Labelling Review row-Online

Primary Antibodies
Villin
Clone CWWB1
1 mL, 0.1 mL lyophilized NCL-VILLIN F P (HIER) W
1 mL liquid NCL-L-VILLIN F P (HIER) W
7 mL Bond ready-to-use PA0106 P (HIER)
Villin and the structurally-related proteins gelsolin, fragmin and severin, all
regulate the framework and assembly of actin. Villin is unique among these
proteins in its ability to cross-link actin filaments into bundles, a process
observed only at low Ca 2+ concentration. Villin is composed of three
domains. The first two domains are homologous and the third domain is
called the “headpiece”. This “headpiece” region is located at the C-terminus.
Villin is mainly produced by epithelial cells that develop a brush border. Cells
producing villin are reported to be found either in the epithelial cells of the
intestinal mucosa and gall bladder, or in epithelial cells of the kidney
proximal tubules and ductuli efferentes of the testis. However, villin is also
reported to be found in some epithelia which lack a brush border but which
are derived from embryonic gut such as duct cells of the exocrine pancreas
and biliary cells of the liver. In these cell types, villin is concentrated in the
apical cytoplasm. Epithelial cells of the intestinal mucosa are continually
being renewed and this involves a migration of these cell types from the
intestinal crypts to the tips of the villi, gradually acquiring their differentiated
phenotype as they do so. The maximum production of villin occurs at the
base of the villus. Villin, therefore, shows tissue-specific expression being
restricted to certain epithelia and their apical domains, thus indicating their
polarity. The morphological loss of polarity of colonic epithelial cells is
reported to be one of the most significant indicators of dysplasia or
neoplasia.
Refer to page 43 for the Bond ready-to-use format.
Vimentin
Clone SRL33
1 mL, 0.1 mL liquid NCL-L-VIM-572 P (HIER) W
7 mL Bond ready-to-use PA0033 P (HIER)
Clone V9
1 mL, 0.1 mL lyophilized NCL-VIM-V9 F P (HIER) W
1 mL liquid NCL-L-VIM-V9 F P (HIER) W
7 mL ready-to-use RTU-VIM-V9 F P (HIER)
Clone VIM 3B4
1 mL lyophilized NCL-VIM F P (Enzyme) W
Eukaryotic cells contain a number of types of cytoplasmic filamentous
proteins, microtubule, microfilaments and intermediate-sized filaments (IF).
Vimentin, a 57 kD protein that is an intermediate filament is reported to be
expressed in most cells of mesenchymal origin, including fibroblasts,
endothelial cells, smooth muscle, melanocytes as well as T and B
lymphocytes.
Refer to page 43 for the Bond ready-to-use format.
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Reference Range
Astrocytoma: immunohistochemical staining for vimentin using NCL-L-VIM-572.
Note intense cytoplasmic staining of astrocytes. Paraffin section.
WAF1 Protein (p21, C1P1)
Clone 4D10
1 mL, 0.1 mL lyophilized NCL-WAF-1 P (HIER)
1 mL liquid NCL-L-WAF-1 P (HIER)
The gene encoding WAF1, also termed p21, is transcriptionally regulated by
the suppressor protein, p53. Overexpression of WAF1 is growth suppressive,
possibly by inhibiting the activity of cyclin/CDK complexes. One
consequence of WAF1 binding to cyclin/CDK complexes is the inhibition of
Rb protein phosphorylation. Induction of WAF1 expression requires wild
type p53 activity in cells undergoing p53 dependent G1 arrest or apoptosis.
Mutation of the p53 gene is a common event in human cancer and results in
the failure to produce WAF1. The effect of this may lead to uncontrolled cell
proliferation.
Wilms' Tumor
Clone WT49
1 mL, 0.1 mL liquid NCL-L-WT1-562 P (HIER)
7 mL Bond ready-to-use PA0562 P (HIER)
Wilms' tumor protein (WT1) has a role in transcriptional regulation and is
expressed in the kidney and a subset of hematopoietic cells. Alteration of
transcription factor function is a common mechanism in oncogenesis. The
WT1 protein contains a DNA binding domain and any deletions or point
mutations of the WT1 gene which destroy this activity result in the
development of the childhood nephroblastoma Wilms' tumor and Denys-
Drash syndrome. The description of WT1 involvement in nephroblastoma is
not clear. Expression of WT1 protein by immunohistochemistry is never
observed (or exceptionally rare) in breast cancer and negativity is
considered a useful marker to distinguish breast carcinoma metastases
from serous ovary primary carcinomas. This is at variance with observations
regarding mRNA in these tumors, but this is a still unresolved and complex
issue.
Product Specific Information
Endothelial cells are prevalently negative using clone WT49. These cells are
otherwise immunoreactive with clone 6FH2.
Refer to page 44 for the Bond ready-to-use format.
Products in this catalog are subject to regulatory approval.
This catalog is not for use in the USA.
Reference Range