Labelling Review row-Online

Alpha Smooth Muscle Actin (SMA)
Clone �sm-1
1 mL lyophilized NCL-SMA F P (Enzyme) W
7 mL ready-to-use RTU-SMA F P (Enzyme)
7 mL Bond ready-to-use PA0943 P
Cytoplasmic actins are part of the microfilament system of cytoskeletal
proteins. Smooth muscle actin is found in vascular walls, intestinal
muscularis mucosae and muscularis propria and in the stroma of various
tissues. It is also reported to be expressed in myofibroblasts and myoepithelial
cells and antibodies to SMA are reported to be a useful tool for the
identification of leiomyomas, leiomyosarcomas and pleomorphic adenomas.
When such antibodies are used in a differential diagnostic situation they
must be used within a panel of antibodies together with the clinical
presentation data and interpreted by a pathologist.
Product Specific Information
Enzyme pretreatment may enhance staining in some cases.
Refer to page 41 for the Bond ready-to-use format.
Alpha-Synuclein
Clone KM51
1 mL lyophilized NCL-ASYN P (HIER)
1 mL liquid NCL-L-ASYN P (HIER)
Alpha-synuclein is a protein of 140 amino acids and a member of the
synuclein family. It shares 61 percent sequence homology with betasynuclein
and is highly conserved between vertebrate species. It does not
possess a signal sequence suggesting that it is an intracellular protein. All
synucleins have an unusual organization based around the eleven residue
repeating motif and an alpha-helical secondary structure resembling those
found in the lipid-binding domain of exchangeable apolipoproteins, including
Apo E. This homology suggests a direct interaction of alpha-synuclein with
membranes consistent with its affinity for synaptosomes. The function of
alpha-synuclein may be to carry a target protein to the inner membrane of
nerve terminals or to the outer surface of synaptic vesicles. Western blot
analyses of highly purified Lewy bodies from Lewy body dementia brain
material has shown full-length, partially truncated and insoluble aggregates
of alpha-synuclein. Alpha-synuclein may be implicated in the formation of
Lewy bodies and the selective degeneration of neurons in sporadic
Parkinson's disease and Lewy body dementia.
Product Specific Information
Clone KM51 is specific for alpha-synuclein and unreactive with betasynuclein.
Pretreatment of tissue sections with 98 to 100 percent formic acid
is also recommended.
Human brain, Lewy body dementia: immunohistochemical staining for alpha synuclein using
NCL-L-ASYN. Note staining of alpha synuclein-containing Lewy bodies. Paraffin section.
Amyloid A Component
Clone mc1
1 mL lyophilized NCL-AAC P
Amyloidosis is a disease characterised by the deposition of amorphous
eosinophilic extracellular material in various body tissues forming confluent
masses and progressively replacing the parenchymatous cells of vital
organs, resulting in gradual loss of function and eventual death. Such
organs become enlarged, firm, pale in colour and develop a waxy texture. It
has been reported that the detection of amyloid A protein in human tissue
biopsies, eg renal or rectal biopsies by immunohistochemistry, to
characterise AA-type amyloidosis (secondary amyloidosis) is often
worthwhile as it may be difficult to observe in hematoxylin and eosin
preparations.
Amyloid P Protein
Clone B5
1 mL lyophilized NCL-AMP FP
Amyloid consists mainly of rigid, non-branching protein fibrils, together with
rod-like aggregates of a pentagonal shaped glycoprotein called amyloid P
protein. Amyloid P protein, also known as P component, comprises 10
percent of amyloid tissue and is present in all but the central nervous system
forms of amyloid. Amyloid P protein is a constituent of normal basement
membranes and the microfibrillary elastic fiber network.
Product Specific Information
NCL-AMP may be used for the identification of amyloid P protein in normal
human tissue and in amyloid deposits. NCL-AMP is only suitable for paraffinembedded
material when the tissue has been fixed in 70 percent ethanol.
Amyloid Precursor Protein
Clone 3G12
1 mL lyophilized NCL-APP-228 P (HIER)
Clone 40.10
1 mL lyophilized NCL-APP P (HIER)
Alzheimer's disease, the most common cause of dementia in the elderly,
exists in both familial and sporadic forms. Genetic studies have identified
three genes; beta-amyloid precursor protein (APP), Presenilin-1 and
Presenilin-2 which, when mutated, can cause familial forms of Alzheimer's
disease. APP and APP-like proteins are transmembrane glycoproteins with
a similar modular domain structure.
Product Specific Information
NCL-APP-228 and NCL-APP have been raised to the extracellular portion of
APP between the Kunitz protease inhibitor domain and the beta amyloid
region. This region shows the least homology with the APP-like proteins.
NCL-APP-228 and NCL-APP do not cross-react with APP-like proteins. NCL-
APP reacts with large pyramidal cells as well as smaller neurons, astrocytes
and microglia. NCL-APP-228 reacts with late-stage neurofibrillary tanglebearing
neurons, neuritic processes surrounding senile plaques and neuropil
threads in gray matter of Alzheimer's disease brain. Unmasking in 1mM EDTA
(pH8.0) in a pressure cooker may be required for up to 5 minutes in order for
NCL-APP-228 to work optimally.
F Frozen I Immunofluorescence E Electron microscopy
P Paraffin C Flow cytometry O Other applications
W Western blotting
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Primary Antibodies