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 β-galactose and binds preferentially to a commonly occurring structure, galactosyl (β-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.
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