Looking for online definition of C-type lectin superfamily member 12 in the Medical Dictionary? C-type lectin superfamily member 12 explanation free. What is C-type lectin superfamily member 12? Meaning of C-type lectin superfamily member 12 medical term. What does C-type lectin superfamily member 12 mean?
Purified Native Ricinus Communis Agglutinin I Protein, Rhodamine labeled from Creative Biomart. Native Ricinus Communis Agglutinin I Protein, Rhodamine labeled can be used for research.
Recombinant Aleuria aurantia lectin is produced in E.coli and has an amino acid sequence identical to native Aleuria aurantia lectin. AAL is a dimeric lectin with two identical subunits of approximately 36 kDa. Each subunit has five carbohydrate-binding sites. The lectin recognizes and binds specifically to fucose and terminal fucose residues on complex oligo saccharides and glycoconjugates. rAAL has binding affinity for fucose in all binding positions (alpha1-2, alpha1-3, alpha1-4 and alpha1-6) and in contrast to AAL purified from natural sources, rAAL is not contaminated with free fucose yielding higher affinity towards fucosylated oligosaccharides than native AAL. Recombinant AAL hemagglutinates erythrocytes irrespective of blood type (A, B and 0) at the same titers as AAL isolated from natural sources. AAL has been widely used for analysis and preparation of oligosaccharides and glycoproteins. Diagnostic applications include analysis of disease-associated glycosylation on plasma proteins.
Purified Native Aleuria Aurantia Lectin Protein from Creative Biomart. Native Aleuria Aurantia Lectin Protein can be used for research.
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Secreted Ectodomain of Sialic Acid-Binding Ig-like Lectin-9 and Monocyte Chemoattractant Protein-1 Promote Recovery after Rat Spinal Cord Injury by Altering Macrophage PolaritySecreted Ectodomain of Sialic Acid-Binding Ig-like Lectin-9 and Monocyte Chemoattractant Protein-1 Promote Recovery after Rat Spinal Cord Injury by Altering Macrophage Polarity ...
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[button size=small text=MSDS & Datasheet link=/wp-content/uploads/media/BCDatasheets_C_10.26/BXXXX/B-2402-2.pdf]Anti-Tk Griffonia simplicifolia L
Nephrotoxicity is one of the most common kidney conditions. However, most conventional drugs are not adequate for treatment. This study was designed to evaluate the nephroprotective activity of 50% hydroethanolic leaf extract of Griffonia simplicifolia (DC.) Benth in drug-induced nephrotoxicity in Sprague-Dawley rats. Nephrotoxicity was induced in experimental animals by administering gentamicin and cisplatin after pretreatment with hydroethanolic extract of G. simplicifolia (GSE). GSE at 100 and 250 mg/kg were administered for 7 and 10 days by oral gavage in the gentamicin and cisplatin models, respectively. Silymarin (120 mg/kg) was given as the standard nephroprotective drug. Nephroprotective effect was studied by assaying the activity of kidney function biomarkers such as creatinine, urea, sodium, chloride, and potassium concentrations. The effect of the treatments on kidney antioxidant enzymes (SOD, MDA, GSH, GPx, GST and NO), inflammatory cytokines (IL 17, IL 23 and COX-2) and the ...
Griffonia simplicifolia is a coarse aggressive brier built-in to West Africa and Central Africa. It grows to about 3 m, and bears greenish flowers followed by atramentous pods. The seeds of the bulb are acclimated as an herbal supplement for their 5-hydroxytryptophan (5-HTP ) content. 5-Hydroxytryptophan is an important architecture block for the animal physique…
Find patient medical information for GRIFFONIA SIMPLICIFOLIA on WebMD including its uses, effectiveness, side effects and safety, interactions, user ratings and products that have it.
Sialic acid-binding Ig-like lectin-7 (Siglec-7) expression is strongly reduced on natural killer (NK) cells from HIV-1 infected viremic patients. To investigate the mechanism(s) underlying this phenomenon, we hypothesized that Siglec-7 could contribute to the infection of CD4pos target cells following its interaction with HIV-1 envelope (Env) glycoprotein 120 (gp120). The ability of Siglec-7 to bind gp120 Env in a sialic acid-dependent manner facilitates the infection of both T cells and monocyte-derived macrophages (MDMs). Indeed, pre-incubation of HIV-1 with soluble Siglec-7 (sSiglec-7) increases the infection rate of CD4pos T cells, which do not constitutively express Siglec-7. Conversely, selective blockade of Siglec-7 markedly reduces the degree of HIV-1 infection in Siglec-7pos MDMs. Finally, the sSiglec-7 amount is increased in the serum of AIDS patients with high levels of HIV-1 viremia and inversely correlates with CD4pos T cell counts. Our results show that Siglec-7 binds HIV-1 and contributes
A number of genes encoding C-type lectin molecules have been mapped to the natural killer gene complex (NKC) at the distal region of mouse chromosome 6 and to a syntenic region on human chromosome 12p12-p13. In addition to those receptors which regulate NK cell function, related structures expressed on other cells types have also been localized to this chromosomal region. Among these are a number of recently characterized genes, including macrophage C-type lectin (MCL), macrophage-inducible C-type lectin (Mincle), dendritic cell immunoreceptor (DCIR) and dendritic cell-associated lectin-2 (Dectin-2). The amino acid sequences comprising the single C-type lectin domains of MCL, Mincle, DCIR and Dectin-2 are shown here to be closely related to each other. These molecules show overall similarity to two groups of animal C-type lectins, groups II and V, which demonstrate type II transmembrane topology. In this study, sequence analysis suggests that MCL, Mincle, DCIR and Dectin-2 represent a subset of group II
Lectins, a well-known class of carbohydrate-binding proteins, are known to be important in a variety of biological processes, mediated through their carbohydrate specificities. Plant lectins are broadly divided into six classes based on their subunit folds. These are legume lectins (see ,PDOC00278,), jacalin-related lectins (JRLs), monocot mannose-binding lectins (see ,PDOC50927,), trefoil lectins, cyanovirin-N lectin, and hevein domain lectins. JRLs derive their name from jacalin, the first member to be identified from the seed of jackfruit. Based on the known sugar specificities, lectins in this family can be broadly divided into two classes: (1) the galactose-specific lectins and (2) the mannose/glucose-specific lectins [1,2,3,4,5]. The ~135-150 amino acid residue jacalin-type lectin domain adopts a β-prism-I fold comprised of three Greek keys (four stranded β-sheets) (see ,PDB:3APA,) [4]. Some proteins known to contain a jacalin-type lectin domain are listed below: ...
