Characterization of a monoclonal antibody (SBU-1) made to the thymic rudiment of sheep.

A monoclonal antibody (SBU-1) was raised to sheep thymic rudiment by fusion of NSI myeloma cells with spleen cells from BALB/c mice immunized with thymic rudiment isolated from fetal sheep between 25-30 days of gestation. By employing the indirect immunoperoxidase technique the antigen recognized by SBU-1 was found to be present in the epithelial reticular cells of the fetal sheep thymus. The intensity of staining decreased as gestation progressed. In the adult thymus the antigen was mainly restricted to Hassall's corpuscles and occasional epithelial cells in the medulla. In addition, the antigen was also shown to be present in epithelial cells of the small intestine, the bronchiole, the keratinized epithelium of the rumen, and the epithelial cells of the kidney tubules. By use of immunofluorescence the antigen was shown to be present in most of the cells of wool follicles and the cortex of developing wool fibers. Western blotting of SBU-1 against the low-sulfur alpha-keratin proteins of wool confirmed that the antigen recognized by SBU-1 belongs to a family of keratins. It was concluded that SBU-1 was raised against alpha-keratin expressed by the epithelial cells of the thymic rudiment and that the expression of this antigen on the reticular network of the thymus declined with advancement of pregnancy.

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Immunocytochemical localization of tissue kallikrein in brain ventricular epithelium and hypothalamic cell bodies.

Journal of Histochemistry & Cytochemistry ◽

10.1177/33.9.3894505 ◽

1985 ◽

Vol 33 (9) ◽

pp. 951-953 ◽

Cited By ~ 33

Author(s):

J A Simson ◽

R Dom ◽

J Chao ◽

C Woodley ◽

L Chao ◽

...

Keyword(s):

Monoclonal Antibody ◽

Epithelial Cells ◽

Third Ventricle ◽

Immunoperoxidase Staining ◽

Tissue Kallikrein ◽

Immunocytochemical Localization ◽

Specific Monoclonal Antibody ◽

The Third ◽

Indirect Immunoperoxidase ◽

Rat Tissue

A specific monoclonal antibody against rat tissue kallikrein was used as the primary antibody for indirect immunoperoxidase staining of rat hypothalamus. Kallikrein was localized in the epithelial cells (ependyma) lining the third ventricle as well as in cell bodies of arcuate, supraoptic, paraventricular, and ventromedial nuclei.

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Characterization of a monoclonal antibody, RTE-21, that binds to keratohyalin granule-associated proteins in epithelial cells of human skin and thymus

Clinical Immunology and Immunopathology ◽

10.1016/0090-1229(86)90057-7 ◽

1986 ◽

Vol 41 (1) ◽

pp. 130-144 ◽

Cited By ~ 4

Author(s):

Andrew J. Laster ◽

Barton F. Haynes

Keyword(s):

Monoclonal Antibody ◽

Epithelial Cells ◽

Human Skin ◽

Associated Proteins ◽

Keratohyalin Granule

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S20.13 A monoclonal antibody against mucin derived from rat gastric surface epithelial cells and partial characterization of the epitope structure by enzyme immunoassay

Glycoconjugate Journal ◽

10.1007/bf01210195 ◽

1993 ◽

Vol 10 (4) ◽

pp. 345-346

Author(s):

M. Kurihara ◽

K. Ishihara ◽

H. Tanaka ◽

H. Eto ◽

S. Shimauchi ◽

...

Keyword(s):

Monoclonal Antibody ◽

Epithelial Cells ◽

Enzyme Immunoassay ◽

Partial Characterization ◽

Epitope Structure

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Keratin 14 protein in cultured nonparenchymal rat hepatic epithelial cells: Characterization of keratin 14 and keratin 19 as antigens for the commonly used mouse monoclonal antibody OV-6

Molecular Carcinogenesis ◽

10.1002/mc.2940070110 ◽

1993 ◽

Vol 7 (1) ◽

pp. 60-66 ◽

Cited By ~ 42

Author(s):

Hanne Cathrine Bisgaard ◽

David C. Parmelee ◽

Harold A. Dunsford ◽

Salvatore Sechi ◽

Snorri S. Thorgeirsson

Keyword(s):

Monoclonal Antibody ◽

Epithelial Cells ◽

Mouse Monoclonal Antibody ◽

Keratin 19 ◽

Keratin 14

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Characterization of a glycosphingolipid antigen defined by the monoclonal antibody MBr1 expressed in normal and neoplastic epithelial cells of human mammary gland.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)42669-x ◽

1984 ◽

Vol 259 (23) ◽

pp. 14773-14777

Author(s):

E G Bremer ◽

S B Levery ◽

S Sonnino ◽

R Ghidoni ◽

S Canevari ◽

...

