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10 mL

Ref. BWG-20120000-1
BIOWORLD

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Détails Produit

Applications:

Arachis hypogaea (Peanut Agglutinin, PNA) Separopore 4B-CL is used for the purification of O-linked glycoproteins.

Peanut agglutinin is a 110,000 molecular weight lectin composed of four identical subunits of approximately 27,000 daltons each. PNA binds preferentially to a commonly occurring structure, galactosyl (Beta-1,3) N-acetylgalactosamine. This carbohydrate sequence (called the “T-antigen”) is present in many glycoconjugates such as M and N blood groups, gangliosides, and many other soluble and membrane-associated glycoproteins and glycolipids. PNA is useful in distinguishing between normal and tumor tissues and in assessing malignancy in transitional mucosa. In addition, PNA binding has been employed as a measure of cellular maturity in lymphoid tissues, to distinguish a variety of lymphocyte human subpopulations and animals, and to measure the levels of lymphoid cell populations in many diseases. Presence of Ca++ can enhance PNA binding.

Technical Specifications:

  • Ligand source: Arachis hypogaea (peanut Lectin).
  • Matrix: Separopore 4B-CL (crosslinked agarose beads, 4%)
  • Particle size range: 52 - 165 µm
  • Matrix activation: Cyanogen bromide
  • Matrix attachment: Amino
  • Ligand density: 5 mg Peanut lectin/ml drained gel.
  • Binding Capacity: 0.5 - 1.5 mg of asialofetuin / ml of drained medium.
  • Inhibiting/Eluting Sugar: 200 mM galactose.
  • Carbohydrate for Elution: 0.1M lactose or 0.2M galactose in buffer. 10-50 mM N-acetylgalactosamine may also be used.
  • Blood Group Specificity: T-antigen
  • Form: 50:50 Liquid Suspension, PBS (1x) pH 7.4 w/ 0.01% Thimerosal
  • pH stability: 4 - 9
  • Storage: 2 - 8 C DO NOT FREEZE
  • Application note: Calcium is required for binding. Ca2+ concentration should not exceed 0.5 mM in the buffer (to not form a white precipitate).

References:

  • Lectin binding and effects in culture on human cancer and non-cancer cell lines: examination of issues of interest in drug design strategies. Acta Histochem. (2007) 109: 491-500.
  • The hydrophobic character of peanut (Arachis hypogaea) isoagglutinins. J Agric Food Chem. (2000) 48: 6267-70.
  • Expression, purification and characterization of peanut (Arachis hypogaea) agglutinin (PNA) from baculovirus infected insect cells. Biosci Rep. (1999) 19: 227-34.
  • Peanut lectin: a mitogen for normal human colonic epithelium and human HT29 colorectal cancer cells. J Natl Cancer Inst. (1992) 84: 1410-6.
  • Human urinary bladder carcinoma glycoconjugates expressing T-(Gal beta(1-3)GalNAc alpha 1-O-R) and T-like antigens: a comparative study using peanut agglutinin and poly- and monoclonal antibodies. Cancer Res. (1992) 52: 5030-6.
  • A phosphatidylinositol-linked peanut agglutinin-binding glycoprotein in central nervous system myelin and on oligodendrocytes. J Cell Biol. (1988) 106: 1273-9.
  • A simplified methodology for purification of peanut (Arachis hypogaea) agglutinin. J Biochem Biophys Methods. (1986) 13: 131-4.
  • Immunosorbent assay of interactions between human parotid immunoglobulin A and dietary lectins. Arch Oral Biol. (1986) 31: 477-81.
  • Detection of incompletely sialylated human chorionic gonadotropin by peanut agglutinin in choriocarcinoma. Jpn J Exp Med. (1985) 55: 75-8.
  • Purification of peanut (Arachis hypogaea) agglutinin isolectins by chromatofocusing. Anal Biochem. (1983) 131: 438-46.
  • Involvement of a tyrosyl residue in the interaction of peanut lectin with lactose. J Biochem. (1982) 91: 945-51.
  • Comparison of isolated peanut agglutinin receptor glycoproteins from human, bovine and porcine erythrocyte membranes. Biochim Biophys Acta. (1980) 603: 185-97.
  • Rapid purification of peanut agglutinin by sialic acid-less fetuin-sepharose column. J Immunol Methods. (1977) 17: 117-21.
  • The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea). J Biol Chem. (1975) 250: 8518-23.

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    Usage : bioWORLD's products are supplied for LABORATORY RESEARCH USE ONLY. The product may not be used as a drug, agricultural or pesticidal product , food additive or as a household chemical.