Sources/Clones
Accurate/Novocastra (FPM1), Biodesign (polyclonal), Biogenesis (242.9, polyclonal), Dako (polyclonal), Fitzgerald (polyclonal), Serotec (polyclonal) and Zymed (UBI1).
Fixation/Preparation
This antibody is applicable to formalin-fixed, paraffin-embedded tissue sections.
Background
Ubiquitin is an 8.5 kD polypeptide found almost universally in plants and animals. The best documented function for ubiquitin involves its conjugation to proteins as a signal to initiate degradation via the ubiquitin-mediated proteolytic pathway (Jahngen-Hodge et al, 1992). Ubiquitin-mediated proteolysis is involved in the turnover of many short-lived regulatory proteins. This pathway leads to the covalent attachment of one or more multiubiquitin chains to target substrates which are then degraded by the 26S multicatalytic chains proteasome complex (Rolfe et al, 1997). Ubiquitin modification of a variety of protein targets within the cells also plays an important role in many cellular processes: regulation of gene expression, regulation of cell cycle and division, involvement in the cellular stress response, modification of cell surface receptors, DNA repair, import of proteins into mitochondria, uptake of precursors into neurons, and biogenesis of mitochondria, ribosomes and peroxisomes (Ciechanover & Schwartz, 1994).
Applications
Ubiquitin immunostaining has been shown to be a highly sensitive and specific method for the detection of Mallory bodies, thereby making it a valuable tool in the study of alcoholic liver disease, adding objectivity to the diagnosis of alcoholic hepatitis (Vyberg & Leth, 1991). In the human spongiform encephalopathies, ubiquitin immunoreactivity has been demonstrated in a punctate distribution at the periphery of prion protein amyloid plaques and in a finely granular pattern in the neurophil around and within areas of spongiform change (Ironside et al, 1993). Ubiquitin has also been simultaneously present with GFAP in the cytoplasm and cell processes of tumor cells of astrocytomas (Galloway & Likavec, 1989). The demonstration of ubiquitin immunolabeling in both ductus efferentes and ductus epididymidis epithelia has suggested that ubiquitinated proteins are secreted into the epididymal lumen (Fraile et al, 1996). Ubiquitin expression has been demonstrated in the lung and adrenal gland in autopsy cases that died by fire accident (Shoji, 1997), suggesting that the adrenal gland reacts strongly to heat shock. Evidence of ubiquitin-positive myocytic intranuclear or cytoplasmic inclusions or positive-staining rimmed vacuoles in the setting of an inflammatory myopathy may be suggestive of a diagnosis of inclusion body myositis (Prayson & Cohen, 1997). On the therapeutic front, prevention of p53 ubiquitination (and subsequent degradation) in human papilloma virus-positive cervical tumors should lead to programed cell death (Rolfe et al, 1997).
References
•Ciechanover A, Schwartz AL 1994. The ubiquitin-mediated proteolytic pathway: mechanisms of recognition of the proteolytic substrate and involvement in the degradation of native cellular proteins. FASEB Journal 8:182-191.
•Fraile B, Martin R, De Miquel MP et al 1996. Light and electron microscopic immunohistochemical localization of protein gene product 9.5 and ubiquitin immunoreactivities in the human epididymis and vas deferens. Biology of Reproduction 55: 291-297.
•Galloway PG, Likavec MJ 1989. Ubiquitin in normal, reactive and neoplastic human astrocytes. Brain Research 500: 343-351.
•Ironside JW, McCardle L, Hayward PA, Bell JE 1993. Ubiquitin immunocytochemistry in human spongiform encephalopathies. Neuropathology and Applied Neurobiology 19: 134-140
•Jahngen-Hodge J, Cyr D, Laxaman E, Taylor A 1992. Ubiquitin and ubiquitin conjugates in human lens. Experimental Eye Research 55: 897-902.
•Prayson RA, Cohen ML 1997. Ubiquitin immunostaining and inclusion body myositis: study of 30 patients with inclusion body myositis. Human Pathology 28: 887-892.
•Rolfe M, Chiu MI, Pagano M 1997. The ubiquitin-mediated proteolytic pathway as a therapeutic area. Journal of Molecular Medicine 75: 5-17.
•Shoji T 1997. Demonstration of heat shock protein, ubiquitin, in fire death autopsy cases by immunohistochemical study: Nippon Hoigaku Zasshi 51: 70-76
•Vyberg M, Leth P 1991. Ubiquitin: an immunohistochemical marker of Mallory bodies and alcoholic liver disease. APMIS Supplement 23: 46-52
Bibliografia
Manual of diagnostic antibodies for immunohistology / Anthony S.-Y. Leong, Kumarasen Cooper, F. Joel W.-M. Leong.
