Phaseolus vulgaris lectin L (PHA-L) is isolated from red kidney beans and purified by affinity chromatography. It is a tetrameric protein with a molecular weight of 126 kDa, each subunit of about 31 kDa Phytohemagglutinin or PHA is a lectin or plant protein found mostly in red kidney beans. In medicine, it is mainly used to test cellular immunity. Although preliminary research suggests PHA could help with diabetes, weight loss, and overactive immune response, high amounts of this lectin are very toxic Lectins are a defense mechanism which all life forms appear to have. Essentially, they are a low level toxin. The purpose of lectins is to discourage other animals from eating that life form. By triggering a negative reaction in the predator, that life form is then viewed as an undesirable food source
Leucoagglutinin PHA-L is a plant lectin, which is transported by the neurons in the central nervous system PHA is a mixture of lectins isolated from the red kidney bean, Phaseolus vulgaris. PHA-L is the fraction of PHA that exhibits strong leukoagglutinating and mitogenic activity, but very little erythroagglutinating activity. This reagent is intended for use in in vitro activation of human and mouse leukocytes Phaseolus vulgaris lectin (PHA-L) is isolated from red kidney beans. It has a molecular weight of 126,000 and is made up of four subunits with an isoelectric point around pH 5.2. PHA-L has a carbohydrate specificity for complex oligosaccharides and elutes with bovine thyroglobulin or acetic acid. PHA-L is known as leu Biotin Conjugated Phaseolus vulgaris Lectin (Red Kidney Bean) -PHA-L-, 2mg . Product volume may vary. With the exception of Diagnostic Microbiology Products all biochemicals described are for research use only. The biochemical reagents are not designed for use in therapeutic or diagnostic applications. We are unable to ship to individuals
For lectin binding, the membrane was incubated in buffer A with l /m\ of lectin (Concanavalin A (ConA) or PHA-L, Sigma Chemicals) conjugated with horseradish peroxidase (HRP) for l h. Bound lectin was identified with a chemoluminescent detection system (ECL, Amer- sham Life Science Inc.) Phaseolus vulgaris lectin (PHA-L) is an affinity purified lectin made up of four subunits with carbohydrate specificity for complex oligosaccharides. PHA-L is known as leucoagglutinin and has high mitogenic and leucoagglutinating activity, and low erythroagglutinating activity. This lectin exhibits no agglutination with human erythrocytes. PHA-E differs from PHA-L in that the leucoagglutinin. In neuroscience, the anterograde labeling method is used to trace the path of efferent axons with PHA-L, a lectin from the kidney bean. A lectin (BanLec) from bananas inhibits HIV-1 in vitro. Achylectins, isolated from Tachypleus tridentatus, show specific agglutinating activity against human A-type erythrocytes Carbohydrate specific sites on the PHA-L lectin is extracted from the crystal structure and used in the investigation of the interactions with the sialic acid. These structures were optimized to obtain the most stable form of the compounds separately. The most stable structures have been used to analyze the interactions Phaseolus vulgaris lectin L (PHA-L) is isolated from red kidney beans and purified by affinity chromatography. It is a tetrameric protein with a molecular weight of 126 kDa, each subunit of about 31 kDa. The lectin recognizes and binds specifically to terminal galactose, N-acetylglucosamine and mannose residues of complex glycans on mammalian glycoproteins
Upon hESCs differentiation to hNP cells and hMP cells, PHA-L lectin binding increases, indicating an up-regulation in expression of complex N-type glycans containing β1-6 linked branches PHA-P, a lectin from Phaseolus vulgaris-P (red kidney bean), is the protein form of phytohemagglutinin (PHA). It consists of two closely related proteins, PHA-E and PHA-L, which agglutinate erythrocytes and lymphocytes, respectively. PHA is well-known as a selective T cell mitogen  A new neuroanatomical method for tracing connections in the central nervous system based on the anterograde axonal transport of the kidney bean lectin, Phaseolus vulgaris-leucoagglutinin (PHA-L) is described. The method, for which a detailed protocol is presented, offers several advantages over pres FITC Conjugated Phaseolus vulgaris Lectin (Red Kidney Bean) -PHA-L-, 2mg . Product volume may vary. With the exception of Diagnostic Microbiology Products all biochemicals described are for research use only. The biochemical reagents are not designed for use in therapeutic or diagnostic applications. We are unable to ship to individuals . The protein has a molecular weight of 126 kDa. It is isolated from red kidney beans by affinity chromatography. Also known as Leucoagglutinin (PHA-L), this lectin has high mitogenic and leucoagglutinating activity, but low erythroagglutinating.
