Anti-Lysozyme/LYZ Antibody Picoband® Fluoro594 Conjugated

This gene encodes human lysozyme, whose natural substrate is the bacterial cell wall peptidoglycan (cleaving the beta[1-4]glycosidic linkages between N-acetylmuramic acid and N-acetylglucosamine) . Lysozyme is one of the antimicrobial agents found in human milk, and is also present in spleen, lung, kidney, white blood cells, plasma, saliva, and tears. The protein has antibacterial activity against a number of bacterial species. Missense mutations in this gene have been identified in heritable renal amyloidosis.

70 kDa ribosomal protein S6 kinase 1 antibody, KS6B1_HUMAN antibody, p70 alpha antibody, P70 beta 1 antibody, p70 ribosomal S6 kinase alpha antibody, p70 ribosomal S6 kinase beta 1 antibody, p70 S6 kinase alpha antibody, P70 S6 Kinase antibody, p70 S6 kinase alpha 1 antibody, p70 S6 kinase alpha 2 antibody, p70 S6K antibody, p70 S6K-alpha antibody, p70 S6KA antibody, p70 (S6K) alpha antibody, p70 (S6K) -alpha antibody, p70-alpha antibody, p70-S6K 1 antibody, p70-S6K antibody, P70S6K antibody, P70S6K1 antibody, p70S6Kb antibody, PS6K antibody, Ribosomal protein S6 kinase 70kDa polypeptide 1 antibody, Ribosomal protein S6 kinase beta 1 antibody, Ribosomal protein S6 kinase beta-1 antibody, Ribosomal protein S6 kinase I antibody, RPS6KB1 antibody, S6K antibody, S6K-beta-1 antibody, S6K1 antibody, Serine/threonine kinase 14 alpha antibody, Serine/threonine-protein kinase 14A antibody, STK14A antibody

E.coli-derived human IMP4 recombinant protein (Position: L2-K236) . Human IMP4 shares 97.9% amino acid (aa) sequence identity with both mouse and rat IMP4.

Downstream effector of TOR signaling pathway involved in osmotic stress response. Could be involved in the control of plant growth and development. Phosphorylates the ribosomal proteins P14, P16 and S6. Functions as a repressor of cell proliferation and required for maintenance of chromosome stability and ploidy levels through the RBR1-E2F pathway.

1. Camara, V. M., Harding, J. W., Prieur, D. J. Inherited lysozyme deficiency in rabbits: the absence of a primary isozyme of lysozyme as the cause of the condition. Lab. Invest. 63: 544-550, 1990. 2. Canet, D., Sunde, M., Last, A. M., Miranker, A., Spencer, A., Robinson, C. V., Dobson, C. M. Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants. Biochemistry 38: 6419-6427, 1999. 3. Dayhoff, M. O. Lactalbumin and Lysozyme. Atlas of Protein Sequence and Structure. Vol. 5. Washington: National Biomedical Research Foundation (pub.) 1972. Pp. D133-D140.