GSL II is affinity purified tetramer that contains a single type of 30 kDa subunit. It has insecticidal structure/function, the first GlcNAc binding legume lectin proven to have insecticidal activity.This lectin has a carbohydrate specificity for αGal and αGalNAc and elutes with galactose or N-acetylgalactosamine. Incr
TY - CHAP. T1 - Role of Cell Surface Carbohydrates in Development and Disease. AU - Fukuda, Michiko N.. AU - Akama, Tomoya O.. AU - Sugihara, Kazuhiro. PY - 2008. Y1 - 2008. N2 - This chapter discusses the roles of cell surface carbohydrates in development, while focusing on embryo implantation, spermatogenesis, and tissue maturation. The outer surface of mammalian cells is covered by glycoproteins and glycolipids. Substantial biochemical and immunochemical evidence suggests that cell surface carbohydrates play significant roles in development and health. Functional studies of cell surface carbohydrates still leave many questions unanswered. In the last decade, genetic approaches and sophisticated chemical analyses have enabled us to reveal the function of specific carbohydrate structures in vivo, and as a result the role of carbohydrates in development and disease is understood. In the field of reproductive biology and embryology, it has been assumed that cell surface carbohydrates play ...
Several lectins recognize n-acetyl-glucosamine in a glycoprotein. Based on the linkage and specificity for binding, different N-Acetyl-Glucosamine-binding lectins are utilized to obtain optimum results.
Lectins were defined as proteins that recognize specific carbohydrate structures and agglutinate cells by binding to cell surface glycoproteins and glycoconjugates. Many kinds of different lectins have been purified from fish eggs. Lectins may have a variety of biological function in fish eggs, such as block of polyspermy, regulation of carbohydrates metabolism, participation in the formation of fertilization envelope after binding with glycoproteins, antibacterial effect and opsonization of pathogens. Therefore, lectins are important components in oocytes and play important roles. Cortical granules were as a kind of secretory vesicles that unique to oocyte. They are synthesized and accumulated during oogenesis, translocated to the cell surface before fertilization and exocytosed after fertilization. Cortical granule contents have diverse components, such as proteases and lectins, and play important roles in egg fertilization and early embryogenesis.Gibel carp oocyte-specific lectin (GOL) had ...
Introduction: The aim of this study was to compare fucose and sialic acid residue expression on fibronectin and alpha(1)-acid glycoprotein in the. seminal plasma PF-6463922 solubility dmso of men suspected of infertility and suffering from leukocytospermia.. Subjects and methods: Seminal ejaculates were collected from 27 leukocytospermic and 18 healthy, normozoospermic men. The relative degree of fucosylation and sialylation of fibronectin and alpha(1)-acid glycoprotein was estimated by ELISA using fucose and sialic acid specific lectins from Aleuria aurantia, Lotus tetragonolobus, and Ulex europaeus as well as Maackia amurensis and Sambucus nigra, respectively.. Results: Leukocytospermic seminal fibronectin, in comparison with fibronectin of normal fertile group, showed lower relative reactivity with AAL, LTA and UEA, and higher reactivity with MAA and SNA, while the AGP of the leukocytospermic group was less reactive with AAL, and the relative reactivity. buy 5-Fluoracil with LTA and MAA was ...
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Do you suffer from symptoms after eating? Such as digestive symptoms, foggy brain, sinus congestion or aches and pains. Do you notice it after gluten containing foods or just cant track whats causing it? Chances are youre body is reacting to components in plants called lectins.. What are lectins? So happy you asked!. Lectins are the plants natural compounds to ward off pests, fungal and bacterial attack. That is, the plants natural immune system. When plants are under attack they raise their lectin numbers to fend off the attacking pests. This is the system by which pesticides work. However, pests are gaining tolerance resulting in needing an increase of pesticide to be applied to the plant and thus a further increase of the plants lectins.. Modern wheat strains vs old style grains. Our modern wheat strains have been modified to produce more lectins to be highly pest resistant. This very clever genetically engineering won Norman Borlaug a Nobel peace prize in 1970 and changed the industry ...
1 Cederberg BM, Gray GR. N-Acetyl-D-glucosamine binding lectins. A model system for the study of binding specificity. Anal Biochem. Oct 15, 1979; 99 (1): 221-30. DOI:10.1016/0003-2697(79)90067-8.. 2 Freed DLJ. Do dietary lectins cause disease? BMJ. Apr 17, 1999; 318 (7190): 1023-4. DOI: 10.1136/bmj.318.7190.1023.. 3 Houser J, Komarek J, Kostlanova N, et. al. A soluble fucose-specific lectin from Aspergillus fumigatus conidia-structure, specificity and possible role in fungal pathogenicity. PLoS One. Dec 10, 2013; 8 (12): e83077. DOI: 10.1371/journal.pone.0083077.. 4 Criado MT, Ferreiros CM. Selective interaction of a Fucus vesiculosus lectin-like mucopolysaccharide with several Candida species. Ann Microbiol (Paris). Mar-Apr 1983; 134A (2): 149-54. DOI: 10.1016/S0769-2609(83)80074-X.. 5 Hankins CN, Kindinger JI, Shannon LM. Legume Lectins: I. Immunological Cross-Reactions between the Enzymic Lectin from Mung Beans and other Well Characterized Legume Lectins. Plant Physiol. Jul 1979; 64 (1): ...