Glycobiology 21:988-993 DOI 10.1093/glycob/cwr080. Hagerbaumer P, Vieth M, Anders M, Schumacher U. 2015. Lectin histochemistry shows WGA, PHA-L and HPA binding increases during progression of human colorectal cancer. Anticancer Research 35(10):5333-5339 PHA-L, like other lectins, is a metalloprotein with two bound metal ions (one Ca 2+ ion and one Mn 2+, a transition metal ion) per monomer in the vicinity of the sugar binding site (Hamelryck et al., 1996) Seed phytic acid reduces mineral bioavailability by chelating minerals. Consumption of common bean seeds with the low phytic acid 1 (lpa1) mutation improved iron status in human trials but caused adverse gastrointestinal effects, presumably due to increased stability of lectin phytohemagglutinin L (PHA-L) compared to the wild type (wt) Vector Laboratories fluorescein labeled l pha. Phaseolus vulgaris Leucoagglutinin PHA L is the name ascribed to a family of lectins each of which consists of four subunits There are two different types of subunits One appears to be involved primarily in red cell agglutination and has been designated the E subunit for erythroagglutinin The other. Lectin phytohemagglutinin-L (PHA-L) is strongly inhibited by N-acetylglucosamine β(1-2) mannopyranosyl residues. This lectin has been shown to agglutinate leukocytes and induce mitogenic activity in T-lymphocytes and has also been used as an anterograde tracer for the study of neuronal pathways
PHA-L N128-->D was obtained and the mutant as well as the wild-type gene expressed in tobacco cells. Lectin (carbohydrate-binding) activity was completely abolished in the mutant protein produced in the tobacco cells. The leucoagglutinating and mitogenic activities characteristic of PHA-L were also eliminated by this mutation, confirming that. The assessment of cell proliferation demonstrated that WGA, Con A and PHA-L very significantly decreased proliferation in the 3 astrocytic cell lines in a dose-dependent manner. Astrocytic tumor cells in the confluent growth phase were less sensitive to the WGA, Con A and PHA-L lectin-induced effects than cells in the log growth phase PHA-L is itself a lectin, one of the many legume lectins. This particular one causes severe allergy by switching on a runaway meitogenic event. It binds to the sugars on the proteins presented on. Phytohemagglutinin-L (PHA-L) isolated from the red kidney bean has a weight of approximately 120,000 . Leeks and taro are also foods with mannose binding lectin (MBL) and those are often high molecular weights. In humans, 600,000 daltons is what one particular lectin specific to mannose and N-acetylglucosamine residue tested out at
Alterations of the N-linked carbohydrate core structure of cell surface glycoproteins (β1-6 branching) can be detected by phytohemagglutinin (PHA-L) lectin binding and has been linked to tumor progression and K-ras activation in colon cancer Description. Lectin phytohemagglutinin-L (PHA-L) is strongly inhibited by N-acetylglucosamine β(1-2) mannopyranosyl residues.[ALTREF PN29369] This lectin has been shown to agglutinate leukocytes and induce mitogenic activity in T-lymphocytes[ALTREF PN29369,PN29368] and has also been used as an anterograde tracer for the study of neuronal pathways.[ALTREF PN20284
PHA-L reacts strongly with certain carcinoma cell lines of high metastatic potential 15,16 . PHA-L has also been proposed as a potential therapeutic agent. The lectin has been used in preliminary studies indicating that it is a good biological response modifier 17 . This lectin shows the potential to inhibit graft vs. host reaction in. We are in the process of testing an in house prepared PHA-L lectin affinity column. It was found out that IgG and alpha acid glycoprotein have some affinity towards it
glutinin-L (PHA-L), a glycosylated lectin from the seeds of the common bean (Phaseolus vul- garis). Single PHA-L crystals were grown by vapor diffusion, using PEG as precipitant. The protein crystallizes in the monoclinic space group C2, and diffracts to a resolution of 2.7 A. The unit cell parameters are a=106.3 A Phaseolus vulgaris lectin L (PHA-L) is composed of four units each of molecular weight of 31 kDa. The protein has a molecular weight of 126 kDa. It is isolated from red kidney beans by affinity chromatography. Also known as Leucoagglutinin (PHA-L), this lectin has high mitogenic and leucoagglutinating activity, but low erythroagglutinating. Translational Relevance. This is the first study investigating the prognostic effect of β(1,6)-branched oligosaccharides recognized by their specific lectin Phaseolus vulgaris leukoagglutinin (PHA-L) binding in human prostate cancer. The potential relevance of these glycan structures was identified in newly established spontaneous metastasis xenograft models of prostate cancer indicating PHA. Seed phytic acid reduces mineral bioavailability by chelating minerals. Consumption of common bean seeds with the low phytic acid 1 (lpa1) mutation improved iron status in human trials but caused adverse gastrointestinal effects, presumably due to increased stability of lectin phytohemagglutinin L (PHA-L) compared to the wild type (wt).A hard-to-cook (HTC) defect observed in lpa1 seeds. Lectin, PHA-L, Phaseolus vulgaris - (Lectin, PHA-L, Phaseolus vulgaris) SDS Safety Data Sheet for Lectin, PHA-L, Phaseolus vulgaris 431784 Material Safety Data Sheet or SDS for Lectin, PHA-L, Phaseolus vulgaris 431784 from Merck for download or viewing in the browser
