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> Lycopersicon esculentum Lectin (LEL, Tomato Lectin, TL) (Biotin)

Lycopersicon esculentum Lectin (LEL, Tomato Lectin, TL) (Biotin)

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Référence L7785-25B-1mg

Conditionnement : 1mg

Marque : US Biological

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L7785-25B Lycopersicon esculentum Lectin (LEL, Tomato Lectin, TL) (Biotin)

Lycopersicon esculentum Lectin
Mouse pancreas in a vessel patency and drug delivery assay using L7785-25B: (A) Ascinar Cells; (D) Ductal Cells; (I) Islet Cells. Functional vasculature labeled by injecting mouse with Lycopersicon Esculentum Lectin. Biotinylated Lycopersicon Esculentum Lectin is preincubated with streptavidin fluorophore (red) prior to injection. Drug delivery is evaluated by coadministering doxorubicin, an autofluorescent, small-molecule drug, with lectin (note green nuclei). DAPI counterstain (blue). Courtesy of Michael A Jacobetz, Cancer Research UK, Cambridge Research Institute, Cambridge, UK. Kenneth P. Olive, et al. Science 324, 1457 (2009); DOI: 10.1126/science.1171362.
Lycopersicon esculentum Lectin
Frozen section of colon using L7785-25B viewed under fluorescein filter, lycopersicon esculentum Lectin (orange staining) and glandular epithelium (green fluorescein label)
Grade
Molecular Biology Grade
Shipping Temp
Blue Ice
Storage Temp
-20°C

Tomato lectin is a very stable glycoprotein containing about 50 percent arabinose and galactose. This lectin is composed of a single polypeptide of about 100,000D that may form aggregates in solution. Like other lectins that bind N-acetylglucosamine oligomers, tomato lectin prefers trimers and tetramers of this sugar. Tomato lectin, although sharing some specificities with potato, Datura lectin and wheat germ agglutinin, has been reported to be dissimilar in many respects. Tomato lectin binds well to such glycoproteins as glycophorin and Tamm-Horsfall glycoprotein. The tomato lectin complements our existing range of lectin reagents and should be a valuable tool in examining rodent tumor angiogenesis, tracing neovascular development in xenograft models and brain research. Tomato lectin (from Lycopersicon esculentum) is an effective marker of blood vessels and microglial cells in rodents. Conjugation of the lectin with biotin facilitates detection and visualization using intravascular perfusion methods or direct application to tissue sections. This biotinylated lectin conjugate is prepared from affinity-purified lectin and is optimally labeled with biotin. Essentially free of inactive lectin conjugate and containing no free biotin, this biotinylated lectin provides an ideal intermediate for examining glycoconjugates using the Biotin-Avidin System. First the biotin-labeled lectin is added, followed by an ABC Reagent, Avidin D conjugate, or streptavidin derivative. Another possible application is in the isolation of lymphokines and other products of mitogenic stimulation.

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

Recommended Dilutions:
Optimal dilutions to be determined by the researcher.

Sugar Specificity:
[GlcNac]1-3, N-Acetylglucosamine

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 6 months after receipt 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.

Applications
Source: Isolated from tomato fruit|Concentration: ~2mg/ml (after reconstitution)|Form: Supplied as a powder in 10mM HEPES, pH 7.5, 0.15M sodium chloride, 0.08% sodium azide, 0.1mM Ca++. Reconstitute with 500ul dH2O. Labeled with Biotin.||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.
Form
Supplied as a liquid in 10mM HEPES, pH 7.5, 0.15M sodium chloride, 0.08% sodium azide, 0.1mM Ca++. Labeled with Biotin.
References
1. Debbage, P.L., et al., Lectin intravital perfusion studies in tumor-bearing mice: Micrometer-resolution, wide-area mapping of microvascular labeling, distinguishing efficiently and inefficiently perfused microregions in the tumor. J. Histochem Cytochem, 1998. 46(5):p. 627-639. 2. Thurston, G., et al., Cationic liposomes target angiogenic endothelial cells in tumors and chronic inflammation in mice. J. Clin Invest, 1998. 101(7):p.1401-1413. 3. Hashizume, H., et al., Openings between defective endothelial cells explain tumor vessel leakiness. Amer J Pathol, 2000. 156(4):p.1363-1380. 4. Debbage, P.L., et al., Intravital lectin perfusion analysis of vascular permeability in human micro- and macro- blood vessels. Histochemistry Cell Biol, 2001. 116(4):p.349-359. 5. Lee, J.C., et al., Interleukin-12 inhibits angiogenesis and growth of transplanted but not in situ mouse mammary tumor virus-induced mammary carcinomas. Cancer Res, 2002. 62(3):p.747-755. 6. Akerman, M.E., et al., Nanocrystal targeting in vivo. Proc Nat Acad Sci Usa, 2002. 99(20):p.12617-12621. 7. Gee, M.S., et al., Tumor vessel development and maturation impose limits on the effectiveness of anti-vascular therapy. Amer J Pathol, 2003. 162(1):p.183-193. 8. Jilani, S.M., et al., Selective binding of lectins to embryonic chicken vasculature. J Histochem Cytochem, 2003. 51(5):p.597-604. 9. Krasnici, S., et al., Effect of the surface charge of liposomes on their uptake by angiogenic tumor vessels. Int J Cancer, 2003. 105(4):p.561-567. 10. Huang, J.Z. et al., Regression of established tumors and metastases by potent vascular endothelial growth factor blockade. Proc Nat Acad Sci Usa, 2003. 100(13):p.7785-7790. 11. Inai, T., et al., Inhibition of vascular endothelial growth factor (VEGF) signaling in cancer causes loss of endothelial fenestrations, regression of tumor vessels, and appearance of basement membrane ghosts. Amer J Pathol, 2004. 165(1):p.35-52.