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Most plants contain lectins, some of which are toxic, inflammatory, or both. Many of these plant and dairy lectin are resistant to cooking and digestive enzymes. Grain lectins, for example, are quite resistant to human digestion but well suited for ruminants like cattle who have multi-chambered stomachs. Therefore, lectins are present in our food and are often resistant to our digestion and some have been scientifically shown to have significant GI toxicity in humans. Others have been shown to be beneficial and maybe even cancer protecting. Either way plant and animal proteins are foreign proteins to the body and are dealt with by digestion and our immune system in a positive or negative manner. The human digestive system was created to handle a variety of plant and animal proteins through the process of digestion and elimination. Some plant and animal proteins or lectins are severely toxic to humans and can not be eaten without causing death like those in Castor beans and some mushrooms. Other ...
First-generation immune checkpoint inhibitors, including anti-CTLA-4 and anti-programmed death 1 (anti-PD-1) antibodies, have led to major clinical progress, yet resistance frequently leads to treatment failure. Thus, new targets acting on T cells are needed. CD33-related sialic acid-binding immunoglobulin-like lectins (Siglecs) are pattern-recognition immune receptors binding to a range of sialoglycan ligands, which appear to function as self-associated molecular patterns (SAMPs) that suppress autoimmune responses. Siglecs are expressed at very low levels on normal T cells, and these receptors were not until recently considered as interesting targets on T cells for cancer immunotherapy. Here, we show an upregulation of Siglecs, including Siglec-9, on tumor-infiltrating T cells from non-small cell lung cancer (NSCLC), colorectal, and ovarian cancer patients. Siglec-9-expressing T cells coexpressed several inhibitory receptors, including PD-1. Targeting of the sialoglycan-SAMP/Siglec pa
PubMed journal article: Wheat germ lectin induces G2/M arrest in mouse L929 fibroblasts. Download Prime PubMed App to iPhone, iPad, or Android
Aberrant glycosylation occurs in essentially all types of human cancers. A difference in glycopattern of proteins will result in a change of function of the proteins. The lectin from Helix pomatia (HPA) recognizes N-acetylgalactosaminylated glycoproteins and very consistent results over the increased binding of HPA in tissue sections are associated with metastasis progression and poor patient prognosis in a range of human adenocarcinomas. The induced modification of protein function after changed glycosylation is unknown, and as a part in characterizing the glycoproteins carrying the specific carbohydrates, we analyzed the major HPA binding proteins in sera from healthy women, women with primary breast cancer with no metastasis (bcmet-), and women with metastasizing breast cancer (bcmet+) using lectin affinity chromatography and lectin blotting. The binding ligands were further identified using mass spectrometry (MALDI-TOF MS) to confirm the captured glycoproteins. The major HPA binding proteins ...
The legume lectins (or L-type lectins) are a family of sugar-binding proteins or lectins found in the seeds and, in smaller amounts, in the roots, stems, leaves and bark of plants belonging to the Fabaceae family. The exact function of the legume lectins in vivo is unknown but they are probably involved in the defense of plants against predators. Related proteins in other plant families and in animals have also been found. They have been used for decades as a model system for the study of protein-carbohydrate interactions, because they show an amazing variety of binding specificities and are easy to obtain and purify. Over the years, a quite impressive amount of structural data has been gathered. Well-studied members of this protein family include phytohemagglutinin and concanavalin A. The legume lectins use an ingenious framework for binding specific sugars. This framework consists of a conserved monosaccharide binding site in which four conserved residues from four separate regions in the ...
Though youve probably never heard of 5-HTP until recently, its actually been studied for more than 30 years. There have been several clinical trials that have proven just how well it helps with controlling hunger and losing weight. In this study, women who used this supplement before eating ate over 1,000 calories less than those who didnt. And in this study, women who took the supplement lost five times more weight over 12 weeks than those were taking a placebo.. If youre the type of person who always feels hungry and you have a hard time controlling your eating habits then 5-HTP may be just what you need to finally lose weight and keep your weight under control for the long run. ...
First-generation immune checkpoint inhibitors, including anti-CTLA-4 and anti-programmed death 1 (anti-PD-1) antibodies, have led to major clinical progress, yet resistance frequently leads to treatment failure. Thus, new targets acting on T cells are needed. CD33-related sialic acid-binding immunoglobulin-like lectins (Siglecs) are pattern-recognition immune receptors binding to a range of sialoglycan ligands, which appear to function as self-associated molecular patterns (SAMPs) that suppress autoimmune responses. Siglecs are expressed at very low levels on normal T cells, and these receptors were not until recently considered as interesting targets on T cells for cancer immunotherapy. Here, we show an upregulation of Siglecs, including Siglec-9, on tumor-infiltrating T cells from non-small cell lung cancer (NSCLC), colorectal, and ovarian cancer patients. Siglec-9-expressing T cells coexpressed several inhibitory receptors, including PD-1. Targeting of the sialoglycan-SAMP/Siglec pathway in ...
Further support came in reading the work of Dr. DAdamo and his Eating for Your Blood Type. ( http://www.dadamo.com/ ) This information dovetailed perfectly with what I had suspecting and confirming over the previous years of research.. So, I will be writing a paper on what I have learned about lectins as soon as possible. In the meantime, I would strongly recommend that the reader do a search for lectins and start reading on their own. You will be amazed at what researchers know about how and why these food-derived glycoproteins drive our tissues and immune systems crazy. You will also see how our own body produces lectins to control cell function. Then you will see how the confusion and dysfunction arise. Again, a good starting point in the link above, http://www.krispin.com/lectin.html.. One of the most fascinating aspects of this topic is the interrelationship between lectins and viruses. I go into this in my newest section, Viruses- Friend or Foe? This really starts to put things ...
Im new to Swami, before I tested as a Gatherer and black tea was a beneficial for me, now I am a Hunter and Black tea is an avoid for me, not even a black dot. I need more information on this. Is it the caffeine that is the problem in all black teas? (Because I know how to naturally de-caffeinate tea) Or is it the lectins in all Black teas that makes it an Avoid? I have so many different kinds of black teas that come from all over the world and are grown and made differently, so I am wondering about the lectins in black teas. Is there a difference in the lectins between the different kinds of black teas? I need more detailed information about Lectins ...
