muscle contraction, which have never previously been found to be expressed in subcultured cells. In the present study, immunocytochemistry and immunoblotting were performed to identify these
Javier Kattan et al.
Developmental dynamics : an official publication of the American Association of Anatomists, 230(1), 34-43 (2004-04-27)
To study the formation of the coronary vessels in the developing avian heart, we stained developmentally staged quail hearts with the endothelial specific antibody QH-1. QH-1 reacted with individual cells in the proepicardial organ in Hamburger and Hamilton stage (HH)
W Rozek et al.
Polish journal of veterinary sciences, 16(4), 663-669 (2013-01-01)
Changes in the level of cellular proteins in cells inoculated with equine influenza virus H7N7 and H3N8 were studied with microarray technique. H3N8 induced pro-apoptotic proteins while H7N7 induced both pro- as well as anti-apoptotic factors. The higher level of
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