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LAMP1 antibody (Lysosomal-Associated Membrane Protein 1) (AA 25-224)

Details for Product anti-LAMP1 Antibody No. ABIN968337, Supplier: Log in to see
Antigen
  • AI196048
  • CD107a
  • Lamp-1
  • LAMPA
  • LGP120
  • LEP100
Epitope
AA 25-224
20
15
13
10
9
9
7
5
5
5
3
3
2
1
1
1
1
1
1
Reactivity
Human
255
123
82
24
14
8
5
3
2
Host
Mouse
189
103
57
2
Clonality (Clone)
Monoclonal ()
Conjugate
This LAMP1 antibody is un-conjugated
42
31
27
16
7
6
5
4
4
3
3
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
Application
Immunofluorescence (IF), Immunoprecipitation (IP), Western Blotting (WB)
179
165
74
73
72
64
44
33
27
19
14
12
4
3
3
2
2
1
1
1
1
1
1
Supplier
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Immunogen Human Lamp-1 aa. 25-224
Clone 25-Lamp
Isotype IgG2b
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Purification The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name Lamp-1 (LAMP1 Antibody Abstract)
Background Lysosomes are digestive compartments in mammalian cells that are responsible for the degradation of numerous substances including foreign materials. The lysosomal membrane is of interest due to its role in maintaining the acidic intralysosomal sac, its resistance to degradation, and its ability to fuse with other membranous organelles. Lamp-1 and lamp-2 (lysosomal-associated membrane proteins -1 and -2) were identified as lysosomal membrane proteins that act as carriers for poly-N-glycans, primarily N-acetyllactosamines. They consist of two heavily glycosylated amino terminal domains, a single trans-membrane domain, and a short cytoplasmic tail. A tyrosine located at the fourth residue from the end of the cytoplasmic tail, a large hydrophobic amino acid as the last residue, and a glycine residue amino terminal to the tyrosine residue targets these proteins from the TGN to the lysosome. The role of the Lamp molecules may be a carrier for poly-N-acetyllactosamines and/or to protect lysosomal membranes from the soluble hydrolases. This antibody is routinely tested by western blot analysis.
Molecular Weight 110 kDa
Pathways
Restrictions For Research Use only
Format Liquid
Concentration 250 μg/mL
Buffer Aqueous buffered solution containing BSA, glycerol, and ≤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
Storage Comment Store undiluted at -20° C.
Supplier Images
Western Blotting (WB) image for anti-LAMP1 antibody (Lysosomal-Associated Membrane Protein 1) (AA 25-224) (ABIN968337) Western blot analysis of Lamp-1 on HepG2 lysate. Lane 1: 1:250, lane 2: 1:500, lane 3...
 image for anti-LAMP1 antibody (Lysosomal-Associated Membrane Protein 1) (AA 25-224) (ABIN968337) anti-Lysosomal-Associated Membrane Protein 1 (LAMP1) (AA 25-224) antibody (Image 2)
Product cited in: Spoerl, Stumpf, Noegel et al.: "Oligomerization, F-actin interaction, and membrane association of the ubiquitous mammalian coronin 3 are mediated by its carboxyl terminus." in: The Journal of biological chemistry, Vol. 277, Issue 50, pp. 48858-67, 2002 (PubMed).

Alto, Soderling, Scott: "Rab32 is an A-kinase anchoring protein and participates in mitochondrial dynamics." in: The Journal of cell biology, Vol. 158, Issue 4, pp. 659-68, 2002 (PubMed).

Hocking, Kowalski: "A cryptic fragment from fibronectin's III1 module localizes to lipid rafts and stimulates cell growth and contractility." in: The Journal of cell biology, Vol. 158, Issue 1, pp. 175-84, 2002 (PubMed).

Fukuda, Viitala, Matteson et al.: "Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Comparison of their deduced amino acid sequences." in: The Journal of biological chemistry, Vol. 263, Issue 35, pp. 18920-8, 1989 (PubMed).

Fukuda: "Lysosomal membrane glycoproteins. Structure, biosynthesis, and intracellular trafficking." in: The Journal of biological chemistry, Vol. 266, Issue 32, pp. 21327-30, 1991 (PubMed).