Corn/Maize contains Lectins which are basically part protein, part carbohydrate.. Lectins are the main problem with corn - the term is used to describe proteins which are part carbohydrate and part protein. Not all lectins are bad but those from corn/maize, wheat, rye, soy and dairy products are toxin lectins.. So lets take a closer look at these toxic lectins in corn/maize, soy, wheat, rye and dairy products.. Toxic Lectins are resistant to stomach acid and digestive enzymes. In other words - they cannot be broken down into a form suitable for digestion.. They may stick to the wall of the digestive tract of your dog and damage its lining, and then may pass through the wall of the digestive tract into general circulation. Toxic accumulation and elimination resulting in skin rashes, itching and excess shedding in dogs.. Lectins can cause alterations in digestive function that may be related to many digestive problems like colitis in dogs, Crohns Disease, Irritable Bowel Syndrome plus leaky gut ...
Lescar, J., R. Loris, E. Mitchell, C. Gautier, V. Chazalet, V. Cox, L. Wyns, S. Pérez, C. Breton, and A. Imberty, Isolectins I-A and I-B of Griffonia (Bandeiraea) simplicifolia. Crystal structure of metal-free GS I-B(4) and molecular basis for metal binding and monosaccharide specificity., J Biol Chem, vol. 277, issue 8, pp. 6608-14, 2002 Feb 22. ...
Clone REA509 recognizes the human CD302 antigen, a single-pass type I membrane protein, which is also known as C-type lectin domain family 13 member A (CLEC13A) or DCL-1. The C-type lectin superfamily is a large group of proteins which are characterized by the presence of one or more C-type lectin-like domains (CTLDs). The superfamily is divided into 17 groups based on their phylogeny and domain organisation. Despite the presence of a highly conserved domain, C-type lectins are functionally diverse and have been implicated in various processes including cell adhesion, tissue integration and remodelling, platelet activation, complement activation, pathogen recognition, endocytosis, and phagocytosis. CD302 was identified as a genetic fusion partner of human CD205 (DEC-205) in Hodgkins lymphoma cell lines and is classified as a group XV C-type lectin. The receptor consists of a single extracellular CTLD, a short spacer followed by a transmembrane region, and a cytoplasmic tail containing a putative
By Dr. Mercola While whole foods are healthy, there are certain caveats to consider even here. Lectins (not to be confused with the phospholipid lecithin) are carbohydrate-binding proteins that are widespread in the plant kingdom. An estimated 30 percent of fresh foods contain lectins.1 Even dairy contains lectins. Grass fed butter is an exception. Grass…
Sie sind hier: Glycopolymer Brushes for Specific Lectin Binding by Controlled Multivalent Presentation of N-acetyllactosamine Glycan Oligomers. ...
4R Health Products created by Dr Robert Siegel MD based on his 30 years of Aloe Vera research.He discovered special molecules in aloe vera gel that provide great benefits for supporting the immune system, to maintain and achieve optimal health.
Referred to: Immunology Department Camelia Botnar Laboratories Level 4 Great Ormond Street Hospital London WC1N 3JH General information Specimen transport: At room temperature Repeat frequency: At significant change of clinical...
Wheat germ agglutinin (WGA) contains a group of closely related isolectins, with an isoelectric point about pH 9. The receptor sugar for WGA is |em|N|/em|-acetylglucosamine, with preferential binding to dimers and trimers of this sugar.
Wheat germ agglutinin (WGA) is a plant protein that binds specifically to sugars expressed, among many others, by human gastrointestinal epithelialand immune cells. WGA is a toxic compound and an anti-nutritional factor, but recent works have shown that it may have potential as an anti-tumor drug and as a carrier for oral drugs. To quantitate the toxicity threshold for WGA on normal epithelial cells we previously investigated the effects of the lectin on differentiated Caco2 cells, and showed that in the micromolar range of concentrations WGA could alter the integrity of the epithelium layer and increase its permeability to both mannitol and dextran. WGA was shown to be uptaken by Caco2 cells and only approximately 0.1% molecules were observed to cross the epithelium layer by transcytosis. Here we show that at nanomolar concentrations WGA is unexpectedly bioactive onimmune cells. The supernatants of WGA-stimulated peripheral blood mononuclear cells (PBMC) can alter the integrity of the ...
Enhances brain serotonin 5-Hydroxytryptophan (5-HTP) is an intermediate in the natural synthesis of the essential amino acid, tryptophan, to serotonin. The enzyme tryptophan hydroxylase adds a hydroxyl group (OH) to tryptophan, forming the 5-HTP intermediate. In the body, it converts to serotonin with the removal of a carboxyl group (COOH) by a second enzyme. Serotonin is an important neurotransmitter involved in the regulation of endocrine and brain activity responsible for emotion, appetite and sleep/wake cycles. In clinical studies, administration of 5-HTP supported serotonin production. The 5-HTP supplied in this supplement is derived from the Griffonia simplicifolia plant. Supplementation with 5-HTP encourages brain serotonin levels that can lead to positive effects on emotional well-being, appetite control, and wake/sleep cycles. each vegetable capsule contains: 5-hydroxytryptophan (Griffonia simplicifolia) 100 mg. (hypo-allergenic plant fiber added to complete capsule
Title: A Sialic Acid-Specific Lectin from the Mushroom Paecilomyces Japonica that Exhibits Hemagglutination Activity and Cytotoxicity. VOLUME: 11 ISSUE: 6. Author(s):Jee Hun Park, Chang Soo Ryu, Ha Na Kim, Young Jun Na, Hyun Joo Park and HaHyung Kim. Affiliation:Physical Pharmacy Laboratory, College of Pharmacy, Chung-Ang University, 221 Huksuk-dong, Dongjakku, Seoul 156-756, Korea Correspondence To: HaHyung Kim.. Keywords:sialic acid, lectin, mushroom, paecilomyces japonica, hemagglutination, cytotoxicity. Abstract: The mushroom Paecilomyces japonica, grown on the silkworm larvae, has been used in Asia as a nutraceutical, tea, and Chinese medicine. In the present study, a sialic acid-specific lectin has been purified from the mushroom P. japonica using affinity chromatography on a fetuin-agarose column. Electrophoretical analyses indicated that this lectin, designated P. japon ica agglu tinin (PJA), is an acidic protein with a molecular mass of 16 kDa, and has no intermolecular disulfide bonds. ...