Alterations of the N-linked carbohydrate core structure of cell surface glycoproteins (beta 1-6 branching) can be detected by phytohemagglutinin (PHA-L) lectin binding and has been linked to tumor progression and K-ras activation in colon cancer Phaseolus vulgaris agglutinin PHA L is the name ascribed to a family of lectins each of which consists of four subunits There are two different types of subunits One appears to be involved primarily in red cell agglutination and has been designated the E subunit for erythroagglutinin The other type is involved in lymphocyte agglutination and. PHA-L Lectins. Antibodies, Recombinant proteins, ELISA kits, RNAi, cDNA clones, Antibody Array, Luminex kits. Reagents and instruments for immunology, cell biology and molecular biology Lectins were classified into five groups according to the binding specificity and inhibitory sugars, including N-acetylglucosamine, mannose, galactose/N-acetylgalactosamine, complex type N-glycan groups (PHA-E and PHA-L), and fucose (Table 1) as discussed previously [5, 7]
The structure of phytohemagglutinin-L (PHA-L), a leucoagglutinating seed lectin from Phaseolus vulgaris, has been solved with molecular replacement using the coordinates of lentil lectin as model, and refined at a resolution of 2.8 Å. The final R-factor of the structure is 20.0%. The quaternary structure of the PHA-L tetramer differs from the structures of the concanavalin A and peanut lectin. Phaseolus vulgaris lectin (PHA E+L, also known as PHA P, P standing for phytohemagglutinin) is isolated from red kidney beans. It consists of two isolectins PHA-E and PHA-L, erythroagglutinin and leucoagglutinin, of which both possess strong mitogenic activity Lectins were prepared in lectin staining buffer (PBS containing 1% FBS, 1 mmol/L CaCl2 , and 2 mmol/L MgCl2 ) and resuspended in FACS buffer (PBS containing 2% fetal calf serum and 0.01% NaN3 , all from Sigma-Aldrich) before analysis using a FACS Canto II (BD Biosciences, Oxford, UK).. For analysis of the assays involving lymphocytes from the. The olfactory and respiratory mucosae of the Corriedale sheep were examined using lectin histochemistry in order to clarify the histochemical and glycohistochemical differences between these two tissues. The olfactory epithelium was stained with 13 lectins out of 21 lectins examined, while the respiratory epithelium was positive to 16 lectins
Libor Grubhoffer, University of South Bohemia, Parasitology Department, Faculty Member. Studies Environmental Research, Plant Pathology, and Plant breeding and genetics Vanderbilt, Vector Laboratories, Virogen, Viva Bioscience, vwr, WSU Monoclonal Antibody Center, Xona Microfluidics, ZEDIRA GmbH, ZeptoMetrix Corporation, ZYAG.. Lectin phytohemagglutinin-L (PHA-L) is strongly inhibited by N-acetylglucosamine β(1-2) mannopyranosyl residues.[ALTREF PN29369] This lectin has been shown to agglutinat
Biotin is a small molecule involved in a wide range of metabolic processes. This ligand forms a complex with Avidin and Streptavidin, resulting in the strongest non-covalent protein-ligand interaction known. Biotinylated Phaseolus vulgaris Lectin (PHA-L) has an appropriate amount of biotin bound to provide optimum detection characteristics when using an Avidin-HRP or Streptavidin-HRP conjugate. Phaseolus vulgaris Gel -PHA-L- Immobilized Lectin, 2mL Kit $ 391.00. Add to Wishlist. Quick View. Rabbit Anti-Lectins Unconjugated Rabbit Anti-PHA-E Antibody, 2mL $ 140.80. Add to Wishlist. Quick View. Colloidal Gold Colloidal Gold Conjugated Phaseolus vulgaris Lectin (Red Kidney Bean) -PHA-L-, 1mL 20nm $ 191.75 Since Con A and PHA-L are the two most widely used lectins for probing glycoprotein N-glycan branching levels, we compared the abilities of PHA-L and Con A to differentiate the branched glycoproteoforms from the collective pools at the intact glycoprotein level (Fig. 5A and B). PHA-L effectively separates highly branched and larger mass. PHA-L lectin and carbohydrate relationship: Conjugation with CdSe/CdS nanoparticles, radiolabeling and in vitro affinities on MCF-7 cells January 2014 Journal of Radioanalytical and Nuclear.
