Labelling Review row-Online

SNAP-25
Clone SP12
0.5 mL lyophilized NCL-SNAP-25 P (HIER) W
The release of neurotransmitters from neurons is regulated by exocytosis of
synaptic vesicles. Exocytosis is mediated by a complex consisting of
membrane components of both the synaptic vesicle and the synaptic plasma
membrane. Synaptosomal-associated protein of 25 kD (SNAP-25) is a
plasmalemmal protein and is one of four proteins which are thought to make
up an initial docking complex for regulated exocytosis. SNAP-25 lacks a
transmembrane domain, but is linked to the membrane by palmitoylated
cysteine residues in the central region of the molecule. SNAP-25 has been
reported to be expressed in tumor cells of prolactinomas, growth hormone
secreting tumors and the granule cell layer and molecular layers of the
cerebellum.
Human small bowel: immunohistochemical staining for SNAP-25 using NCL-SNAP-25.
Note intense cytoplasmic staining of neural elements. Paraffin section.
Spectrin Antibodies
Clone RBC2/3D5
1 mL lyophilized Spectrin (recommended for human use)
NCL-SPEC1 FWE
Clone RBC1/5B1
1 mL lyophilized Spectrin (broad spectrum) NCL-SPEC2 F
Spectrin is a cytoskeletal protein which has some structural homology with
dystrophin, the protein that is defective in Duchenne and Becker muscular
dystrophy. Subtle membrane damage frequently occurs during the excision
and freezing of muscle samples. Labeling for spectrin is necessary to
monitor membrane integrity. It is reported that fibers which show negative
labeling for both dystrophin and spectrin are damaged (or in the early stages
of regeneration), whereas fibers which are negative for dystrophin but
positive for spectrin reflect true abnormalities of dystrophin expression.
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.
Superoxide Dismutase (Cu/Zn)
Clone 30F11
1 mL lyophilized NCL-SOD1 P (HIER) W
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.
Surfactant Precursor Protein B
Clone 19H7
1 mL, 0.1 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.
F Frozen I Immunofluorescence E Electron microscopy
P Paraffin C Flow cytometry O Other applications
W Western blotting
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Primary Antibodies