Arachis hypogaea Lectin (PNA) - Biotinylated

Arachis hypogaea (Peanut) Lectin - Biotinylated

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.

Biotinylated peanut agglutinin has an appropriate number of biotins bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated biotins and is preserved with sodium sodium azide. The biotinylated lectin is an ideal intermediate for examining glycoconjugates using the Biotin-Avidin/Streptavidin System.

Technical Specifications:

Ligand Source: Arachis hypogaea

Molecular Weight: 110 kDa

Carbohydrate Specificity: GalBeta1,3GalNAc

Inhibiting/Eluting Sugar: Galactose

Carbohydrate for Elution: 0.2M Galactose

Blood Group Specificity: T antigen (M, N)

Conjugate: Biotinylated

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.

DOCUMENTATION: MSDS -

http://www.bio-world.com/site/accounts/masterfiles/MSDS/MS-21510000.pdf

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

REFERENCES:

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• Magnetic bead-based fluorometric detection of lectin-glycoprotein interactions. Talanta. (2010) 81: 1676-80.
• Distribution of lectin-bindings in the testis of the lesser mouse deer, Tragulus javanicus. Anat Histol Embryol. (2009) 38: 208-13.
• Branchial expression and localization of SLC9A2 and SLC9A3 sodium/hydrogen exchangers and their possible role in acid-base regulation in freshwater rainbow trout (Oncorhynchus mykiss). J Exp Biol. (2008) 211: 2467-77.
• Post-translational modifications in glycosylation status during epididymal passage and significance in fertility of a 33 kDa glycoprotein (MEF3) of rhesus monkey (Macaca mulatta). Reproduction. (2008) 135: 761-70.
• A lectin histochemical study on the testis of the babirusa, Babyroussa babyrussa (Suidae). Anat Histol Embryol. (2007) 36: 343-8.
• Lectin binding pattern in meningiomas of various histological subtypes. Folia Neuropathol. (2007) 45: 9-18.
• Differential binding to glycotopes among the layers of three mammalian retinal neurons by man-containing N-linked glycan, T(alpha) (Galbeta1-3GalNAcalpha1-), Tn(GalNAcalpha1-Ser/Thr) and I (beta)/II (beta) (Galbeta1-3/4GlcNAcbeta-) reactive lectins. Neurochem Res. (2006) 31: 619-28.
• Aberrantly glycosylated serum IgA1 are closely associated with pathologic phenotypes of IgA nephropathy. Kidney Int. (2005) 68: 167-72.
• Age-related alterations in the carbohydrate residue composition of the cell surface in the unexposed normal human epidermis. Gerontology. (2005) 51: 155-60.
• Qualitative and quantitative alterations of cell surface carbohydrate residues during epidermal morphogenesis. Anat Embryol (Berl). (2005) 209: 207-15.
• BETA2/NeuroD1 null mice: a new model for transcription factor-dependent photoreceptor degeneration. J Neurosci. (2003) 23: 453-61.
• Cone photoreceptor recovery after experimental detachment and reattachment: an immunocytochemical, morphological, and electrophysiological study. Invest Ophthalmol Vis Sci. (2003) 44: 416-25.
• A histochemical study of inflammatory lesions of the maxillary sinus mucosa using biotinylated lectins. J Oral Sci. (2000) 42: 87-91.
• Müller cell outgrowth after retinal detachment: association with cone photoreceptors. Invest Ophthalmol Vis Sci. (2000) 41: 1542-5.
• Analysis of zona pellucida modifications due to cortical granule exocytosis in single porcine oocytes, using enhanced chemiluminescence. Theriogenology. (1999) 52: 629-40.
• Lectin binding studies of parotid salivary glycoproteins in Sjögren's syndrome. Electrophoresis. (1999) 20: 2124-32.
• Lectin binding patterns in nonsensory regions of rat cochlea during postnatal development. J Anat. (1999) 194: 497-504.