lectins, PHA-L and Concanavalin A (Con A)21,22 for aﬃnity puri cation and MS analysis. We uncover multi-fucosylation on Hp and show how this attenuates binding to PHA-L. Moreover, we demonstrate how this lectin aﬃnity puri cation-MS approach has the potential to become a generic method, capable of characterizing the inherent. Abstract. The plant lectin Phaseolus vulgaris leukoagglutinin (PHA-L) has unique properties that have made it particularly useful for tracing the axonal projections of neurons (Gerfen and Sawchenko, 1984, 1985). When PHA-L is injected by iontophoresis into the brain and subsequently localized by standard im-munohistochemical techniques, neurons at the injection site are labeled in their. using multi-lectin anity chromatography and quantitative mass spectrometry-based proteomics. Specic lectins (AAL, PHA-L and PHA-E) were used to target and chromatographically separate core-fucosylated and highly-branched protein glycoforms for analysis, as dierential expression of these glycan types have been previously associated with PCa Interestingly SBA only stimulated TLR4, ConA, TLR2/6 and PHA-L, TLR2/6, 4 and 5. As each lectin family exhibits different sugar ligand specificity for interaction, these results suggest that the pharmacology of this TLR agonism is encoded by the lectin's carbohydrate recognition motifs and the appropriate surface presentation of these motifs on.
Agarose-bound AAL and PHA-L/E lectins were purchased from Vector Laboratories (Burlingame, CA) and gravity packed in house, as previously described 25. All chromatography was performed on an. The Phaseolus vulgaris leukoagglutinating lectin (PHA-L) binds to β 1,6 branches of tri- and tetra-antennary oligosaccharides. We have applied digoxigenin- and biotin-conjugated PHA-L to establish a non-radioactive detection system for β 1,6 branches, which can be used in lectin blotting as well as light and electron microscopic cytochemistry Five superficial two or three layers that occurs in late diestrus and proes- iectins (CSA, HAA, PHA-L, PWM, VVA) reacted with all the cell trus is a unique feature of the rodent estrous cycle, and although layers except the surface layer, whereas one lectin (UEA-I) reacted the significance of this event remains unknown its occurrence im- only.
