Lysosomal-Associated Membrane Protein 1 (LAMP1) antibody

Details for Product No. ABIN361797
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Synonyms AI196048, CD107a, Lamp-1, LAMPA, LGP120, LEP100
Rat (Rattus), Hamster
(181), (76), (59), (9), (6), (3), (3), (2)
(122), (97), (41), (2)
Clonality (Clone)
Monoclonal ()
(32), (25), (20), (14), (5), (3), (3), (3), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Western Blotting (WB), Immunoprecipitation (IP), Immunocytochemistry (ICC)
(142), (123), (62), (51), (45), (41), (38), (25), (19), (10), (6), (5), (2), (2), (2), (1), (1), (1)
Pubmed 5 references available
Quantity 100 μg
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Catalog No. ABIN361797
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Immunogen Rat liver lysosomal membrane preparations
Clone Ly1C6
Isotype IgG1
Specificity Detects an approx. 120 kDa protein corresponding to the molecular mass of LAMP1 on SDS PAGE immunoblots.
Sensitivity 1 µg/ml was sufficient for detection of LAMP1 in rat liver miscrosome by ECL immunoblot analysis.
Purification Protein G Purified
Alternative Name LAMP1
Background Synonyms:
CD107, CD107a, LAMPA, LGP120, IgpA
Lysosme associated membrane proteins, or LAMP1 and LAMP2, are major constituents of the lysosomal membrane. The two have closely related structures,with 37 % sequence homology. They are both transmembrane glycoproteins that are localized primarily in lysosomes and late endosomes. Newly synthesized molecules are mostly transported from the trans-Golgi network directly to endosomes and then to lysosomes. A second pathway involves the lamps being delivered from the Golgi to the cell surface, and then along the endocytic pathway to the lysosomes. A minor pathway involves transport via the plasma membrane.Upon stimulation, a rapid translocation of intracellular LAMPs to the cell membrane is dependent on a carboxyl-terminal tyrosine based motif (YXXI). If there is a disturbance in this spacing, lysosome localization of LAMP1 is abolished and the mutant protein then cycles between the membrane and the endosome. This stimulation has also been shown to have an associated release of histamine, leukotriene C and prostaglandinD, which shows that LAMP-1 and LAMP-2 are activation markers for normal mast cells. They have also been linked to the inflammatory response in that they promote adhesion of human peripheral blood mononuclear cells (PBMC) to vascular endothelium, and therefore possibly the adhesion of PBMC to the site of inflammation.
Gene ID 25328
NCBI Accession NP_036989
UniProt P14562
Research Area Cancer, Hematopoietic Progenitors, Organelles, Chaperones
Application Notes Recommended Dilution: 1 µg/mL was sufficient for detection by immunoblot analysis
Restrictions For Research Use only
Concentration 1 mg/mL
Buffer PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
anti-Lysosomal-Associated Membrane Protein 1 (LAMP1) antibody Lamp1 (Ly1C6), IF in transfected HeLa cells Courtesy of Robert H Edwards, U of Cali, San Fran School of Medicine.
anti-Lysosomal-Associated Membrane Protein 1 (LAMP1) antibody (2) LAMP1 WB 1 in 1000 rat liver micosomes 20ug copy.
Background publications Grützkau, Smorodchenko, Lippert et al.: "LAMP-1 and LAMP-2, but not LAMP-3, are reliable markers for activation-induced secretion of human mast cells." in: Cytometry. Part A : the journal of the International Society for Analytical Cytology, Vol. 61, Issue 1, pp. 62-8, 2004 (PubMed).

Jones, Jiang, Yamamoto et al.: "Tuberin is a component of lipid rafts and mediates caveolin-1 localization: role of TSC2 in post-Golgi transport." in: Experimental cell research, Vol. 295, Issue 2, pp. 512-24, 2004 (PubMed).

Kannan, Stewart, Bounds et al.: "Lysosome-associated membrane proteins h-LAMP1 (CD107a) and h-LAMP2 (CD107b) are activation-dependent cell surface glycoproteins in human peripheral blood mononuclear cells which mediate cell adhesion to vascular endothelium." in: Cellular immunology, Vol. 171, Issue 1, pp. 10-9, 1996 (PubMed).

Rohrer, Schweizer, Russell et al.: "The targeting of Lamp1 to lysosomes is dependent on the spacing of its cytoplasmic tail tyrosine sorting motif relative to the membrane." in: The Journal of cell biology, Vol. 132, Issue 4, pp. 565-76, 1996 (PubMed).

Lewis, Green, Marsh et al.: "Glycoproteins of the lysosomal membrane." in: The Journal of cell biology, Vol. 100, Issue 6, pp. 1839-47, 1985 (PubMed).

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