• Characterization of a stage-specific Mr16000 schistosomular surface glycoprotein antigen of Schistosoma mansoni. Mol Biochem Parasitol. (1999) 100: 85-94.
• All pyruvylated galactose in Schizosaccharomyces pombe N-glycans is present in the terminal disaccharide, 4,6-O-[(R)-(1-carboxyethylidine)]-Galbeta1,3Galalpha1-. Glycobiology. (1998) 8: 1087-95.
• Lectin cytochemical analysis of lacrimal pleomorphic adenomas. Jpn J Ophthalmol. (1998) 42: 249-55.
• Histochemical study of the epithelia of nasal polyps by biotinylated lectins and neoglycoprotein. A comparison with the normal human respiratory epithelium. Eur J Morphol. (1997) 35: 79-86.
• Fluorometric assessments of acrosomal integrity and viability in cryopreserved bovine spermatozoa. Biol Reprod. (1997) 56: 991-8.
• O-glycosylation of fibrinogen from different mammalian species as revealed by the binding of Escherichia coli biotinylated lectins. Thromb Haemost. (1996) 76: 710-4.
• Lectin-histochemical study of O-linked glycoconjugates in dysplastic retina of Norrie disease. Jpn J Ophthalmol. (1996) 40: 251-4.
• Galactose-containing glycoconjugates of the iris, the aqueous outflow passages and the cornea in capsular glaucoma. A lectin histochemical study. Graefes Arch Clin Exp Ophthalmol. (1995) 233: 192-9.
• Bauhinia purpurea (BPA) binding to normal and neoplastic thyroid glands. Pathol Res Pract. (1994) 190: 1005-11.
• Distribution of carbohydrates in the zona pellucida of human oocytes. J Reprod Fertil. (1994) 102: 81-6.
• Lectin-binding profiles in MNNG-induced shrew esophageal carcinomas. Anticancer Res. (1994) 14: 1569-72.
• Variations in the distribution of sugar residues in the zona pellucida as possible species-specific determinants of mammalian oocytes. J Reprod Fertil. (1994) 100: 35-41.
• Interaction of coagulase negative staphylococci with lectins. J Clin Pathol. (1993) 46: 761-3.
• Silver-enhanced colloidal-gold labelling of rabbit kidney collecting-duct cell surfaces imaged by scanning electron microscopy. J Microsc. (1993) 171: 107-15.
• Demonstration of feline and canine platelet glycoproteins by immuno- and lectin histochemistry. Histochemistry. (1993) 100: 83-91.
• Ultrastructural distribution of lectin-binding sites on gastric superficial mucus-secreting epithelial cells. The role of Golgi apparatus in the initial glycosylation. Histochemistry. (1993) 99: 181-9.
• Lectin-binding profiles for normal skin appendages and their tumors. J Cutan Pathol. (1992) 19: 483-9.
• Lectin binding sites as markers of neonatal porcine uterine development. J Histochem Cytochem. (1992) 40: 1937-42.
• Method for the detection of glycopeptides at the picomole level in HPLC peptide maps. Anal Biochem. (1992) 207: 100-5.
• Peanut agglutinin (lectin from Arachis hypogaea) binding to hemopoietic cells: an immunophenotypic study using a biotin streptavidin technique. Pathology. (1992) 24: 173-6.
• Identification of lectin binding proteins in human tears. Invest Ophthalmol Vis Sci. (1991) 32: 3277-84.
• Lectin binding of endometrium in women with unexplained infertility. Fertil Steril. (1991) 56: 660-7.
• Lectin binding in skeletal muscle. Evaluation of alkaline phosphatase conjugated avidin staining procedures. Histochem J. (1991) 23: 345-54.
• Glycoprotein changes in the rat sperm plasma membrane during maturation in the epididymis. Mol Reprod Dev. (1991) 29: 357-64.
• Lectin binding sites in developing mouse limb buds. Anat Embryol (Berl). (1991) 184: 479-88.
• Immunohistochemical identification of tubular segments in percutaneous renal biopsies. Histochemistry. (1991) 95: 351-6.