Accurate/Novocastra (FPM1), Biodesign (polyclonal), Biogenesis (242.9, polyclonal), Dako (polyclonal), Fitzgerald (polyclonal), Serotec (polyclonal) and Zymed (UBI1).
Fixation/Preparation
This antibody is applicable to formalin-fixed, paraffin-embedded tissue sections.
Background
Ubiquitin is an 8.5 kD polypeptide found almost universally in plants and animals. The best documented function for ubiquitin involves its conjugation to proteins as a signal to initiate degradation via the ubiquitin-mediated proteolytic pathway (Jahngen-Hodge et al, 1992). Ubiquitin-mediated proteolysis is involved in the turnover of many short-lived regulatory proteins. This pathway leads to the covalent attachment of one or more multiubiquitin chains to target substrates which are then degraded by the 26S multicatalytic chains proteasome complex (Rolfe et al, 1997). Ubiquitin modification of a variety of protein targets within the cells also plays an important role in many cellular processes: regulation of gene expression, regulation of cell cycle and division, involvement in the cellular stress response, modification of cell surface receptors, DNA repair, import of proteins into mitochondria, uptake of precursors into neurons, and biogenesis of mitochondria, ribosomes and peroxisomes (Ciechanover & Schwartz, 1994).
Applications
Ubiquitin immunostaining has been shown to be a highly sensitive and specific method for the detection of Mallory bodies, thereby making it a valuable tool in the study of alcoholic liver disease, adding objectivity to the diagnosis of alcoholic hepatitis (Vyberg & Leth, 1991). In the human spongiform encephalopathies, ubiquitin immunoreactivity has been demonstrated in a punctate distribution at the periphery of prion protein amyloid plaques and in a finely granular pattern in the neurophil around and within areas of spongiform change (Ironside et al, 1993). Ubiquitin has also been simultaneously present with GFAP in the cytoplasm and cell processes of tumor cells of astrocytomas (Galloway & Likavec, 1989). The demonstration of ubiquitin immunolabeling in both ductus efferentes and ductus epididymidis epithelia has suggested that ubiquitinated proteins are secreted into the epididymal lumen (Fraile et al, 1996). Ubiquitin expression has been demonstrated in the lung and adrenal gland in autopsy cases that died by fire accident (Shoji, 1997), suggesting that the adrenal gland reacts strongly to heat shock. Evidence of ubiquitin-positive myocytic intranuclear or cytoplasmic inclusions or positive-staining rimmed vacuoles in the setting of an inflammatory myopathy may be suggestive of a diagnosis of inclusion body myositis (Prayson & Cohen, 1997). On the therapeutic front, prevention of p53 ubiquitination (and subsequent degradation) in human papilloma virus-positive cervical tumors should lead to programed cell death (Rolfe et al, 1997).
References
•Ciechanover A, Schwartz AL 1994. The ubiquitin-mediated proteolytic pathway: mechanisms of recognition of the proteolytic substrate and involvement in the degradation of native cellular proteins. FASEB Journal 8:182-191.
•Fraile B, Martin R, De Miquel MP et al 1996. Light and electron microscopic immunohistochemical localization of protein gene product 9.5 and ubiquitin immunoreactivities in the human epididymis and vas deferens. Biology of Reproduction 55: 291-297.
•Galloway PG, Likavec MJ 1989. Ubiquitin in normal, reactive and neoplastic human astrocytes. Brain Research 500: 343-351.
•Ironside JW, McCardle L, Hayward PA, Bell JE 1993. Ubiquitin immunocytochemistry in human spongiform encephalopathies. Neuropathology and Applied Neurobiology 19: 134-140
•Jahngen-Hodge J, Cyr D, Laxaman E, Taylor A 1992. Ubiquitin and ubiquitin conjugates in human lens. Experimental Eye Research 55: 897-902.
•Prayson RA, Cohen ML 1997. Ubiquitin immunostaining and inclusion body myositis: study of 30 patients with inclusion body myositis. Human Pathology 28: 887-892.
•Rolfe M, Chiu MI, Pagano M 1997. The ubiquitin-mediated proteolytic pathway as a therapeutic area. Journal of Molecular Medicine 75: 5-17.
•Shoji T 1997. Demonstration of heat shock protein, ubiquitin, in fire death autopsy cases by immunohistochemical study: Nippon Hoigaku Zasshi 51: 70-76
•Vyberg M, Leth P 1991. Ubiquitin: an immunohistochemical marker of Mallory bodies and alcoholic liver disease. APMIS Supplement 23: 46-52
Bibliografia
Manual of diagnostic antibodies for immunohistology / Anthony S.-Y. Leong, Kumarasen Cooper, F. Joel W.-M. Leong.
