Lysosomal-associated membrane protein 1 is a glycoprotein from a family of Lysosome-associated membrane glycoproteins. [5] The LAMP-1 glycoprotein is a type I transmembrane protein [6] which is expressed at high or medium levels in at least 76 different normal tissue cell types. [7] It resides primarily across l ysosomal membranes, [8] and functions to provide selectins with carbohydrate ligands. [5] CD107a has also been shown to be a marker of degranulation on lymphocytes such as CD8+ and NK cells, [9] and may also play a role in tumor cell differentiation and metastasis. Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine. Schleutker J, Haataja L, Renlund M, Puhakka L, Viitala J, Peltonen L, Aula P (Nov 1991). "Confirmation of the chromosomal localization of human lamp genes and their exclusion as candidate genes for Salla disease". Human Genetics. 88 (1): 95–7. doi: 10.1007/BF00204936. PMID 1959930. S2CID 31520394. Carlsson SR, Fukuda M (Dec 1989). "Structure of human lysosomal membrane glycoprotein 1. Assignment of disulfide bonds and visualization of its domain arrangement". The Journal of Biological Chemistry. 264 (34): 20526–31. doi: 10.1016/S0021-9258(19)47094-4. PMID 2584229.

LAMP-1-deficient Normal Lysosomal Morphology and Function in LAMP-1-deficient

Sawada R, Jardine KA, Fukuda M (Apr 1993). "The genes of major lysosomal membrane glycoproteins, lamp-1 and lamp-2. 5'-flanking sequence of lamp-2 gene and comparison of exon organization in two genes". The Journal of Biological Chemistry. 268 (12): 9014–22. doi: 10.1016/S0021-9258(18)52972-0. PMID 8517882. Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine. Mattei MG, Matterson J, Chen JW, Williams MA, Fukuda M (May 1990). "Two human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2, are encoded by genes localized to chromosome 13q34 and chromosome Xq24-25, respectively". The Journal of Biological Chemistry. 265 (13): 7548–51. doi: 10.1016/S0021-9258(19)39148-3. PMID 2332441. PDBe-KB provides an overview of all the structure information available in the PDB for Human Lysosome-associated membrane glycoprotein 1

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The Blagdon Inpond 6000 is an instant solution for achieving a healthy, clear and beautiful pond. The pond filter has been designed for ponds up to 6000 litres in size and boasts 5 innovative features merged into one design - all of which remain unmatched when it comes to pond filters on the market right now. The innovation comes complete with 4 stunning fountain heads for a range of breathtaking effects. A low wattage LED spotlight automatically illuminates the pond during nighttime, switching on after dark to provide an eye-catching focal feature for your garden over those long summer nights. Höning S, Sandoval IV, von Figura K (Aug 1998). "A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3". The EMBO Journal. 17 (5): 1304–14. doi: 10.1093/emboj/17.5.1304. PMC 1170479. PMID 9482728. Kima, P. E.; Burleigh, B.; Andrews, N. W. (Dec 2000). "Surface-targeted lysosomal membrane glycoprotein-1 (Lamp-1) enhances lysosome exocytosis and cell invasion by Trypanosoma cruzi". Cellular Microbiology. 2 (6): 477–486. doi: 10.1046/j.1462-5822.2000.00071.x. ISSN 1462-5814. PMID 11207602. S2CID 19192092. Lee N, Wang WC, Fukuda M (Nov 1990). "Granulocytic differentiation of HL-60 cells is associated with increase of poly-N-acetyllactosamine in Asn-linked oligosaccharides attached to human lysosomal membrane glycoproteins". The Journal of Biological Chemistry. 265 (33): 20476–87. doi: 10.1016/S0021-9258(17)30529-X. PMID 2243101.

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a b c d e Carlsson SR, Fukuda M (Dec 1989). "Structure of human lysosomal membrane glycoprotein 1. Assignment of disulfide bonds and visualization of its domain arrangement". The Journal of Biological Chemistry. 264 (34): 20526–31. doi: 10.1016/S0021-9258(19)47094-4. PMID 2584229. a b c d e f g h Andrejewski N, Punnonen EL, Guhde G, Tanaka Y, Lüllmann-Rauch R, Hartmann D, von Figura K, Saftig P (Apr 1999). "Normal lysosomal morphology and function in LAMP-1-deficient mice". The Journal of Biological Chemistry. 274 (18): 12692–701. doi: 10.1074/jbc.274.18.12692. PMID 10212251. Residing primarily across lysosomal membranes, these glycoproteins consist of a large, highly glycosylated end with N-linked carbon chains on the luminal side of the membrane, and a short C-terminal tail [6] exposed to the cytoplasm. [8] The extracytoplasmic region contains a hinge-like structure which can form disulphide bridges homologous to those observed in human immunoglobulin A. [8] Other characteristics of the structure of the LAMP-1 glycoproteins include: a b c Carlsson SR, Roth J, Piller F, Fukuda M (Dec 1988). "Isolation and characterization of human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Major sialoglycoproteins carrying polylactosaminoglycan". The Journal of Biological Chemistry. 263 (35): 18911–9. doi: 10.1016/S0021-9258(18)37369-1. PMID 3143719.Significant quantities of polylactosaminoglycan and sialic acid to traverse the trans- Golgi cisternae. [10] Lysosomal-associated membrane protein 1 ( LAMP-1) also known as lysosome-associated membrane glycoprotein 1 and CD107a ( Cluster of Differentiation 107a), is a protein that in humans is encoded by the LAMP1 gene. The human LAMP1 gene is located on the long arm (q) of chromosome 13 at region 3, band 4 (13q34). Immunofluorescence staining of HeLa Cells with antibody to reveal lysosomal LAMP1 in red and vimentin containing intermediate filaments in green. Nuclear DNA is seen in blue. Antibodies and image courtesy EnCor Biotechnology Inc.