Peanut agglutinin  (Synonyms: PNA)

Peanut agglutinin (PNA) is a carbohydrate-recognition protein that binds competitively and irreversibly to cell-surface β-D-Gal (1-3)-GalNAc, and this binding can be inhibited by D-galactose and asialofetuin. Peanut agglutinin recognizes exposed glycoepitopes and reflects the glycosylation status of cells. Peanut agglutinin can label glycoconjugates at neuromuscular junctions to safely visualize synaptic structures. Peanut agglutinin can be used to synthesize dyes to distinguish between normal and tumor tissues. Peanut agglutinin provides support for research on leukemia, Burkitt's tumors, and cutaneous squamous lesions^[1][2][3].

Peanut agglutinin (PNA) (500 μg/mL; 15 min) binds to 60-80% of normal human thymocytes, less than 2% of untreated normal human peripheral blood lymphocytes (100% after neuraminidase treatment), most acute leukemia and Burkitt tumor blasts, and rarely binds to chronic lymphatic leukemia cells^[1].
Peanut agglutinin (2 mg/mL; 15 min) agglutinates the PNA-positive subpopulation of normal human thymocytes, enabling separation from the minor PNA-negative subpopulation with high cell viability^[1].
Peanut agglutinin separates normal human thymocytes into subpopulations where the PNA-positive subpopulation shows poor mitogenic response to PHA and mixed lymphocyte culture, indicating functional immaturity, while the PNA-negative subpopulation responds robustly like mature peripheral blood T cells^[1].
Peanut agglutinin (5-125 μg/mL; 60 min) binds to 1.5 × 10⁵ sites per immature normal human thymocyte and 2.5 × 10⁴ sites per mature normal human thymocyte, with immature cells showing 6-fold more binding sites^[1].
Peanut agglutinin conjugated with horseradish peroxidase (100 μg/mL; 1 h) binds specifically to carbohydrates in the extracellular matrix capping Schwann cells at frog cutaneous pectoris muscle neuromuscular junctions^[2].
Peanut agglutinin conjugated with tetramethylrhodamine isothiocyanate (50 μg/mL; 30 min) does not alter synaptic transmission parameters (resting potential, endplate potentials, miniature endplate potentials, quantal content) in frog cutaneous pectoris muscle neuromuscular junctions, and 10 min of halogen light illumination of stained junctions also has no effect on these parameters^[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

Peanut agglutinin conjugated with fluorescent probes (50 μg/mL; bath application) produces only faint staining of mouse diaphragm neuromuscular junction terminal boutons^[2].
Fluorescently conjugated peanut agglutinin (50 μg/mL; 30 min) intensely stains the extracellular matrix surrounding neuromuscular junction terminal boutons in garter snake (Thamnophis) costo-cutaneous muscle, while also staining myelinated axons and blood vessels in this tissue^[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

Solid

White to off-white

[Peanut agglutinin]

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• [1]. Reisner Y, et al. Interaction of peanut agglutinin with normal human lymphocytes and with leukemic cells. Proc Natl Acad Sci U S A. 1979;76(1):447-451.

  [2]. Ko CP, et al. A lectin, peanut agglutinin, as a probe for the extracellular matrix in living neuromuscular junctions. J Neurocytol. 1987;16(4):567-576.

  [3]. Kannon G, et al. Utility of peanut agglutinin (PNA) in the diagnosis of squamous cell carcinoma and keratoacanthoma. Am J Dermatopathol. 1990;12(1):31-36.