Absolute Lectins, perfect for Glycoscience. Medicago is a primary manufacturer of a wide variety of exceptionally pure lectins purified by affinity chromatography. Lectins are non-enzymatic proteins of non-immunoglobulin origin that bind specifically and reversibly to carbohydrate moieties without altering the covalent structure of the glycosyl. Notably, signals for PHA-L, a representative lectin binding to tetraantennary N-glycans, are similar for the WT and β3GnT2-KO mice. These results were confirmed by flow cytometry using LEL and PHA-L as probes (Figure 4C) . The ability of this lectin to fill entire neurons and remain in place over long periods suggested it might be an ideal marker for donor cells to be grafted into hosts for long survival periods About Phytohaemagglutinin (PHA) Phytohaemagglutinin (PHA) is a lectin found in red kidney bean that consists of two closely related proteins called PHA-L and PHA-E. The letters L and E indicate these proteins agglutinate leukocytes or erythrocytes. For immunoassays, PHA-L is well suited for functional analysis of T cells because PHA-L binds and crosslinks components of the T cell receptor to. PHA-L consists of two family of four different polypeptides encoded by four tightly linked genes, generally referred to as the phytohemagglutinin Downloaded from www.jbc.org by guest, on February 19, 2013 canonical legume lectin dimers that pack together through the formation of a close contact between two family of bean proteins
. It is a plant lectin also found in white kidney beans, green beans and other beans. The PHA is made up of the two protein units one is PHA-L and PHA-E RESULTS Binding patterns of all lectins except SNA-I, Con A and DBA changed during the adenoma-carcinoma sequence. CONCLUSION The results indicate that lectins specific for mannose, N-acetylgalactosamine, N-acetylglucosamine, sialic acid, β-1,6-branched oligosaccharides and α-1-fucose may be associated with malignant progression
FITC. Size. 1 set. Handling Advice. Upon arrival store at -20 °C. Centrifuge the vial before opening at 1,000 x g for 1 minute. (To dislodge any material that may be dispersed on the wall or cap of the vial). Reconstitute the lyophilized material with appropriate buffer to the desired concentration and store the solutions at -20°C Phytohemagglutinin (PHA), the seed lectin of the common bean, Phaseolus vulgaris, is encoded by two highly homologous, tandemly linked genes, dlec1 and dlec2, which are coordinately expressed at high levels in developing cotyledons.Their respective transcripts translate into closely related polypeptides, PHA-E and PHA-L, constituents of the tetrameric lectin which accumulates at high levels in.
In a follow-up study, additional GalNAc-specific lectins (VVA, SBA, HPA) were shown to bind the rodent NMJ specifically while lectins with other glycan specificities (e.g., ConA, WGA, RCA, PHA-L) bound the sarcolemma indiscriminately, demonstrating that the rodent NMJ is uniquely modified with terminal GalNAc structures (Scott et al. 1988) Product Description. Unconjugated Rabbit Anti-PHA-L Antibody, 2mL. With the exception of Diagnostic Microbiology Products all biochemicals described are for research use only. The biochemical reagents are not designed for use in therapeutic or diagnostic applications. We are unable to ship to individuals In the seeds of a common bean (P. vulgaris), two lectin-like proteins, α-amylase inhibitor and arcelin, are present. 18,) Both proteins have insecticidal activity toward bean weevils, and their amino acid sequences are very similar (50-60% identity) to that of PHA-L, a lectin occurring in the same seed Then Aleuria aurantia lectin (AAL) ELISA was performed according to ELISA index to test the protein fucosylation level of NRG1 (Fuc-NRG1). Results: We got glycan profiles of 14 lectins, including GNL, GSL2, AAL, BPL, ECL, CAL, NML, HHL, PHA-L, RCA-I, ConA, DBA, PWA and LEL. Six of them, namely, GSL2, BPL, NML, HHL, PHA-L and LEL, had. Legume lectin allergens like the lectins from peanut (Ara h agglutinin/PNA), kidney bean (PHA-E, PHA-L), soybean (SBA), horse gram (DbA), lentil (LcA), and pea (PsA), occur as seed storage proteins sequestered in protein bodies, together with the major cupin allergens, 7S globulins/vicilins and 11S globulins/legumins, and 2S albumin allergens
The anterograde axonal tracing technique utilizing the plant lectin, Phaseolus vulgaris-leucoagglutin (PHA-L) was developed in 1983 (Gerfen and Sawchenko, 1984), and has been used in over 1000 published studies.The technique involves iontophoretic injection of the plant lectin PHA-L into the brain and, following a 1-3 week survival period, the tracer is visualized using standard. Lectins. Lectins Showing 1-16 of 1224 results. Add to cart Added to cart! Agaricus bisporus (Mushroom) Lectin (ABA/ABL) - Separopore 4B. Login to see prices Add to Compare Add to Wishlist. Add to cart Added to cart! Agaricus bisporus (Mushroom) Lectin (ABA/ABL) - Separopore 4B. Login to see prices Add to Compare Add to Wishlist. Add to. Article Snippet: The lectin fluorescein labeled Phaseolus Vulgaris Leucoagglutinin (PHA-L) (1:200; Vector Laboratories) was used to stain for PHA-L. For O4 staining, the cells were first incubated in primary antibody mouse-anti-O4 antibody (Clone 81; 1:100; EMD millipore ), followed by secondary antibody incubation, anti-Mouse IgM Alexa Fluor.