The motility and the chemotactic response towards plant roots of Radopholus similis, after treatment with novel types of lectins, were examined in vitro by analysing movement tracks on agar plates. Six plant lectins belonging to five different lectin families and a banana thaumatin-like protein (BanTLP) were included in the experiment. A 1% concentration of Phaseolus vulgaris agglutinin (PHA) had an adverse effect on the motility of R. similis females: 63% showed no or very little movement on agar plates compared to an average of 33% for other lectins and 3% for the control treatment. A 0.05% concentration of PHA still reduced the motility of R. similis females by 75%. Concanavalin A and wheat germ agglutinin did not alter the chemotactic response towards plant roots, despite binding of both lectins to R. similis. In contrast, Galanthus nivalis agglutinin (GNA) reduced orientated movement of R. similis towards plant roots. Subsequently, secretions of R. similis were stained with Coomassie Brilliant Blue
TY - JOUR. T1 - Differences in lectin binding patterns of normal human endometrium between proliferative and secretory phases. AU - Aoki, D.. AU - Kawakami, H.. AU - Nozawa, S.. AU - Udagawa, Y.. AU - Iizuka, R.. AU - Hirano, H.. PY - 1989/5/1. Y1 - 1989/5/1. N2 - Lectin binding patterns in normal human endometrium were examined by light and electron microscopy using seven different lectins (ConA, WGA, RCA, PNA, UEA-1, DBA, and SBA). For light microscopic observations, criteria based on the incidence and intensity of cells positive for the lectin staining were adopted to evaluate the different staining patterns of the proliferative and secretory endometria obtained by the avidin-biotin-peroxidase complex (ABC) technique. At the light microscopic level, ConA, WGA, and RCA stained endometrial glandular cells in both phases. The number of PNA-positive cells with the binding sites entirely limited to the apical surface tended to be reduced slightly in the secretory phase. UEA-1 weakly stained the ...
Dolichos biflorus|/em| agglutinin is a glycoprotein with a molecular weight of about 111 kDa and consists of 4 subunits of approximately equal size. This lectin has a carbohydrate specificity toward α-linked N-acetylgalactosamine.
A lectin was isolated from root tubers of winter aconite (Eranthis hyemalis) by affinity chromatography on fetuin-agarose, and it was partially characterized with respect to its biochemical, physicochemical and carbohydrate-binding properties. The Eranthis hyemalis lectin is a dimeric protein (Mr 62000) composed of two different subunits of Mr 30000 and 32000, held together by disulphide bonds. It is especially rich in asparagine/aspartic acid, glutamine/glutamic acid and leucine, and contains 5% covalently bound carbohydrate. Hapten inhibition assays indicated that the winter-aconite lectin is specific for N-acetylgalactosamine. In addition, the lectin exhibits a pronounced specificity towards blood-group-O erythrocytes. The winter-aconite lectin is the first lectin to be isolated from a species belonging to the plant family Ranunculaceae. It appears to be different from all previously described plant lectins.. ...
Looking for online definition of C-type lectin domain family 4, member J in the Medical Dictionary? C-type lectin domain family 4, member J explanation free. What is C-type lectin domain family 4, member J? Meaning of C-type lectin domain family 4, member J medical term. What does C-type lectin domain family 4, member J mean?
Mucins are high-molecular weight glycoproteins (0.25-20 MDa) containing one or more domains that are heavily O-glycosylated. Their implications as targets for cancer treatment have increased the interest in these glycoproteins, mainly in the fields of vaccines and antibodies. However, mucins present high heterogeneity, posing challenges that affect purification processes and quality control analysis. In that sense, it is necessary to develop and improve downstream processes and analytical methods to characterize these products. Here a tool based on biolayer interferometry analysis to improve mucins detection and quantification in a fast, simple and label free-way is presented. Taking advantage of lectin recognition of mucins carbohydrate structures, several lectins were evaluated and immobilized on streptavidin biosensors. Different assay conditions were optimized and the most suitable lectin, Aleuria aurantia lectin (AAL), was selected. Bovine Submaxillary Gland and human MUC5B mucins were ...
Background: Pneumococcal hemolytic uremic syndrome (P-HUS) is a rare but severe complication of invasive pneumococcal disease (IPD) in young children. Consensual biologic diagnosis criteria are currently lacking. Study design and methods: A prospective study was conducted on 10 children with culture-confirmed IPD. Five presented with full-blown P-HUS, three had an incomplete form with hemolytic anemia and mild or no uremia (P-HA), and two had neither HUS nor HA. Thomsen-Friedenreich (T), Th, and Tk cryptantigens and sialic acid expression were determined on red blood cells (RBCs) with peanut (PNA), Glycine soja (SBA), Bandeiraea simplicifolia II, and Maackia amurensis lectins. Plasma concentrations of the major endogenous T-antigen-binding protein, galectin-3 (Gal-3), were analyzed. Results: We found that RBCs strongly reacted with PNA and SBA lectins in all P-HUS and P-HA patients. Three P-HUS and three P-HA patients showed also concomitant Tk activation. Direct antiglobulin test (DAT) was
Progress in glycosciences has documented that biological information transfer not only exploits protein-protein and nucleic acid-protein interactions but also protein-carbohydrate recognition.1 Proteins involved in interaction with carbohydrates are known as lectins. Based on structural analysis of the carbohydrate recognition domains, animal lectins are currently classified into five categories: C type, I type, P type, galectins, and pentraxins.2 Cells as well as extracellular matrix molecules of normal and pathological corneas and conjunctivas in mammals are already known to contain glycans recognised by numerous plant lectins.3 4 The sugar receptors in these tissues have been demonstrated by employing labelled neoglycoligands.5 This experimental basis encourages us to further investigate expression of endogenous lectins on the eye surface. In this report, we focus on a member of the animal lectin family of the galectins. Mammalian galectins at present comprise nine proteins sharing the ...
