Hetyre Night Light Bluetooth Speaker, 5 in 1 Touch Control Bedside Lamp Dimmable Multi-Color Changing, Bedroom Alarm Clock, Best Birthday Gift Ideas for 10 11 12 13 14 Year Old Teenage Girls/Boys

£14.995
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Hetyre Night Light Bluetooth Speaker, 5 in 1 Touch Control Bedside Lamp Dimmable Multi-Color Changing, Bedroom Alarm Clock, Best Birthday Gift Ideas for 10 11 12 13 14 Year Old Teenage Girls/Boys

Hetyre Night Light Bluetooth Speaker, 5 in 1 Touch Control Bedside Lamp Dimmable Multi-Color Changing, Bedroom Alarm Clock, Best Birthday Gift Ideas for 10 11 12 13 14 Year Old Teenage Girls/Boys

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Price: £14.995
£14.995 FREE Shipping

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LAMP1 expression on the surface of tumor cells has been observed for a number of different cancer types, particularly in highly metastatic cancers such as pancreatic cancer, [18] [19] colon cancer [16] [17] and melanoma. [16] [17] The structure of LAMP1 correlates with differentiation [8] [20] and metastatic potential [11] of tumor cells as it is thought to help mediate cell-cell adhesion [17] and migration. [15] [18] Indeed, the adhesion of some cancer cells to the extracellular matrix is mediated by interactions between LAMP1 and LAMP2 and E-selectin and galectins, with the LAMPs serving as ligands for the cell-adhesion molecules. [17] Furuta K, Yang XL, Chen JS, Hamilton SR, August JT (May 1999). "Differential expression of the lysosome-associated membrane proteins in normal human tissues". Archives of Biochemistry and Biophysics. 365 (1): 75–82. doi: 10.1006/abbi.1999.1147. PMID 10222041. 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. Polylactosamine attachments which protect the glyocoprotein from degradation by lysosomal proteases [10] a b c Jensen SS, Aaberg-Jessen C, Christensen KG, Kristensen B (2013). "Expression of the lysosomal-associated membrane protein-1 (LAMP-1) in astrocytomas". International Journal of Clinical and Experimental Pathology. 6 (7): 1294–1305. PMC 3693194. PMID 23826410.

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. 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): 9014–9022. doi: 10.1016/S0021-9258(18)52972-0. PMID 8517882. 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. 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. Zhang H, Li XJ, Martin DB, Aebersold R (Jun 2003). "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry". Nature Biotechnology. 21 (6): 660–6. doi: 10.1038/nbt827. PMID 12754519. S2CID 581283.Howe CL, Granger BL, Hull M, Green SA, Gabel CA, Helenius A, Mellman I (Oct 1988). "Derived protein sequence, oligosaccharides, and membrane insertion of the 120-kDa lysosomal membrane glycoprotein (lgp120): identification of a highly conserved family of lysosomal membrane glycoproteins". Proceedings of the National Academy of Sciences of the United States of America. 85 (20): 7577–81. Bibcode: 1988PNAS...85.7577H. doi: 10.1073/pnas.85.20.7577. PMC 282235. PMID 3174652.

PDBe-KB provides an overview of all the structure information available in the PDB for Human Lysosome-associated membrane glycoprotein 1 When shopping for a smart lamp, first consider its use. Where do you want to place this lamp? Is it for reading, lighting up a room, or ambiance? A properly lit room should have between five to seven light sources. And ideally, they should be a mix of different types of lights, positioned throughout the room at varied heights and. By combining floor lamps, table lamps and wall lamps, it'll be easier for you to create perfect lighting and help your room come to life. Use height when deciding on indoor lighting Storage & organisation Furniture Textiles Kitchenware & tableware Kitchens Lighting Decoration Rugs, mats & flooring Beds & mattresses Baby & children Smart home Bathroom products Laundry & cleaning Plants & plant pots Home electronics Home improvement Outdoor living Food & beverages Christmas Shop Shop by room LAMP1 and LAMP2 glycoproteins comprise 50% of all lysosomal membrane proteins, [6] and are thought to be responsible in part for maintaining lysosomal integrity, pH and catabolism. [6] [11] The expression of LAMP1 and LAMP2 glycoproteins are linked, as deficiencies in LAMP1 gene will lead to increased expression of LAMP2 glycoproteins. [11] The two are therefore thought to share similar functions in vivo. [6] However, this makes the determining the precise function of LAMP1 difficult, because while the LAMP1 deficient phenotype is little different than the wild type due to LAMP2 up regulation, [6] [11] the LAMP1/ LAMP2 double deficient phenotype leads to embryonic lethality. [11]To help you improve the lighting in your home, we have everything from ceiling to floor lamps, as well as all of the in-betweens. A lamp here, a lamp there 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.



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