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QF0159 Marketing Release Record

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Novocastra Glial Fibrillary Acidic<br />

Protein<br />

Clone GA5<br />

1 mL lyophilized NCL-GFAP-GA5 FP IVD<br />

7 mL BOND ready-to-use PA0026 P (HIER)<br />

Antigen Background<br />

Glial fibrillary acidic protein (GFAP) is an intermediate filament protein of<br />

52 kD reported to be expressed in glial cells eg astrocytes and ependymal<br />

cells. In the peripheral nervous system, GFAP has been reported to be<br />

expressed in Schwann cells, enteric glial cells and satellite cells of human<br />

sensory ganglia and in neoplastic tissues GFAP has been reported to be<br />

expressed in astrocytomas and ependymomas.<br />

Product Specific Information<br />

When using NCL-GFAP-GA5 the heat induced epitope retrieval (HIER)<br />

technique may improve staining in some cases.<br />

Novocastra Glucagon<br />

Polyclonal<br />

0.5 mL lyophilized NCL-GLUCp FP IVD<br />

Polyclonal<br />

7 mL BOND ready-to-use PA0594 P (HIER)<br />

Antigen Background<br />

Glucagon expression has been reported in the endocrine cells of the<br />

pancreatic islets and also in the mucosa of small and large intestine.<br />

Pancreatic glucagon, a peptide of 29 amino acids, has biological activities<br />

including glycogenolysis, lipolysis, gluconeogenesis and ketogenesis. These<br />

effects are all antagonistic to insulin action and, therefore, lead to increased<br />

blood sugar levels. The majority of glucagonomas are reported to arise from<br />

the pancreas and produce pancreatic glucagon. These tumors are found<br />

chiefly in the main body or tail of the pancreas.<br />

Human pancreas: immunohistochemical staining for Glucagon using NCL-GLUCp.<br />

Note cytoplasmic staining in the endocrine cells of the islets. Paraffin section.<br />

IVD<br />

IVD<br />

Novocastra Glucocorticoid Receptor<br />

Clone 4H2<br />

1 mL lyophilized NCL-GCR P (HIER) W<br />

RUO*<br />

The glucocorticoid receptor of molecular weight 90 kD has three main<br />

functional regions; the N-terminal modulating region, the DNA binding<br />

region and the C-terminal steroid binding region. The glucocorticoid<br />

receptor is reported to be widely distributed and expressed in many cultured<br />

cell lines eg CEM-C7. Glucocorticoid receptor is reported to be expressed in<br />

neoplastic cells of chronic lymphocytic leukemia (CLL). Two isoforms of<br />

glucocorticoid receptor exist; alpha and beta, with the alpha form usually<br />

the most abundant. The control of gene expression by glucocorticoids has<br />

been widely studied as a model for transcriptional regulation. Glucocorticoid<br />

receptors are reported to induce or repress the expression of genes in<br />

response to glucocorticoids, mediating such processes as cell growth,<br />

differentiation and apoptosis. Glucocorticoid receptors may also form a<br />

complex with heat shock protein 90 and in certain instances render the nonligand<br />

bound receptor transcriptionally inactive.<br />

Product Specific Information<br />

NCL-GCR is raised to the N-terminal modulating region.<br />

Human tonsil: immunohistochemical staining for glucocorticoid receptor using NCL-GCR.<br />

Note nuclear staining in a wide distribution of cell types. Paraffin section.<br />

Novocastra Glutathione S-Transferase<br />

(GST) Antibodies<br />

Clone 10H6<br />

1 mL lyophilized Glutathione S-Transferase (mu)<br />

NCL-GSTmu-437 P RUO*<br />

Clone LW29<br />

1 mL lyophilized Glutathione S-Transferase (pi)<br />

NCL-GSTpi-438 FP IVD<br />

The glutathione S-transferases (GSTs) are a multigene family of isoenzymes<br />

which catalyze the conjugation of glutathione to electrophilic substrates.<br />

These enzymes are involved in the detoxification of both endogenous and<br />

exogenous electrophiles which can react with cellular components such as<br />

DNA. The modification of DNA by reactive compounds can initiate carcinogenesis<br />

and the GSTs are believed to play a role in neutralizing carcinogens.<br />

The cytosolic GST isoenzymes have been classified into four evolutionary<br />

classes; alpha, mu, pi and theta. These isoenzymes are reported to be singly<br />

or multi-expressed in a variety of normal tissues, including stomach, bowel,<br />

brain, heart, liver, pancreas, breast, kidney and skin at differing levels. In<br />

gastric cancers, the levels of GSTalpha and pi are reported to differ from<br />

normal gastric tissue with GSTalpha showing decreased levels and GSTpi<br />

increased levels. High levels of GSTpi are reported in some breast cancer<br />

cells and have been associated with chemotherapeutic agents. Likewise, in<br />

human lung squamous cell carcinomas, high levels of GSTpi are reported to<br />

be associated with resistance to the drug cisplatin. The expression of<br />

GSTmu has been reported to be high in acute myeloid leukemias. GSTmu is<br />

also known to play a role in detoxification of epoxides released from<br />

cigarette smoke.<br />

F Frozen I Immunofluorescence E Electron microscopy<br />

P Paraffin C Flow cytometry O Other applications<br />

W Western blotting<br />

/67<br />

Primary Antibodies

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