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QF0159 Marketing Release Record

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Novocastra Gross Cystic Disease Fluid<br />

Protein-15<br />

Clone 23A3<br />

1 mL, 0.1 mL lyophilized NCL-GCDFP15 P (HIER)<br />

1 mL liquid NCL-L-GCDFP15 P (HIER)<br />

7 mL ready-to-use RTU-GCDFP15 P (HIER)<br />

7 mL BOND ready-to-use PA0350 P (HIER)<br />

Antigen Background<br />

Gross cystic disease of the breast is a benign premenopausal disorder in<br />

which cysts are a predominant pathological lesion. These cysts appear to be<br />

formed from excessive apocrine cystic secretions. This fluid is composed of<br />

several glycoproteins including a unique 15 kD monomer protein, GCDFP15. It<br />

has been reported that cytosolic analysis of normal tissue from all major<br />

organs has demonstrated GCDFP15 in apocrine epithelia, lacrimal,<br />

ceruminous and Moll's glands and in numerous serous cells of the<br />

submandibular, tracheal, bronchial, sublingual and minor salivary glands.<br />

Cytosol from breast carcinoma lesions are reported to contain GCDFP15 at a<br />

wide range of concentrations. The concentration is reported to be highest in<br />

more differentiated carcinomas and GCDFP15 shows only a few positive<br />

individual epithelial cells within lobules and small ducts in normal breast.<br />

Expression has also been reported in fibroadenomas within areas of apocrine<br />

metaplasia. GCDFP15 and prostate specific antigen are reported to be coexpressed<br />

in androgen receptor-positive breast tumors.<br />

Human breast, Paget's disease: immunohistochemical staining for gross cystic disease fluid<br />

protein (15 kD) using RTU-GCDFP15. Note variable cytoplasmic staining of tumor cells. Paraffin<br />

section.<br />

Novocastra Heat Shock Protein 27<br />

Clone 2B4<br />

1 mL lyophilized NCL-HSP27 FPW<br />

Prokaryotes and eukaryotes express a variety of heat shock proteins (Hsps)<br />

in response to stress, including sublethal heat shock, exposure to heavy<br />

metals, hormones and viral infection. Hsp27 (27 kD) is the most common<br />

small Hsp found in man. In breast tissue, it is reported that expression of<br />

Hsp27 is taken as evidence of a functional estrogen receptor pathway.<br />

Human breast carcinoma: immunohistochemical staining for Hsp27 using NCL-HSP27.<br />

Note intense cytoplasmic staining of tumor cells. Paraffin section.<br />

IVD<br />

RUO*<br />

IVD<br />

IVD<br />

IVD<br />

Novocastra Heat Shock Protein 70<br />

Clone 8B11<br />

1 mL lyophilized NCL-HSP70 P (HIER)<br />

The response of cells or organisms to stress, such as exposure to heat or<br />

chemicals, is associated with the induction of heat shock proteins. Heat<br />

shock protein 70 (Hsp70) is reported to have a protective role in ischemic<br />

disease, inflammation, infection and a potential role in antigen processing<br />

as well as a possible regulatory role in cytokine biosynthesis. Hsp70 exists in<br />

the cell in equilibrium between its free state, in the cytoplasm, and its bound<br />

state, protecting proteins in the nucleolus, perhaps either by helping refold<br />

some of the unfolded ribosomal proteins or by solubilizing the denatured<br />

ribosomal proteins to facilitate their turnover. During recovery from heat<br />

shock and as the nucleoli begin to return to their normal activities, most of<br />

the Hsp70 returns to the cytoplasm.<br />

Product Specific Information<br />

NCL-HSP70 is reactive with Hsp70 and heat shock cognate 70 (Hsc70) in man,<br />

mouse and rat.<br />

Novocastra Heat Shock Protein 105<br />

Clone 58F12<br />

1 mL lyophilized NCL-HSP105 P (HIER) W<br />

Heat shock protein 105 (Hsp105) exists as two isoforms; alpha and beta<br />

which belong to the Hsp105/Hsp110 protein family. Hsp105 acts as both a<br />

chaperone to prevent thermal aggregation of proteins and as a regulator of<br />

mammalian cells. The Hsp105 isoforms are reported to be found in the<br />

cytoplasm but not in the nucleoli under non-stressed and stressed conditions.<br />

In rodents, Hsp105 isoforms are reported to be moderately expressed<br />

in the adrenal glands, spleen, liver and heart and both are markedly<br />

increased after heat shock. In the testis, Hsp105 is specifically localized in<br />

the cytoplasm of germ cells but may translocate to the nucleus after heat<br />

shock. The most abundant expression of Hsp105 occurs in the brain with<br />

nuclear and cytoplasmic expression in nearly all neurons, oligodendrocytes,<br />

microglia and astrocytes. Increased expression reported during<br />

embryogenesis suggests that Hsp105 may have an important role during<br />

mouse development.<br />

Human brain, cerebellum: immunohistochemical staining for heat shock protein 105 using<br />

NCL-HSP105. Note intense cytoplasmic and nuclear staining of Purkinje cells and neuronal<br />

processes. Paraffin section.<br />

F Frozen I Immunofluorescence E Electron microscopy<br />

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

W Western blotting<br />

IVD<br />

RUO*<br />

/69<br />

Primary Antibodies

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