Keyword(s):

Monoclonal Antibody ◽

Mammary Gland ◽

Epithelial Cells ◽

Human Mammary Gland ◽

Neoplastic Epithelial Cells

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Production and Characterization of a Monoclonal Antibody against Low-sulfur Component of Bovine Hair Keratin

Nihon Chikusan Gakkaiho ◽

10.2508/chikusan.62.114 ◽

1991 ◽

Vol 62 (2) ◽

pp. 114-121

Author(s):

Katsuhiko ARAI ◽

Ayako MATSUNAGA ◽

Kohkichi UEHARA

Keyword(s):

Monoclonal Antibody ◽

Hair Keratin ◽

Low Sulfur

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NO-tryptophan: a new small molecule located in the rat brain

European Journal of Histochemistry ◽

10.4081/ejh.2016.2692 ◽

2016 ◽

Vol 60 (3) ◽

Author(s):

A. Mangas ◽

J. Yajeya ◽

N. González ◽

S. Duleu ◽

M. Geffard ◽

...

Keyword(s):

Nitric Oxide ◽

Monoclonal Antibody ◽

Rat Brain ◽

Morphological Characteristics ◽

Mammalian Brain ◽

Immunoperoxidase Technique ◽

Specific Monoclonal Antibody ◽

Septal Nucleus ◽

Physiological Mechanisms ◽

Indirect Immunoperoxidase

<p>A highly specific monoclonal antibody directed against nitric oxide-tryptophan (NO-W) with good affinity (10<sup>-9 </sup>M) and specificity was developed. In the rat brain, using an indirect immunoperoxidase technique, cell bodies containing NO-W were exclusively found in the intermediate and dorsal parts of the lateral septal nucleus. No immunoreactive fibres were found in the rat brain. This work reports the first visualization and the morphological characteristics of cell bodies containing NO-W in the mammalian brain. The restricted distribution of NO-W in the rat brain suggests that this molecule could be involved in specific physiological mechanisms. </p>

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Functional Characterization of PM6/13, a β3-specific (GPIIIa/CD61) Monoclonal Antibody that Shows Preferential Inhibition of Fibrinogen Binding over Fibronectin Binding to Activated Human Platelets

Thrombosis and Haemostasis ◽

10.1055/s-0037-1614247 ◽

1998 ◽

Vol 79 (01) ◽

pp. 177-185 ◽

Cited By ~ 10

Author(s):

Ashia Siddiqua ◽

Michael Wilkinson ◽

Vijay Kakkar ◽

Yatin Patel ◽

Salman Rahman ◽

...

Keyword(s):

Monoclonal Antibody ◽

Platelet Aggregation ◽

Platelet Rich Plasma ◽

Functional Characterization ◽

Human Platelets ◽

Western Blots ◽

Activated Platelets ◽

Reducing Conditions ◽

Fibronectin Binding

SummaryWe report the characterization of a monoclonal antibody (MAb) PM6/13 which recognises glycoprotein IIIa (GPIIIa) on platelet membranes and in functional studies inhibits platelet aggregation induced by all agonists examined. In platelet-rich plasma, inhibition of aggregation induced by ADP or low concentrations of collagen was accompanied by inhibition of 5-hydroxytryptamine secretion. EC50 values were 10 and 9 [H9262]g/ml antibody against ADP and collagen induced responses respectively. In washed platelets treated with the cyclooxygenase inhibitor, indomethacin, PM6/13 inhibited platelet aggregation induced by thrombin (0.2 U/ml), collagen (10 [H9262]g/ml) and U46619 (3 [H9262]M) with EC50 = 4, 8 and 4 [H9262]g/ml respectively, without affecting [14C]5-hydroxytryptamine secretion or [3H]arachidonate release in appropriately labelled cells. Studies in Fura 2-labelled platelets revealed that elevation of intracellular calcium by ADP, thrombin or U46619 was unaffected by PM6/13 suggesting that the epitope recognised by the antibody did not influence Ca2+ regulation. In agreement with the results from the platelet aggregation studies, PM6/13 was found to potently inhibit binding of 125I-fibrinogen to ADP activated platelets. Binding of this ligand was also inhibited by two other MAbs tested, namely SZ-21 (also to GPIIIa) and PM6/248 (to the GPIIb-IIIa complex). However when tested against binding of 125I-fibronectin to thrombin stimulated platelets, PM6/13 was ineffective in contrast with SZ-21 and PM6/248, that were both potent inhibitors. This suggested that the epitopes recognised by PM6/13 and SZ-21 on GPIIIa were distinct. Studies employing proteolytic dissection of 125I-labelled GPIIIa by trypsin followed by immunoprecipitation with PM6/13 and analysis by SDS-PAGE, revealed the presence of four fragments at 70, 55, 30 and 28 kDa. PM6/13 did not recognize any protein bands on Western blots performed under reducing conditions. However Western blotting analysis with PM6/13 under non-reducing conditions revealed strong detection of the parent GP IIIa molecule, of trypsin treated samples revealed recognition of an 80 kDa fragment at 1 min, faint recognition of a 60 kDa fragment at 60 min and no recognition of any product at 18 h treatment. Under similar conditions, SZ-21 recognized fragments at 80, 75 and 55 kDa with the 55kDa species persisting even after 18 h trypsin treatment. These studies confirm the epitopes recognised by PM6/13 and SZ-21 to be distinct and that PM6/13 represents a useful tool to differentiate the characteristics of fibrinogen and fibronectin binding to the GPIIb-IIIa complex on activated platelets.

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