Plus de 50 ans d’expérience à votre service

Tel. : 01 45 33 67 17 / E-mail : coger@coger.fr

Stock épuisé.
En rupture de stock
Quantité minimum d'achat
La quantité minimum d'achat n'est pas atteinte

 

 

5 mg

Ref. BWG-21761000-2
BIOWORLD

photos non contractuelles

Prix sur demande. Demandez un devis : coger@coger.fr

Alerte réapprovisionnement
Recevez une alerte par email dès que votre choix sera de retour en stock
Votre e-mail*:

Détails Produit

Arachis hypogaea (Peanut) Lectin - FITC-Conjugated (SKU # 21761000)

SYNONYMS: Peanut Agglutinin; PNA; Galactose-binding Lectin

CATEGORY: Bioconjugates > Lectins

Uniprot ID: P02872

PRODUCT DESCRIPTION:

Lectins are proteins or glycoproteins of non-immune origin that agglutinate cells and/or precipitate complex carbohydrates. Lectins are capable of binding glycoproteins even in presence of various detergents.

Arachis hypogaea lectin or Peanut Agglutinin (PNA) is isolated from peanuts and purified by affinity chromatography. The lectin has a molecular weight of 110 kDa and consists of four identical subunits of approximately 27 kDa each. PNA does not agglutinate normal human erythrocytes, but strongly agglutinates neuraminidase treated erythrocytes. Lectin PNA is specific for terminal Beta-galactose and binds preferentially to a commonly occurring structure, galactosyl (Beta-1,3) N-acetylgalactosamine. PNA has potent anti-T activity similar to the anti-T antibody in human sera. PNA has been used in tumour tissue determination for transitional mucosa malignancies. The lectin also agglutinates neuraminidase-treated human erythrocytes at < 0.1 µg/ml after trypsin treatment of cells and its activity is inhibited by lactose and galactose. Though PNA does not require any divalent cations for activity, the presence of calcium ions in diluents can enhance the binding of PNA to receptors, possibly by neutralizing the negative charges on sialic acid residues adjacent to the receptor sequence.

PNA is useful in distinguishing between normal and tumor tissues and in assessing malignancy in transitional mucosa. In addition, PNA binding can be used to measure cellular maturity in lymphoid tissues, to distinguish a variety of lymphocyte subpopulations in man and experimental animals, and to measure the levels of lymphoid cell populations in many diseases. PNA can be employed in the fractionation of stem cells in mice for use in bone marrow transplantation across histocompatibility barriers.

Fluorescein labeled Peanut agglutinin has an appropriate number of fluorochromes bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated fluorochromes. FITC-conjugated PNA has an excitation at 495 nm and an emission at about 515 nm. Fluorescent Conjugates are extremely light sensitive.

Technical Specifications:

Ligand Source: Arachis hypogaea

Molecular Weight: 110 kDa

Carbohydrate Specificity: GalBeta1,3GalNAc (T-antigen)

Inhibiting/Eluting Sugar: Galactose

Carbohydrate for Elution: 0.2M Galactose

Blood Group Specificity: T antigen (M, N)

Conjugate: FITC

Form: Liquid

Isoelectric (pI): 5.5-6.5

Storage: -20 C

Application note: Calcium and Magnesium are required for binding.


APPLICATIONS

  • Biotynylated PNA can be used for the detection of relocalization of Tag antigen in large bowel carcinoma
  • Biotynylated PNA can be used to distinguish between human lymphocyte subsets.
  • Biotynylated PNA can be used as probe in histochemistry and immuno-histochemistry.
  • Biotynylated PNA can be used in human erythrocyte/lymphocyte studies.

UNIT DEFINITION: One unit will form 1mg purpurogallin in 20 sec from pyrogallol at pH 6.0 at 20 C

REFERENCES:

