P9318
Monoclonal Anti-Plectin antibody produced in mouse
clone 7A8, ascites fluid
Sign In to View Organizational & Contract Pricing.
Select a Size
About This Item
Conjugate:
unconjugated
Clone:
7A8, monoclonal
Application:
ARR, DB, ELISA (i), ICC, IF, IHC (f), WB
Citations:
9
biological source
mouse
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
7A8, monoclonal
mol wt
antigen 300 kDa
contains
15 mM sodium azide
species reactivity
marsupial (Ptoorous tridactylis PtK2 cell line), rat
technique(s)
dot blot: suitable, immunocytochemistry: suitable, immunohistochemistry (frozen sections): suitable, indirect ELISA: suitable, indirect immunofluorescence: 1:200 using unfixed frozen sections of rat heart, microarray: suitable, western blot: suitable
isotype
IgG1
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
rat ... Plec1(64204)
General description
Monoclonal Anti-Plectin (mouse IgG1 isotype) is derived from the 7A8 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse. Plectin is an abundant, high molecular weight, cytomatrix protein (300 kDa) found in a wide variety of tissue and cell types. Plectin is found in stratified and non-stratified epithelia, fibroblasts, endothelial cells and astrocytes, as well as in striated, smooth and cardiac muscle, but not in neurons.
Immunogen
plectin from rat glioma C6 cells
Application
Monoclonal Anti-Plectin antibody produced in mouse has been used in:
- ELISA
- immunoblot
- dot blot
- immunocytochemistry
- immunoelectron microscopy
Biochem/physiol Actions
Plectin plays a role in the cross-linking of intermediate filaments, the interlinking of intermediate filaments with microtubules and microfilaments and the anchoring of intermediate filaments to the plasma membrane and the nuclear membrane. It is a part of the signal transduction mechanism involving kinases A and C, because in vitro as well as in vivo phosphorylation of the protein by those kinases differentially affected its binding affinities to vimentin and lamin B.
The antibody recognizes an epitope located in the middle section of the rod domain of the plectin molecule, approximately halfway between the globular end domains. The kinase C phosphorylation site was found on the same terminal segment as this antibody epitope. The antibody specifically labels the 300 kDa band of plectin, however, lower M.W. band(s) may also be detected. The antibody stains filamentous structures on immunohistochemical staining of frozen tissue sections. The antibody inhibits the interaction of plectin with vimentin and lamin B. An additional application for this antibody is immunoelectronmicroscropy.
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.
Not finding the right product?
Try our Product Selector Tool.
Storage Class
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
新产品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Plectin isoforms as organizers of intermediate filament cytoarchitecture
Wiche G and Winter L
Bioarchitecture, 1(1), 14-20 (2011)
Daisuke Tsuruta et al.
The Journal of biological chemistry, 278(40), 38707-38714 (2003-07-18)
Within each hemidesmosome, alpha6beta4 integrin plays a crucial role in hemidesmosome assembly by binding to laminin-5 in the basement membrane zone of epithelial tissue. Recent analyses have implicated "specificity-determining loops" (SDLs) in the I-like domain of beta integrin in regulating
Plectin-1 as a novel biomarker for pancreatic cancer
Bausch D, et al.
Clinical Cancer Research, 17(2), 302-309 (2011)
T M Svitkina et al.
The Journal of cell biology, 135(4), 991-1007 (1996-11-01)
By immunogold labeling, we demonstrate that "millipede-like" structures seen previously in mammalian cell cytoskeletons after removal of actin by treatment with gelsolin are composed of the cores of vimentin IFs with sidearms containing plectin. These plectin sidearms connect IFs to
Kiyoko Uehara et al.
Anatomical record (Hoboken, N.J. : 2007), 293(12), 2034-2043 (2010-11-23)
The ultrastructural distribution of vimentin intermediate filaments (IFs) and localizations of the related proteins in sinus endothelial cells of the rat spleen was examined by confocal laser scanning and electron microscopy with detergent extraction, myosin-fragment 1 decoration, and immunogold labeling
Related Content
Datasheet
Datasheet
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service