TY - JOUR. T1 - The binding of fucose-containing glycoproteins by hepatic lectins. Re-examination of the clearance from blood and the binding to membrane receptors and pure lectins. AU - Lehrman, M. A.. AU - Pizzo, S. V.. AU - Imber, M. J.. AU - Hill, R. L.. PY - 1986. Y1 - 1986. N2 - The nature of the hepatic receptors that bind glycoproteins through fucose at the non-reducing termini of oligosaccharides in glycoproteins has been examined by three different approaches. First, the clearance from blood of intravenously injected glycoproteins was examined in mice with the aid of neoglycoproteins of bovine serum albumin (BSA). The clearance of fucosyl-BSA was rapid and was not strongly inhibited by glycoproteins that inhibit clearance mediated by the galactose or the mannose/N-acetylglucosamine receptors of liver. The clearance of Fucα1,3(Galβ1,4)GlcNAc-BSA (where Fuc is fucose) was inhibited weakly by either Fuc-BSA or Galβ1,4GlcNAc-BSA but strongly by a mixture of the two neoglycoproteins, ...
Definition of vicia villosa in the Definitions.net dictionary. Meaning of vicia villosa. What does vicia villosa mean? Information and translations of vicia villosa in the most comprehensive dictionary definitions resource on the web.
5 - HTP Natural Source 5- hydroxytryptophanNOW searches worldwide for high quality effective nutritional products that safely supply our customers needs. We supply a complete line of amino acids, vitamins, minerals, herb capsules, and herb extracts.Each Capsule Contains: 5-htp (5-hydroxytryptophan) 50mg (Griffonia simplicifolia seed)Other ingredients: White Rice Powder.Griffonia simplicifolia is an African Plant which is extracted to produce 5-HTP, the intermediate metabolite between the amino acid L-tryptophane and serotonin. Contains no yeast, wheat, corn, soy, milk, sugar, salt, colors or preservatives.Suggested Usage: As a dietary supplement, take 1 capsule daily, preferably at bedtime.Warning: If you are currently taking antidepressant medications please consult a physician prior to use. May cause drowsiness.
In order to test the use of lectins as a tool for the differentiation of harmful algal species, 13 species and 23 strains of algae were tested with 14 fluorescein isothiocyanate (FITC)-conjugated lectins, and the results examined using flow cytometry (FCM), epifluorescence microscopy (EFM) and spectrofluorometry (SFM). The lectin probes SBA, WGA, GSL I, DBA and PHA-E could distinguish between morphologically similar Gymnodinium-like species, such as Karenia mikimotoi (GMDH01), Takayama pulchellum (TPXM01) and Gymnodinium sp. (GspXM01), by their different binding activities. With the precise quantitative measurements of binding obtained using SFM and FCM, lectins appeared to be useful in distinguishing different strains of the same species. The results also showed that PHA-E could differentiate Alexandrium tamarense (ATDH04) from other strains of this species, and SJA could distinguish A. tamarense (ATMJ02) from other strains of this species (including ATMJ01). Similarly, PNA could identify A. ...
A variety of lectins were tested in vitro for inhibitory action against the activities of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase and the N-glycohydrolases (alpha-glucosidase, beta-glucosidase and beta-glucuronidase). Lectins from Phaseolus vulgaris, Momordica charantia, Ricinus communis and its constituent chains, and Agaricus bisporus were able to inhibit HIV-1 reverse transcriptase. P. vulgaris lectin and A. bisporus lectin were the most potent. The aforementioned lectins had only weak or no inhibitory effects on the glycohydrolases. The inhibitory effect of polysaccharopeptide from the mushroom Coriolus versicolor on HIV-1 reverse transcriptase and alpha-glucosidase was enhanced after chemical modification with chlorosulfonic acid. However, the inhibitory effect of the algal polysaccharide fucoidan on HIV-1 reverse transcriptase and alpha-glucosidase was not augmented by sulfation. Trypsin inhibitors from Phaseolus lunatus and Glycine max, gossypol and alkaloids from
Jacalin, isolated by affinity chromatography from jackfruit seeds, belongs to the family of galactose-binding lectins. Jacalin is a tetrameric two-chain lectin with a molecular weight of 66 kDa. Applications include isolating IgA from human serum, isolating human plasma glycoproteins and histochemistry. A post-translational proteolytic modification of Jacalin gives the lectin a novel carbohydrate-binding site involving the N terminus of the alpha-chain. The relative affinities of the lectin for galactose derivatives, as well as the structural basis of its T-antigen specificity, are explained by its protein structure. Artocarpus integrifolia lectin is supplied without preservatives as a lyophilized white to light-yellow powder, essentially salt-free. For laboratory use only.
A number of different families of proteins share a conserved domain which was first characterized in some animal lectins and which seem to function as a calcium-dependent carbohydrate-recognition domain [(PUBMED:3290208), (PUBMED:8341801)]. This domain, which is known as the C-type lectin domain (CTL) or as the carbohydrate-recognition domain (CRD), consists of about 110 to 130 residues. There are four cysteines which are perfectly conserved and involved in two disulfide bonds.. There are proteins with modules similar in overall structure to CRDs that serve functions other than sugar binding. Therefore, a more general term C-type lectin-like domain was introduced to refer to such domains, although both terms C-type lectin and C-type lectin-like are sometimes used interchangeably [(PUBMED:16336259)].. C-type lectins can be further divided into seven subgroups based on additional non-lectin domains and gene structure: (I) hyalectans, (II) asialoglycoprotein receptors, (III) collectins, (IV) ...
