Recombinant Human LAMP-2/CD107b Protein, CF Summary
Product Specifications
Leu29-Phe375, with a C-terminal 10-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
6228-LM
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 700 μg/mL in PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
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).
- Eskelinen, E.-L. et al. (2003) Trends Cell Biol. 13:137.
- Fukuda, M. et al. (1988) J. Biol. Chem. 263:18920.
- Carlsson, S.R. et al. (1988) J. Biol. Chem. 263:18911.
- Konecki, D.S. et al. (1995) Biochem. Biophys. Res. Commun. 215:757.
- Cuervo, A.M. and J.F. Dice (2000) Traffic 1:570.
- Cuervo, A.M. and J.F. Dice (1996) Science 273:501.
- Tanaka, Y. et al. (1990) Nature 406:902.
- Peters, P.J. et al. (1991) J. Exp. Med. 173:1099.
- Betts, M.R. et al. (2003) J. Immunol. Meth. 281:65.
- Grutzkau, A. et al. (2004) Cytometry 61:62.
- Kannan, K. et al. (1996) Cell. Immunol. 171:10.
- Silverstein, R.L. and M. Febbraio (1992) Blood 80:1470.
- Skrincosky, D.M. et al. (1993) Cancer Res. 53:2667.
- Inohara, H. and Raz, A. (1994) Biochem. Biophys. Res. Commun. 201:1366.
- Ohannesian D.W. et al. (1994) Cancer Res. 54:5992.
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