• Purity

  >95%, by SDS-PAGE under reducing conditions and visualized by silver stain

• Endotoxin Level

  <0.01 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its binding ability in a functional ELISA. When Recombinant Human LAMP2/CD107b is coated at 1 μg/mL, Recombinant Human Galectin‑3 (Catalog # ) binds with an apparent K    _D <25 nM.  

• Source

  Mouse myeloma cell line, NS0-derived Leu29-Phe375, with a C-terminal 10-His tag

• Accession #

• N-terminal Sequence    
  Analysis

  Leu29

• Predicted Molecular Mass

  39.7 kDa

• SDS-PAGE

  100-110 kDa, reducing conditions

Background: LAMP-2/CD107b

Lysosomal associated membrane protein 2 (LAMP2), also known as CD107b and LGP110, is an approximately 110 kDa transmembrane glycoprotein that is a major component of lysosomal membranes (1). Mature human LAMP2 consists of a 347 amino acid (aa) intralumenal domain, a 24 aa transmembrane segment, and a 35 aa cytoplasmic tail (2). Its lumenal domain is organized into two heavily N-glycosylated regions separated by a Ser/Pro-rich linker that carries a minor amount of O‑linked glycosylation (2, 3). Alternate splicing generates a human LAMP2 isoform (LAMP2B) with a substituted juxtamembrane lumenal region, transmembrane segment, and cytoplasmic tail (4). Within the lumenal domain, human LAMP2 shares approximately 64% aa sequence identity with mouse and rat LAMP2. LAMP2 itself is subject to lysosomal degradation following cleavage of its lumenal domain (5). It mediates the lysosomal uptake of the chaperone HSC73 in complex with cargo proteins and is required for the lysosomal destruction of autophagic vacuoles (6, 7). In cytotoxic T cells and mast cells, LAMP2 is expressed in the membranes of intracellular granules that contain effector molecules such as perforin, granzymes, eicosanoids, and histamine (8-10). Up‑regulated LAMP2 at the plasma membrane serves as an indicator of cell activation of CD8  ⁺ T cells, mast cells, monocytes, and platelets (9-12). LAMP2 is a native ligand for lectins Galectin-1 and Galectin-3 (13‑15).

• References:

1. Eskelinen, E.-L. et al. (2003) Trends Cell Biol. 13:137.

2. Fukuda, M. et al. (1988) J. Biol. Chem. 263:18920.

3. Carlsson, S.R. et al. (1988) J. Biol. Chem. 263:18911.

4. Konecki, D.S. et al. (1995) Biochem. Biophys. Res. Commun. 215:757.

5. Cuervo, A.M. and J.F. Dice (2000) Traffic 1:570.

6. Cuervo, A.M. and J.F. Dice (1996) Science 273:501.

7. Tanaka, Y. et al. (1990) Nature 406:902.

8. Peters, P.J. et al. (1991) J. Exp. Med. 173:1099.

9. Betts, M.R. et al. (2003) J. Immunol. Meth. 281:65.

10. Grutzkau, A. et al. (2004) Cytometry 61:62.

11. Kannan, K. et al. (1996) Cell. Immunol. 171:10.

12. Silverstein, R.L. and M. Febbraio (1992) Blood 80:1470.

13. Skrincosky, D.M. et al. (1993) Cancer Res. 53:2667.

14. Inohara, H. and Raz, A. (1994) Biochem. Biophys. Res. Commun. 201:1366.

15. Ohannesian D.W. et al. (1994) Cancer Res. 54:5992.

• Long Name:

  Lysosome-associated Membrane Glycoprotein 2

• Entrez Gene IDs:

  3920 (Human)

• Alternate Names:

  CD107 antigen-like family member B; CD107b antigen; CD107b; LAMP2; LAMP-2; LAMPB; LGP110; lysosomal-associated membrane protein 2; lysosome-associated membrane glycoprotein 2; Lysosome-associated membrane protein 2