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Objective. To study the relationship between the human secreted protein stabilin-1-interacting chitinase-like protein (SI-CLP) and rheumatoid arthritis (RA).. Methods. The expression of SI-CLP in peripheral blood mononuclear cells (PBMCs) and synovial fluid from patients with RA and the effects of cytokines on SI-CLP expression were examined by Western blotting. Fluorescence-activated cell sorting analysis was performed to investigate the binding between SI-CLP and cells. Bone marrow-derived macrophages were isolated from wild-type and SI-CLP-/- mice, and real-time quantitative polymerase chain reaction was performed to detect the levels of messenger RNA for cytokines or SI-CLP in SI-CLP- or cytokine-treated macrophages. Histologic studies were conducted to evaluate inflamma-tion and the expression of interleukin-12 (IL-12), IL-13, and SI-CLP in lesions. Enzyme-linked immunosorbent assays were used to detect the cytokine levels in bone marrow-derived macrophages. Rats or mice with ...
The oligosaccharide chains of microheterogeneous bovine pancreatic DNAases were characterized by the lectin-nitrocellulose sheet method. The active fractions of the DNAases from column chromatography showed four major and several minor spots on a two-dimensional polyacrylamide gel. They were transferred on to nitrocellulose sheets and treated with glycosidases (neuraminidase, endo-beta-N-acetyl glucosaminidase H or F, or peptide N-glycosidase F) and treated with peroxidase-coupled lectins (concanavalin A, Ricinus communis agglutinin or wheat-germ agglutinin). From the results, the most probable oligosaccharide types were proposed to be as follows: the four major spots contained components which had high-mannose type or hybrid-type oligosaccharides, such as those susceptible to endo-beta-N-acetylglucosaminidase H. In addition, spot 1 contained a complex-type biantennary oligosaccharide without sialic acid and spot 3 contained a tri- or tetra-antennary complex-type oligosaccharide with sialic ...
The Anti-Siglec-H antibody reacts with the 34 kDa mouse sialic acid-binding immunoglobulin-like lectin (Siglec) H. Siglec-H is specifically expressed on mouse plasmacytoid dendritic cells1 - a subset of CD11c+ dendritic cells detected at low frequency in all lymphoid tissues, peripheral blood, and some non-lymphoid tissues. Binding of antibodies to Siglec-H inhibits type I interferon production, which can be induced in plasmacytoid dendritic cells by DNA and RNA viruses.2,3 | USA
CD33 (gp62 or siglec-3) is a glycosylated transmembrane protein that is a member of the sialic acid-binding immunoglobulin-like lectin (siglec) family. The genomic locus of this protein has been mapped to chromosome 19q13.1-3.5. The function of CD33 is not known, but it may have a role in cell-to-cell adhesion. In maturing granulocytic cells, there is progressive down-regulation of CD33 from the blast stage to mature neutrophils. However, in monocytes and macrophages/histiocytes, strong expression of CD33 is maintained throughout maturation ...
Magnetic nanoparticles represent a new paradigm for molecular targeting therapy in cancer. However, the transformative targeting potential of magnetic nanoparticles has been stymied by a key obstacle-safe delivery to specified target cells in vivo. As cancer cells grow under nutrient deprivation and hypoxic conditions and decorate cell surface with excessive sialoglycans, sialic acid binding lectins might be suitable for targeting cancer cells in vivo. Here we explore the potential of magnetic nanoparticles functionalized with wheat germ lectin (WGA) conjugate, so-called nanomagnetolectin, as apoptotic targetable agents for prostate cancer. In the presence of magnetic field (magnetofection) for 15min, 2.46nM nanomagnetolectin significantly promoted apoptosis (∼12-fold, p value ,0.01) of prostate cancer cells (LNCaP, PC-3, DU-145) compared to normal prostate epithelial cells (PrEC, PNT2, PZ-HPV-7), when supplemented with 10mM sialic acid under nutrient deprived condition. Nanomagnetolectin ...
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Abstract: Siglecs are a family of sialic acid-recognizing immunoglobulin-like lectins that exhibit multiple human-specific and human-universal differences, including changes in binding specificity (Siglec-5, -7, -9, -11, -12 and 14); changes in expression pattern (Siglec-1, -5, -6, and -11); gene conversion (SIGLEC11); gene deletion (SIGLEC13) and pseudogenization (SIGLEC17). Human-unique pseudogenes of SIGLEC12, SIGLEC14 and SIGLEC16 are also polymorphic within human populations, suggesting ongoing selection on this family of genes. The apparently higher concentration of SIGLEC changes in the human lineage may have been selected by interactions with pathogens binding Siglecs, and/or as compensatory responses to the loss of the sialic acid N-glycolylneuraminic acid (Neu5Gc) in humans. Human-specific Siglec changes of particular interest include expression of Siglec-11 in brain microglia, expression of Siglec-6 on placental trophoblast, suppression of Siglec-5 expression on adaptive immune cells, ...
Franziska Beran, Sujit Adhikary, Sankar Gayen, Christian Ulrichs, Arunava Goswami: Genetic Polymorphism of Dolichos biflorus L. in India at the Seed Storage Level
1. Blood type specific lectins. A lectin is a carbohydrate binding protein (http://en.wikipedia.org/wiki/Lectin). The most extreme example is ricin from the castor bean. Because a single lectin has multiple receptors it can bind to many cells that have the carbohydrate on its surface, effectively causing the cells to clump together. There are three types of human blood antigen, A, B, and H. The red blood cells start off with the H antigen. The gene at the ABO locus produces an enzyme to convert the H antigen, i.e. people with type A produce the enzyme to change the H antigen to the A antigen and similarly for type B. The gene for type O people is defective so they are left with the H antigen. Some lectins are specific for for these blood antigens and will agglutinate (clump together) red blood cells for that blood type. This was first discovered by Boyd, who discovered lima beans have a lectin specific for type A blood ...
