Sources/Clones
Accurate (2B6F9, 568), American Research Products (568), Axcel/Accurate (polyclonal), Biodesign (1601, 1602, 120-5), Biogenesis (BIO-FIBTN-001, Bo, Rt, polyclonal), Biogenex (2755-8), Calbiochem (3E1, polyclonal), Caltag Laboratories, Cymbus Bioscience (FN4), Dako (polyclonal), EY Labs, Fitzgerald (polyclonal), Harlan Seralab/Accurate (2.3F9), Novocastra (polyclonal), Serotec (polyclonal), Sigma (FN-15, FN3-E2) and Zymed (Z068, FN12-8).
Fixation/Preparation
The antibody is well suited for both formalin-fixed, paraffin embedded sections and cryostat sections. Proteolytic predigestion with protease or pepsin of formalin-fixed tissue is recommended (Kirkpatrick & D'Ardenne, 1984).
Background
Fibronectin is a non-collagenous connective tissue glycoprotein found in association with both basement membranes and interstitial connective tissue (Stenman & Vaheri, 1978). The exact ultrastructural localization of fibronectin within the basement membrane is still controversial (Laurie et al, 1982). Fibronectin is ab-glycoprotein with a molecular weight of 44 kD, comprising two nearly identical subchains. It is widely distributed throughout many normal tissues including connective tissues, blood vessel walls and basement membranes. Some of the properties of fibronectin include forming crosslinks with fibrin in blood clots through factor XIII and binding to heparin and collagen. It is also thought to play a role in cellular adhesion, wound healing and tissue repair (Mosher & Fiocht, 1981). Antiserum to human fibronectin was produced from purified human material isolated from a pool of normal human plasma.
Applications
Fibronectin (and laminin) has been demonstrated to line cystic lumina and around tumor islands in adenoid cystic breast and salivary gland carcinomas (D'Ardenne et al, 1986). This pattern of distribution has been recommended as an aid to the diagnosis of these tumors, whilst the absence may have important prognostic implications with an aggressive outcome. Fibronectin immunoreactivity in breast adenoid cystic carcinomas is also useful to distinguish them from cribriform carcinoma, the latter being negative.
In a comparative study of epithelial neoplasms of gastrointestinal and salivary gland origin, the difficulty in distinguishing between fibronectin of epithelial and fibroblastic origin was emphasized (D'Ardenne et al, 1983). In addition, carcinoma fibronectin was sometimes but not invariably lost from epithelial cell surfaces, suggesting that loss of cell surface fibronectin was unlikely to serve as a useful diagnostic marker for malignancy. In soft tissue tumors, fibronectin was found to be most abundant in the stroma, both benign and malignant (D'Ardenne et al, 1984).
Comments
The major role of fibronectin is in the diagnosis of adenoid cystic carcinoma of the salivary gland and breast, with the latter being distinguished from cribriform carcinoma. Either adenoid cystic carcinoma or connective tissue stroma may be used as a positive control.
References
•D'Ardenne AJ, Burns J, Skyes BC, Bennett MK 1993. Fibronectin and type III collagen in epithelial neoplasms of gastrointestinal tract and salivary gland. Journal of Clinical Pathology 36: 756-763.
•D'Ardenne AJ, Kirkpatrick P, Sykes BC 1984. The distribution of laminin, fibronectin and interstitial collagen type III in soft tissue tumors. Journal of Clinical Pathology 37: 895-904.
•D'Ardenne AJ, Kirkpatrick P, Wells CA, Davies JD 1986. Laminin and fibronectin in adenoid cystic carcinoma. Journal of Clinical Pathology 39: 138-144.
•Kirkpatrick P, D'Ardenne AJ 1984. Effects of fixation and enzymatic digestion on the immunohistochemical demonstration of laminin and fibronectin in paraffin embedded tissue. Journal of Clinical Pathology 37: 639-644.
•Laurie GW, Leblond CP, Martin GR 1982. Localisation of type IV collagen, laminin, heparan sulphate proteoglycan and fibronectin to the basal lamina of basement membranes. Journal of Cell Biology 95: 340-344.
•Mosher DF, Fiocht L 1981. Fibronectin: review of its structure and possible functions. Journal of Investigative Dermatology 77: 175-180.
•Stenman S, Vaheri A 1978. Distribution of a major connective tissue protein, fibronectin, in normal human tissues. Journal of Experimental Medicine 147: 1054-1064.
Bibliografía
Manual of diagnostic antibodies for immunohistology / Anthony S.-Y. Leong, Kumarasen Cooper, F. Joel W.-M. Leong.
