Search results for: Anti c Myc produced in rabbit
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Immunohistologic c-myc protein in benign breast disease and cancer.
We have studied the histopathology and differential distribution of the c-myc protein (Myc) in human breast tissues including 17 cases of infiltrating mammary carcinoma, 4 cases of fibroadenoma, 5 cases with fibrocystic changes, and 1 case of reduction mammoplasty (as a control). Using a sensitive immunohistochemical method on frozen tissue sections, both a rabbit polyclonal anti-c-myc antibody and a mouse monoclonal anti-c-myc antibody, H51C116, produced high levels of Myc staining in the nuclei of epithelial cells of infiltrating mammary carcinomas (30-90% of cells stained). In contrast, the nuclei of epithelial cells of fibroadenomas, and breast tissues with fibrocystic changes stained infrequently. We studied benign tissue surrounding the tumors in four cases; three were essentially negative, and one showed nuclear epithelial cell staining throughout the lobules. Sixteen of the tumors were examined in parallel, using formalin-fixed, paraffin-embedded samples. Immunohistological procedures for Myc produced uniform, intense epithelial cell cytoplasmic staining (8 cases); light epithelial cell cytoplasmic staining (5 cases) or were unstained (3 cases). We argue that the differences between frozen and paraffin sections are incompatible with the notion of simple displacement of nuclear Myc to the cytoplasm during fixation. Elevated levels of nuclear Myc in tumor cells and subsets of benign tissue are consistent with a role for Myc in mammary cell proliferation and tumorigenesis.N Tulchin, L Ornstein, I Bleiweiss, S Dikman, R Cardiff
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Distribution of the c-myc oncoprotein in normal and neoplastic tissues of the rat colon.
A rat model of 5-azoxymethane induced colon cancer was studied in order to correlate histopathological changes and the differential distribution of the c-myc protein. Weanling Fisher 344 rats were injected with three, one week apart, subcutaneous injections of 5-azoxymethane (AOM) (15 mg kg-1) and the animals were divided into low and high fat diet groups. Nine colon tumors, of varying degrees of malignancy, that developed in the AOM-treated rats, and sections of normal colonic mucosa were examined. A rabbit polyclonal anti-c-myc antibody produced nuclear staining at 1:100 dilution in cryostat frozen sections of the normal rat colonic mucosa and the colon tumors when prepared with a Cryostat Frozen Sectioning Aid (CFSA). The tissue localization of the c-myc antibody staining revealed: (1) in normal mucosa, nuclei of the basal portion of the mucosa; (2) in adenomatous polyps, nuclei at all levels of the mucosa; and (3) in a carcinoma in situ, intense staining of glandular epithelial cell nuclei at all levels within the tumor. This procedure may provide a sensitive method for detecting abnormal cells in the colonic epithelium that have an altered proliferative capacity.N Tulchin, L Ornstein, J Guillem, K O'Toole, M E Lambert, I B Weinstein
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Proteins encoded by v-myc and c-myc oncogenes: identification and localization in acute leukemia virus transformants and bursal lymphoma cell lines.
We have prepared an antiserum against a synthetic dodecapeptide whose sequence corresponds to the C terminus of the MC29 v-myc protein. This antiserum (anti-v-myc 12C) specifically precipitates the known gag-myc fusion proteins produced by the defective leukemia viruses MC29, CMII, and OK10, but does not react with gag-precursor or product proteins. In addition, proteins of 62 kd and 61/63 kd are precipitated by anti-v-myc 12C from OK10 and MH2 transformants, respectively. The serum also recognizes comigrating 62 kd proteins from three chicken bursal lymphoma cell lines and from the products of in vitro translation of c-myc-specific mRNA. All of these myc-related proteins are phosphorylated and all appear to be localized in the cell nucleus. In uninfected quail cells, anti-v-myc 12C also recognizes a candidate c-myc protein of 60 kd, which does not appear to be phosphorylated and is present in low levels relative to v-myc and lymphoma c-myc proteins.S R Hann, H D Abrams, L R Rohrschneider, R N Eisenman