According to Dr. Gundry, M.D., who wrote the book, The Plant Paradox about dietary lectins:. …our microbiomes are capable of eating lectins…Weve killed off most of our good bugs [that would eat up lectins] with broad-spectrum antibiotics…and artificial sweeteners…Just one packet of artificial sweetener kills 50 percent of the bacteria in our guts.. Lectins are controversial, but increased toxins in our environment, glyphosate in our foods, prescription medications and overuse of antibiotics, is definitely changing the shape of our microbiomes.. The ironic thing about lectins is that they are typically associated with foods that are nutrient-dense, so giving up lectin-containing foods means cutting out a large variety of healthy foods. For vegans and vegetarians, this would mean eliminating many foods that supply needed protein in a meatless diet.. Although lectins have been associated with a slew of negative side effects, you dont need to totally eliminate all lectin-rich foods ...
In the interpretation of glycan profiling patterns (i.e., glycan profiles) taken by lectin microarrays, I have summarized important things and procedures as follows.. 1. Some sort of normalization is absolutely necessary in comparing glycan profiles differentially. One of the most useful normalization methods is Average Normalization. In this case, all of the lectin signals are devided by the average of all lectins on the array, and for convenience, the values are then multiplied by 100. 2. And, the differences in glycan profiles are interpreted taking lectin binding characteristics and CV (coefficient of variation) into consideration. Usually the CV is less than 10% in a lot, and that of lot-to-lot variation gets a little bit bigger than this. Lectin binding specificity is not one-to-one relationship like an antigen-antibody reaction, but is fairly broader than that. So, we must be careful in the interpretation if other lectins with similar binding characteristics are reacting in the same way ...
The role of individual carbohydrate-binding sites in the function of the potent anti-HIV lectin Griffithsin. Jie Xue, Yongguang Gao, Bart Hoorelbeke, Ioannis Kagiampakis, Bo Zhao, Borries Demeler, Jan Balzarini, and Patricia J. LiWang Molecular Pharmaceutics 4, 2613-2625 (2012).. Griffithsin (GRFT) is a lectin that has been shown to inhibit HIV infection by binding to high mannose glycan structures on the surface of gp120, and is among the most potent HIV entry inhibitors reported so far. However, important biochemical details on the antiviral mechanism of GRFT action remain unexplored. In order to understand the role of the three individual carbohydrate-binding sites (CBS) in GRFT, mutations were made at each site (D30A, D70A, and D112A), and the resulting mutants were investigated. NMR studies revealed that each GRFT variant was folded but showed significant peak movement on the carbohydrate-binding face of the protein. The wild-type and each point mutant protein appeared as tight dimers with ...
The binding of the plant lectin soybean agglutinin (SBA) to primary sensory neurones has been investigated in the rat. SBA binding was found in Lissauers tract and in laminae I and IIo of the dorsal horn at cervical, thoracic and lumbar levels. Morphometric analysis of the S1 dorsal root ganglia revealed that SBA binding was associated with the small diameter cell population, considered to be the cell bodies of unmyelinated afferent fibres (C-fibres). These findings suggest that SBA may be a useful ultrastructural marker for C-fibre terminals ...
Regenerating islet-derived protein 3 alpha (or Regenerating islet-derived protein III-alpha) formerly known as HIP/PAP (Hepatocarcinoma-Intestine-Pancreas/Pancreatitis-Associated Protein) is a protein that in humans is encoded by the REG3A gene. This gene encodes a pancreatic secretory protein that may be involved in cell proliferation or differentiation. It has similarity to the C-type lectin superfamily. The enhanced expression of this gene is observed during pancreatic inflammation and liver carcinogenesis. Multiple alternatively spliced transcript variants encoding the same protein have been described for this gene but the full length nature of some transcripts is not yet known. Reg3A (UniProt Q0614 1) is a bactericidal C-type lectin that is constitutively produced in the intestine that has antibacterial properties against Gram-positive bacteria. Bacterial killing is mediated by binding to surface-exposed carbohydrate moieties of bacterial peptidoglycan. GRCh38: Ensembl release 89: ...
Domain combinations containing the Carbohydrate-binding domain superfamily in Proterospongia sp. ATCC 50818 . Domain architectures illustrate each occurrence of the Carbohydrate-binding domain superfamily.
S (2008) 333:353Many but not all ret-positive cells shed trkA expression postnataly and bind the lectin, Griffonia simplicifolia isolectin B4 Postnatally, neurons coexpressing ret and trkA, as analysed by double ISH, undergo trkA extinction, which appears to be full at P14 (Luo et al. 2007). This method is ret-dependent as it is slowed down in ret mutants. Conversely, ret expression is NGF-dependent as, in NGF/Bax (bcl-2 connected pro-apoptotic protein) double-mutants, only some ret-positive neurons are present at P0 and these are trkA-negative (Luo et al. 2007). In mature animals, the overlap of ret and trkA expression is limited and amounts to 5 five in mouse lumbar segment 5 (L5) DRG (Molliver et al. 1997; Orozco et al. 2001). In adult rat, 26 eight of trkA-positive cells in lumbar DRG express ret and 15 of ret-positive cells express trkA (Bennett et al. 1998; Kashiba et al. 1998, 2003). A total of 9 of DRG neurons express both. Roughly half of trkB- and trkCpositive cells express ret ...
Leukoagglutinin and hemagglutinin (MAL I+II) are seed lectins from Maackia amurensis, and are used as glycoanalytical tools to probe biological targets for ?2-3-linked sialic acids. These lectins have a molecular weight of 130,000 and an isoelectric point of pH 4.7. MAL I+II can be used to detect glycans containing ?2-
Sialic acid binding immunoglobulin-type lectin (Siglec) family are inhibitory receptors with diverse roles in the immune system. Siglec family contains 14 members in human and 9 in murine. Differentially expressed on various white blood cells. Here in this review we are focusing on CD22, also known as Sialic Acid-Binding Ig-Like Lectin 2 (Siglec-2). CD22 gene is located on 19q13.12 and is encoding a 140 kD type I transmembrane glycoprotein on the surface of B cells and is part of the immunoglobulin (Ig) superfamily and has been found only on B cells. CD22 has been shown to play a major role in establishing a baseline level of B-cell inhibition, and thus is a critical determinant of homeostasis in humoral immunity ...