Accurate (2B6F9, 568), American Research Products (568), Axcel/Accurate (polyclonal), Biodesign (1601, 1602, 120-5), Biogenesis (BIO-FIBTN-001, Bo, Rt, polyclonal), Biogenex (2755-8), Calbiochem (3E1, polyclonal), Caltag Laboratories, Cymbus Bioscience (FN4), Dako (polyclonal), EY Labs, Fitzgerald (polyclonal), Harlan Seralab/Accurate (2.3F9), Novocastra (polyclonal), Serotec (polyclonal), Sigma (FN-15, FN3-E2) and Zymed (Z068, FN12-8).
Fixation/Preparation
The antibody is well suited for both formalin-fixed, paraffin embedded sections and cryostat sections. Proteolytic predigestion with protease or pepsin of formalin-fixed tissue is recommended (Kirkpatrick & D'Ardenne, 1984).
Background
Fibronectin is a non-collagenous connective tissue glycoprotein found in association with both basement membranes and interstitial connective tissue (Stenman & Vaheri, 1978). The exact ultrastructural localization of fibronectin within the basement membrane is still controversial (Laurie et al, 1982). Fibronectin is ab-glycoprotein with a molecular weight of 44 kD, comprising two nearly identical subchains. It is widely distributed throughout many normal tissues including connective tissues, blood vessel walls and basement membranes. Some of the properties of fibronectin include forming crosslinks with fibrin in blood clots through factor XIII and binding to heparin and collagen. It is also thought to play a role in cellular adhesion, wound healing and tissue repair (Mosher & Fiocht, 1981). Antiserum to human fibronectin was produced from purified human material isolated from a pool of normal human plasma.
Applications
Fibronectin (and laminin) has been demonstrated to line cystic lumina and around tumor islands in adenoid cystic breast and salivary gland carcinomas (D'Ardenne et al, 1986). This pattern of distribution has been recommended as an aid to the diagnosis of these tumors, whilst the absence may have important prognostic implications with an aggressive outcome. Fibronectin immunoreactivity in breast adenoid cystic carcinomas is also useful to distinguish them from cribriform carcinoma, the latter being negative.
In a comparative study of epithelial neoplasms of gastrointestinal and salivary gland origin, the difficulty in distinguishing between fibronectin of epithelial and fibroblastic origin was emphasized (D'Ardenne et al, 1983). In addition, carcinoma fibronectin was sometimes but not invariably lost from epithelial cell surfaces, suggesting that loss of cell surface fibronectin was unlikely to serve as a useful diagnostic marker for malignancy. In soft tissue tumors, fibronectin was found to be most abundant in the stroma, both benign and malignant (D'Ardenne et al, 1984).
Comments
The major role of fibronectin is in the diagnosis of adenoid cystic carcinoma of the salivary gland and breast, with the latter being distinguished from cribriform carcinoma. Either adenoid cystic carcinoma or connective tissue stroma may be used as a positive control.
References
•D'Ardenne AJ, Burns J, Skyes BC, Bennett MK 1993. Fibronectin and type III collagen in epithelial neoplasms of gastrointestinal tract and salivary gland. Journal of Clinical Pathology 36: 756-763.
•D'Ardenne AJ, Kirkpatrick P, Sykes BC 1984. The distribution of laminin, fibronectin and interstitial collagen type III in soft tissue tumors. Journal of Clinical Pathology 37: 895-904.
•D'Ardenne AJ, Kirkpatrick P, Wells CA, Davies JD 1986. Laminin and fibronectin in adenoid cystic carcinoma. Journal of Clinical Pathology 39: 138-144.
•Kirkpatrick P, D'Ardenne AJ 1984. Effects of fixation and enzymatic digestion on the immunohistochemical demonstration of laminin and fibronectin in paraffin embedded tissue. Journal of Clinical Pathology 37: 639-644.
•Laurie GW, Leblond CP, Martin GR 1982. Localisation of type IV collagen, laminin, heparan sulphate proteoglycan and fibronectin to the basal lamina of basement membranes. Journal of Cell Biology 95: 340-344.
•Mosher DF, Fiocht L 1981. Fibronectin: review of its structure and possible functions. Journal of Investigative Dermatology 77: 175-180.
•Stenman S, Vaheri A 1978. Distribution of a major connective tissue protein, fibronectin, in normal human tissues. Journal of Experimental Medicine 147: 1054-1064.
Bibliografía
Manual of diagnostic antibodies for immunohistology / Anthony S.-Y. Leong, Kumarasen Cooper, F. Joel W.-M. Leong.
