Lectins
Cayman Chemical Cholesteryl Eicosapentaenoate
A potent and selective VEGFR2 inhibitor selective for VEGFR2 over VEGFR1 PDGFRB FGFR1 EGFR and ErbB2 at concentrations greater than 50 UM inhibits VEGF-A-stimulated cell proliferation of HUVECs (IC50 8 nM)
Enterprise Technology Solutions Lotus Dual Monitor Arm Kit
Lotus Dual Monitor Arm Kit For 26 Monitors Silver Supports 13 Lb
Vector Laboratories Sambucus Nigra Lectin (SNA, EBL) Fluorescein-labeled 2 mg
Sambucus nigra lectin (SNL) is isolated from elderberry bark and binds preferentially to sialic acid attached to terminal galactose in a-2,6 and to a lesser degree, a-2,3 linkage. Also called SNA (Sambucus nigra agglutinin) and EBL (elderberry lectin), SNL can inhibit cell-free protein synthesis. Binding is also inhibited to some extent by lactose or galactose. This lectin does not appear to bind sialic acid linked to N-acetylgalactosamine. SNA has been reported to inhibit cell-free protein synthesis. This fluorescein-labeled SNL features a ratio of fluorophores to lectin protein that provides optimal staining (excitation 495 nm, emission 515 nm). Supplied as a solution essentially free of unconjugated fluorophores, it is preserved with sodium azide. The recommended inhibiting/eluting sugar is 500 mM lactose in buffered saline followed by 500 mM lactose in acetic acid.
Vector Laboratories Lycopersicon esculentum lectin (LEL, TL) Biotinylated 1 mg
Lycopersicon esculentum lectin (LEL or tomato lectin, TL) binds well to glycophorin and Tamm-Horsfall glycoprotein and has been used effectively to label vascular endothelium in rodents. This conjugate features a ratio of biotin to lectin protein that provides optimal avidin/streptavidin and lectin binding activity. Supplied essentially free of unconjugated biotins, it is preserved with sodium azide.
Vector Laboratories Lycopersicon Esculentum (Tomato) Lectin (LEL, TL), Texas Red 1 mg
Lycopersicon esculentum lectin (LEL or tomato lectin, TL), binds to glycophorin and Tamm-Horsfall glycoprotein and has been used effectively to label and image vascular endothelium in rodents. This Texas Red conjugate features a ratio of fluorochrome to lectin protein that provides optimal staining (excitation 595 nm, emission 615 nm). It is supplied essentially free of unconjugated biotins and preserved with sodium azide.
Vector Laboratories Biotinylated Lectin Kit III
Vector Laboratories lectin screening kits are designed to provide the investigator with a panel of seven biotinylated lectins with different sugar specificities. Lectin Kit III consists of 0.5 mg of the following lectin conjugates: DSL, ECL, GSL II, Jacalin, LEL, STL, VVL. These biotinylated lectins are essentially free of inactive lectin and free biotin and provide ideal intermediates for detecting glycoconjugates using a standard VECTASTAIN ABC Kit.
Vector Laboratories Griffonia (Bandeiraea) Simplicifolia Lectin I (GSL I, BSL I), Fluorescein-labeled 5 mg
Griffonia simplicifolia lectin I (GSL I) is a family of glycoproteins w/ molecular weights of approximately 114 kDa. 2 subunits ("A" & "B") have slightly different molecular weights & combine to form tetrameric structures, resulting in five isolectins. The "A"-rich lectin preferentially agglutinates blood group A erythrocytes & appears to be specific for α-N-acetylgalactosamine residues, while the "B"-rich lectin preferentially agglutinates blood group B cells & is specific for α-galactose residues. Our GSL I is a mixture of the five isolectins & binds several glycoproteins, including laminin. This fluorescein-labeled GSL I features a ratio of fluorophores to lectin protein that provides optimal staining (excitation 495 nm, emission 515 nm). Supplied as a solution essentially free of unconjugated fluorophores, it is preserved with sodium azide. The recommended inhibiting/eluting sugar is a mixture of 200 mM galactose & 200 mM N-acetylgalactosamine.
Vector Laboratories Erythrina Cristagalli Lectin (ECL, ECA) Fluorescein-labeled 5 mg
Erythrina cristagalli lectin (ECL, ECA) binds a carbohydrate structure frequently found in mammalian membrane and serum glycoproteins. Sialic acid substitution on this structure prevents binding, which allows the use of agarose-bound ECL to isolate or fractionate mammalian glycoproteins. ECL is useful for isolating human natural killer (NK) cells using negative selection panning. These cells lack accessible carbohydrate structures required for binding ECL and, unlike other mononuclear cells, do not adhere to ECL-coated dishes. High recovery of viable NK cells is possible. Adherent cells can also be recovered by incubation in galactose or lactose. This fluorescein-labeled lectin features a ratio of fluorophores to lectin protein that provides optimal staining (excitation 495 nm, emission 515 nm). Supplied as a solution essentially free of unconjugated fluorophores, it is preserved with sodium azide. The recommended inhibiting/eluting sugar is 200 mM lactose.
Vector Laboratories Phaseolus Vulgaris Leucoagglutinin (PHA-L) Unconjugated 5 mg
Peanut agglutinin (PNA) binds the T-antigen, a galactosyl (β-1,3) N-acetylgalactosamine structure present in many glycoconjugates, gangliosides, and other soluble and membrane-associated glycoproteins and glycolipids. With exceptions, the glycan that PNA binds PNA is normally sialylated, which prevents binding. PNA can distinguish between normal and tumor tissues and is used to assess malignancy in transitional mucosa. PNA binding is also used to measure cellular maturity in lymphoid tissues, to distinguish a variety of lymphocyte subpopulations in man and experimental animals, and measure the levels of lymphoid cell populations in many diseases. PNA has been used for fractionation of stem cells in mice for use in bone marrow transplantation across histocompatibility barriers. The inhibiting/eluting sugar is 200 mM galactose.
Vector Laboratories Griffonia (Bandeiraea) Simplicifolia Lectin I (GSL I, BSL I), Unconjugated 5 mg
Griffonia simplicifolia lectin I (GSL I) is a family of glycoproteins with molecular weights of approximately 114 kDa. Two subunits ("A" and "B") have slightly different molecular weights and combine to form tetrameric structures, resulting in five isolectins. The "A"-rich lectin preferentially agglutinates blood group A erythrocytes and appears to be specific for α-N-acetylgalactosamine residues, while the "B"-rich lectin preferentially agglutinates blood group B cells and is specific for α-galactose residues.