Fibronectin is an adhesive glycoprotein with a molecular mass of 440kD. It is believed to be important for the formation of a provisional matrix that promotes cell adhesion and migration during wound healing. Its age-dependent increase in plasma and tissues may be accompanied in pathological states, especially in tumor growth, by its proteolytic breakdown by a number of neutral proteases. It has also shown that several of its proteolytic breakdown products exhibit unexpected and mostly harmful biological activities (1).
Suitable for use in ELISA, Western Blot and Immunohistochemistry. Other applications not tested.
ELISA: 1:30000 (1-,6)
Western Blot: 1:100 (1)
Optimal dilutions to be determined by the researcher.
Storage and Stability:
May be stored at 4°C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot and add glycerol (40-50%). Freeze at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
|Lysed bovine corneal endothelial cells and extracellular matrix.|
|Purified by Protein A/G affinity chromatography from culture supernatant.|
|Supplied as a liquid in PBS, pH 7.2, 15mM sodium azide.|
|Highly specific for fibronectin. There is no evidence for cross-reactivity with other connective tissue proteins (vitronectin, elastin, collagen, laminin). Cross-reacts with human and chicken fibronectin. Other species have not been tested. Epitope is located in the 120kD cell binding fragment. Can be used in ELISA, Western blotting, immunoprecipitation and immunostaining of frozen PLP-fixed sections of bovine and human tissues. The antibody inhibits integrin-mediated cell adhesion to the cell binding domain of fibronectin. It can be used to probe fibronectin conformation. Strong reaction is seen in ELISA with thrombospondin directly coated onto the microtiter well.|
|Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.|
1. Underwood PA, Dalton BA, Steele JG, Bennett FA, Strike P (1992) Anti-fibronectin antibodies that modify heparin binding and cell adhesion: evidence for a new cell binding site in the heparin binding region. J Cell Sci 102:833-845.|
2. Underwood PA, Steele JG, Dalton BA (1993) Effects of polystyrene surface chemistry on biological activity of solid phase fibronectin and vitronectin, analysed with monoclonal antibodies. J Cell Sci 104:793-803.
3. Di Girolamo N, Underwood PA, McCluskey PJ, Wakefield D (1993) Functional activity of plasma fibronectin in patients with Diabetes mellitis. Diabetes 42:1606-1613.
4. Dalton BA, McFarland CD, Underwood PA, Steele JG (1995) Role of heparin binding domain of fibronectin in attachment and spreading of human bone derived cells. J Cell Sci 108:2083-2092.
5. Underwood PA, Bean PA, Mitchell SM, Whitelock JM (2001) Specific affinity depletion of cell adhesion molecules and growth factors from serum. J Immunol Methods 247:217-224.
6. Underwood PA, Steele JG, Dalton BA, Bennett FA (1990) Solid phase monoclonal antibodies. A novel method of directing the function of biologically active molecules by presenting a specific orientation. J Immunol Methods 127:91-102.