  • Stattic V, a STAT3 inhibitor, affects human spermatozoa through regulation of mitochondrial activity. J Cell Physiol. (2013) 228: 704-13.
  • Effect of sod (superoxide dismutase) protein supplementation in semen extenders on motility, viability, acrosome status and ERK (extracellular signal-regulated kinase) protein phosphorylation of chilled stallion spermatozoa. Theriogenology. (2011) 75: 1201-10.
  • A 32-kDa tyrosine-phosphorylated protein shows a protease-dependent increase in dead boar spermatozoa. J Reprod Dev. (2008) 54: 502-7.
  • Morphological and glycohistochemical studies on the epididymal region of the Sudani duck (Cairina moschata). Res Vet Sci. (2009) 86: 7-17.
  • Histochemical mapping of glycoconjugates in the testis of the one humped camel (Camelus dromedarius) during rutting and non-rutting seasons. Acta Histochem. (2008) 110: 124-33.
  • Differential lectin labelling of circulating hemocytes from Biomphalaria glabrata and Biomphalaria tenagophila resistant or susceptible to Schistosoma mansoni infection. Mem Inst Oswaldo Cruz. (2006) 101: 185-92.
  • Surface carbohydrates of Eudiplozoon nipponicum pre- and post-fusion. J Helminthol. (2004) 78: 63-8.
  • Functional changes and motility characteristics of Japanese Black bull spermatozoa separated by Percoll. Anim Reprod Sci. (2003) 77: 157-72.
  • A triple-stain flow cytometric method to assess plasma- and acrosome-membrane integrity of cryopreserved bovine sperm immediately after thawing in presence of egg-yolk particles. Biol Reprod. (2003) 68: 1828-35.
  • Ultrastructural localization of binding sites for PNA and VVA-B(4) lectins in human breast cancer cell lines detected by confocal fluorescence microscopy. Int J Oncol. (2002) 21: 1009-14.
  • Trypanosoma cruzi I and Trypanosoma cruzi II: recognition of sugar structures by Arachis hypogaea (peanut agglutinin) lectin. J Parasitol. (2002) 88: 582-6.
  • Telomere length measurement by fluorescence in situ hybridization and flow cytometry: tips and pitfalls. Cytometry. (2002) 47: 89-99.
  • Germinal center formation following immunization with the polysaccharide dextran B512 is substantially increased by cholera toxin. Int Immunol. (1998) 10: 851-9.
  • Lectin binding to extracellularly melanized microfilariae of Brugia malayi from the hemocoel of Anopheles quadrimaculatus. J Invertebr Pathol. (1995) 66: 277-86.
  • Evaluation of mouse sperm acrosomal status and viability by flow cytometry. Mol Reprod Dev. (1993) 36: 183-94.
  • Localization of glycosylated matrix proteins in secretory porcine enamel and their possible functional roles in enamel mineralization. Arch Oral Biol. (1992) 37: 953-62.
  • Distribution of glycoconjugates localized by peanut and Maclura pomifera agglutinins during mouse molar root development. Acta Anat (Basel). (1992) 145: 149-55.
  • Lectin-binding sites in testis of men with acrosomeless round-headed spermatozoa. Andrologia. (1989) 21: 271-4.
  • Characterization of stroma from Fuchs' endothelial dystrophy corneas. Cornea. (1989) 8: 90-7.
  • Changes in the lectin-binding pattern of PNA-agglutinin and UEA1 during the DMH-induced carcinogenesis in the normal appearing colonic mucosa of the rat. Eur J Clin Invest. (1988) 18: 196-201.
  • Detection of acrosome-reacted toad sperm based on specific lectin binding to the inner acrosomal membrane. Gamete Res. (1987) 18: 215-33.
  • Relationship between cell differentiation and binding of fluorescein isothiocyanate (FITC)-conjugated insulin of keratinocytes in culture. J Invest Dermatol. (1987) 89: 73-7.
  • Identification of glycoproteins expressing tumour-associated PNA-binding sites in colorectal carcinomas by SDS-GEL electrophoresis and PNA-labelling. Br J Cancer. (1987) 55: 361-5.
  • Detection of surface carbohydrates on Pneumocystis carinii by fluorescein-conjugated lectins. Parasitol Res. (1987) 74: 43-9.
  • Lectin binding to collagen strands in histologic tissue sections. Histochemistry. (1987) 87: 557-60.
  • Abnormal patterns of colorectal mucin secretion after urinary diversion of different types: histochemical and lectin binding studies. Hum Pathol. (1986) 17: 834-40.
  • Lectin-binding sites in eccrine sweat gland tumours. Br J Dermatol. (1986) 114: 451-8.
  • Lectin-binding sites in Paget's disease. Br J Dermatol. (1985) 113: 17-24.
  • Pregnancy-related changes in the human endometrium revealed by lectin histochemistry. Histochemistry. (1985) 82: 275-80.
  • Binding of four lectins to normal human oral mucosa. Scand J Dent Res. (1984) 92: 443-7.
  • Specific binding of peanut lectin to a class of retinal photoreceptor cells. A species comparison. Invest Ophthalmol Vis Sci. (1984) 25: 546-57.
  • Trypanosoma rhodesiense bloodstream trypomastigote and culture procyclic cell surface carbohydrates. J Protozool. (1983) 30: 662-8.
  • Studies on growth inhibition by lectins of Penicillia and Aspergilli. Arch Microbiol. (1978) 116: 119-21.