Recombinant Human LAMP-1/CD107a Protein, CF Summary
Product Specifications
Ala29-Met382 with a C-terminal 6-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.
4800-LM
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 200 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-1/CD107a
Lysosomal associated membrane protein 1 (LAMP1), also known as CD107a and LGP120, is an approximately 120 kDa transmembrane glycoprotein that is a major protein component of lysosomal membranes (1). Mature human LAMP1 consists of a 354 amino acid (aa) intralumenal domain (ECD), a 23 aa transmembrane segment, and a 12 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). Within the lumenal domain, human LAMP1 shares approximately 64% aa sequence identity with mouse and rat LAMP1. The sorting of LAMP1 to lysosomes relies on a tyrosine motif in the cytoplasmic tail (3, 4). In cytotoxic T cells and mast cells, LAMP1 is expressed in the membranes of intracellular granules that contain effector molecules such as perforin, granzymes, eicosanoids, and histamine (5-7). LAMP1 is presented on the plasma membrane during the activation of NK cells, CD8+ T cells, mast cells, basophils, monocytes, and platelets (6-12). A glycoform of LAMP1 known as M150 is expressed on the surface of activated macrophages where it promotes T cell costimulation and a Th1 biased immune response (13). Exposure of epithelial cells to pathogenic Neisseria bacteria induces the redistribution of LAMP1 to the cell surface where it can be cleaved by the Neisseria IgA1 protease (14). LAMP1 is a native ligand for lectins Galectin-1 and Galectin-3 (15‑17).
- Eskelinen, E.L. et al. (2003) Trends Cell Biol. 13:137.
- Viitala, J. et al. (1988) Proc. Natl. Acad. Sci. 85:3743.
- Carlsson, S.R. et al. (1988) J. Biol. Chem. 263:18911.
- Rohrer, J. et al. (1996) J. Cell Biol. 132:565.
- 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.
- Alter, G. et al. (2004) J. Immunol. Meth. 294:15.
- Tomescu, C. et al. (2009) J. Leukoc. Biol. 85:871.
- Hennersdorf, F. et al. (2005) Cell Res. 15:325.
- Kannan, K. et al. (1996) Cell. Immunol. 171:10.
- Fabbraio, M. and R.L. Silverstein (1990) J. Biol. Chem. 265:18531.
- Prasad, D.V.R. et al. (2002) J. Immunol. 169:1801.
- Lin, L. et al. (1997) Mol. Microbiol. 24:1083.
- 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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