QF0159 Marketing Release Record

Primary Antibodies
Product Specific Information
NCL-SPEC1 and NCL-SPEC2 recognize the beta chain of spectrin in
erythrocytes and muscle. NCL-SPEC1 reacts with human beta-spectrin
whereas NCL-SPEC2 reacts moderately with human beta-spectrin and
weakly with rabbit, rat, mouse and dog beta-spectrin.
Western blot: detection of human beta-spectrin (253 kD in muscle) using NCL-SPEC1. Lane A,
molecular weight markers. Lane B, urea extract of human muscle immunoblotted with
NCL-SPEC1.
Novocastra Superoxide Dismutase
(Cu/Zn)
Clone 30F11
1 mL lyophilized NCL-SOD1 P (HIER) W RUO* Superoxide
dismutase (SOD) is an enzyme which catalyzes the dismutation of
superoxide anion to oxygen and hydrogen peroxide. These enzymes are
metalloproteins classified according to the metal ion which is a necessary
cofactor for enzymic activity. Their function is to act as a cellular defence
mechanism against oxidative damage caused by superoxide radicals
produced as a by-product of aerobic metabolism. Almost all eukaryotic cells
have a mitochondrial and cytoplasmic SOD. The cytoplasmic enzyme is a
dimer of identical subunits with each subunit containing one Zn and one Cu
atom, the latter being involved as an electron acceptor in the dismutation
reaction. The distribution of cells containing the copper/zinc SOD enzyme
(SOD1) in the hippocampi from normal humans and individuals with
Alzheimer's disease (AD) has been studied. Reports indicated a higher level
of SOD1 in subsets of hippocampal neurons, pyramidal and granule cells, in
AD. The gene for SOD1 is carried on chromosome 21 and in Down's
syndrome, increased SOD1 activity reflects a gene dosage effect where
high levels of SOD1 mRNA have been identified. These individuals develop
an accelerated ageing of the brain and histopathological changes are
reminiscent to that of AD.
Novocastra Surfactant Precursor
Protein B
Clone 19H7
1 mL lyophilized NCL-SPPB P (HIER)
Pulmonary surfactant is a phospholipid-rich mixture that reduces the
surface tension at the alveolar air-liquid interface, providing alveolar
stability necessary for normal ventilation. Four distinct proteins which have
been isolated from pulmonary surfactant are SP-A, SP-B, SP-C and SP-D.
Surfactant precursor protein B (pro-SP-B) with a molecular weight of 42 kD
undergoes proteolytic processing resulting in a 9 kD non-collagenous
hydrophobic pulmonary surfactant, SP-B. SP-B mRNA has been detected in
both type II cells and in bronchiolar epithelial cells of adult human, mouse,
rat and rabbit lung. Pro-SP-B protein and SP-B mRNA have been reported to
be found in approximately 60 percent and 53 percent of pulmonary
adenocarcinomas, respectively, with expression noted in adenocarcinomas
with acinar, papillary, bronchoalveolar and solid growth patterns. Squamous
cell and large cell carcinomas of the lung and nonpulmonary adenocarcinomas
are reported not to express pro-SP-B or SP-B.
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RUO*
Human lung adenocarcinoma: immunohistochemical staining for surfactant precursor protein
B using NCL-SPPB. Note cytoplasmic staining of Clara cells and extracellular protein. Paraffin
section.
Novocastra Surfactant Protein A
Clone 32E12
1 mL lyophilized NCL-SP-A P (HIER)
Antigen Background
Pulmonary surfactant plays a critical role in maintaining the structural
integrity of the respiratory epithelium by reducing surface tension during
expiration. It is a lipoprotein complex which is synthesized and secreted into
the alveoli of the lung by type II pneumocytes. Lung surfactant protein-A (SP-
A) is a major phospholipid-associated glycoprotein in surfactant and is a
member of the C-type lectin superfamily that also inhibits lipid secretion and
enhances the uptake of phospholipid by alveolar type II cells. Levels of SP-A
in amniotic fluid are reported to reflect the degree of fetal lung maturity and
inadequate levels of surfactant at birth, a frequent occurrence in premature
infants, results in respiratory failure. In individuals with lung
adenocarcinomas, high concentrations of SP-A have been reported in pleural
effusions except in poorly differentiated lung adenocarcinomas where a
significant decrease of SP-A immunoreactivity has been reported (Zamecnik
J and Kodek R. Virchows Arch. 440(4): 353-61 (2002).
Novocastra Synaptic Vesicle Protein 2
Clone 15E11
1 mL lyophilized NCL-SV2 P (HIER)
Synaptic vesicle protein 2 (SV2) is an integral membrane glycoprotein. It is
required for normal neurotransmission and may play a role in the regulation
of calcium-stimulated exocytosis. SV2 exists in three isoforms, SV2A, SV2B
and SV2C, each containing 12 transmembrane spanning regions. SV2
proteins are reported to be among the most abundant and conserved
components of synaptic vesicles in vertebrates. They are present on all
small synaptic vesicles independent of transmitter type. SV2A and SV2B are
reported to be widely distributed in the nervous system, whereas SV2C is
only observed in a small number of neurons in a few areas of the brain. In
the brain, SV2A is reported to be expressed at the highest levels in
subcortical regions, whereas the highest level of expression of SV2B is in
the cortex and hippocampus. SV2 is also reported to be expressed on
secretory vesicles of neuroendocrine cells in the gastrointestinal tract,
pancreas, anterior pituitary gland, thyroid, parathyroid and adrenal medulla
and also in exocrine chief cells of gastric mucosa.
Product Specific Information
NCL-SV2 is raised to the N-terminal cytoplasmic region of the SV2A isoform.
IVD
RUO*
Products in this catalog are subject to regulatory approval.
Please consult your Leica Microsystems representative for availability in your region.
* For Research Use Only. Not for use in diagnostic procedures.