Recombinant Human LAMP-1/CD107a Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human LAMP1/CD107a is coated at 1 μg/mL, Recombinant Human Galectin‑3 (Catalog # 1154-GA) binds with an apparent K D <25 nM. |
Source |
Mouse myeloma cell line, NS0-derived human LAMP-1/CD107a protein Ala29-Met382 with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Ala29 & Met30 |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
LAMP1 |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note |
<0.01 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
39.2 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
100-110 kDa, reducing conditions |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions |
Reconstitute at 200 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human LAMP-1/CD107a Protein, CF
Background
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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