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> mouse Anti-Fibronectin (FN, Cold-insoluble Globulin, CIG) Monoclonal Antibody [Clone:IST-9]

mouse Anti-Fibronectin (FN, Cold-insoluble Globulin, CIG) Monoclonal Antibody [Clone:IST-9]

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Referência 368507-100ug

Tamanho : 100ug

Marca : US Biological

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368507 Fibronectin (FN, Cold-insoluble Globulin, CIG)

Clone Type
Monoclonal
Host
mouse
Source
human
Swiss Prot
P02751
Isotype
IgG1
Grade
Affinity Purified
Applications
E IC IHC WB
Crossreactivity
Bo Ca Ch Hu Mk Mo Po Rt
Shipping Temp
Blue Ice
Storage Temp
-20°C

Fibronectin is a major component of the extracellular matrix that binds to integrins, cell surfaces and various compounds including collagen, fibrin, heparin, DNA and actin. It occurs in two main forms: plasma and cellular fibronectin. EDA (Extra Domain A)-containing cellular fibronectin (EDA-FN) plays a major role in cell adhesion, growth, migration and differentiation and it is important for processes such as wound healing and embryonic development. It is associated with fibroblast differentiation by increasing alpha-SMA expression, collagen deposition, cell contractility and focal adhesion kinase (FAK) activation. EDA-FN promotes cell spread by interacting with the integrins alpha5-beta1, alpha4-beta1 and alpha9-beta1 and has been shown to promote angiogenesis, lymphangiogenesis and metastasis of colorectal tumors. In transformed or tumor-derived cells the EDA segment is about 10-times higher than in fibronectin from normal fibroblasts and it may therefore be a significant marker for malignancy.

Applications:
Suitable for use in ELISA, Western Blot, Immunohistochemistry, Immunocytochemistry and Blocking. Other applications not tested.

Recommended Dilutions:
Western Blot: 1:1000
Immunohistochemistry (Frozen): 1-2ug/ml
Immunohistochemistry (Paraffin): 2-10ug/ml
Immunocytochemistry: 1:200
Blocking: Inhibits binding of Fibronectin EDA domain to alpha5-beta1, alpha4-beta1 and alpha9-beta1 integrins. Inhibits cell adhesion mediated by alpha5-beta1, alpha4-beta1 and alpha9-beta1 integrins. Blocks the differentiation of fibroblasts into myo-fibroblasts and the TGF-beta1-triggered enhancement of alpha-smooth muscle actin and collagen type I.
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Applications
Product Type: Mab|Isotype: IgG1|Clone No: IST-9|Host: mouse|Source: human|Concentration: As Reported |Form: Supplied as a liquid in 20mM sodium phosphate, 150mM sodium chloride, pH 7.6. No preservative added. |Purity: Purified by immunoaffinity chromatography from concentrated hybridoma tissue culture supernatant. |Endotoxin: ≤0.04EU/ug (LAL).|Immunogen: Recombinant protein corresponding to Extra Domain A (EDA) region of human cellular Fibronectin.|Specificity: Recognizes an epitope located in the EDA sequence of human cellular fibronectin (FN). Does not detect extracellular FN (plasma FN). Species Crossreactivity: mouse, rat, monkey, porcine, canine, bovine and chicken.||Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
Immunogen
Recombinant protein corresponding to Extra Domain A (EDA) region of human cellular Fibronectin.
Form
Supplied as a liquid in 20mM sodium phosphate, 150mM sodium chloride, pH 7.6. No preservative added.
Purity
Purified by immunoaffinity chromatography from concentrated hybridoma tissue culture supernatant. |Endotoxin: ≤0.04EU/ug (LAL).
Specificity
Recognizes an epitope located in the EDA sequence of human cellular fibronectin (FN). Does not detect extracellular FN (plasma FN). Species Crossreactivity: mouse, rat, monkey, porcine, canine, bovine and chicken.
References
1. Monoclonal antibodies in the analysis of fibronectin isoforms generated by alternative splicing of mRNA precursors in normal and transformed human cells: L. Borsi, et al.; J. Cell Biol. 104, 595 (1987). 2. Localization of the cellular-fibronectin-specific epitope recognized by the monoclonal antibody IST-9 using fusion proteins expressed in E. coli: B. Carnemolla, et al.; FEBS Lett. 215, 269 (1987). 3. Molecular and immunologic differences in canine fibronectins from articular cartilage and plasma: N. Burton- Wurster & G. Lust; Arch. Biochem. Biophys. 269, 32 (1989). 4. Coordinate on codevelopmental modulation of alternative splicing of fibronectin pre-messenger RNA at ED-A, ED-B, and CS1 regions in human liver tumors: F. Oyama, et al.; Cancer Res. 53, 2005 (1993). 5. Endogenous fibronectin of blood polymorphonuclear leukocytes: immunochemical characterization and subcellular localization: R. Salcedo, et al.; Exp. Cell Res. 233, 25 (1997). 6. The fibronectin domain ED-A is crucial for myofibroblastic phenotype induction by transforming growth factor- beta1: G. Serini, et al.; J. Cell Biol. 142, 873 (1998). 7. Identification of two amino acids within the EIIIA (ED-A) segment of fibronectin constituting the epitope for two function-blocking monoclonal antibodies: Y.F. Liao, et al.; J. Biol. Chem. 274, 17876 (1999). 8. Engagement of alpha4beta7 integrins by monoclonal antibodies or ligands enhances survival of human eosinophils in vitro: J. Meerschaert, et al.; J. Immunol. 163, 6217 (1999). 9. Segmental antigen challenge increases fibronectin in bronchoalveolar lavage fluid: J. Meerschaert, et al.; Am. J. Respir. Crit. Care Med. 159, 619 (1999). 10. Deletion of the alternatively spliced fibronectin EIIIA domain in mice reduces atherosclerosis: M.H. Tan, et al.; Blood 104, 11 (2004). 11. Fibronectin-alpha4beta1 integrin interactions regulate metalloproteinase-9 expression in steatotic liver is- chemia and reperfusion injury: C. Moore, et al.; Am. J. Pathol. 170, 567 (2007). 12. Identification of the peptide sequences within the EIIIA (EDA) segment of fibronectin that mediate integrin alpha9beta1-dependent cellular activities: A.V. Shinde, et al.; J. Biol. Chem. 283, 2858 (2008).