When Recombinant Mouse LAMP‑2/CD107b Fc Chimera (Catalog # 10552-LM) is immobilized at 1 μg/mL (100 μL/well), it binds to Recombinant Human Galectin-3 (1154-GA) with an ED50 of 0.1-10 μg/mL
2 μg/lane of Recombinant Mouse LAMP-2/CD107b Fc Chimera (Catalog # 10552-LM) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands ...read more
Recombinant Mouse LAMP-2/CD107b Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Mouse LAMP‑2/CD107b Fc Chimera is immobilized at 1 μg/mL
(100 μL/well), it binds to Recombinant Human Galectin-3
(Catalog #
1154-GA)
with an ED50 of 0.1-10 μg/mL.
Source
Mouse myeloma cell line, NS0-derived mouse LAMP-2/CD107b protein
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
66 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
109-122 kDa, under reducing conditions
Publications
Read Publication using 10552-LM in the following applications:
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 visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 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 Mouse LAMP-2/CD107b Fc Chimera Protein, CF
CD107 antigen-like family member B
CD107b antigen
CD107b
LAMP2
LAMP-2
LAMP2A
LAMP-2A
LAMPB
LGP110
LGP-96
Lysosomal Associated Membrane Protein 2
lysosomal-associated membrane protein 2
lysosome-associated membrane glycoprotein 2
Lysosome-associated membrane protein 2
Background
Lysosomal associated membrane protein 2 (LAMP-2), also known as CD107b
and LGP110, is an approximately 110 kDa transmembrane glycoprotein that is a
major component of lysosomal membranes (1). Mature mouse LAMP-2 consists of a 354
amino acid (aa) intralumenal domain, a 25 aa transmembrane segment, and a 11 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 two additional mouse
LAMP-2 isoforms (LAMP-2B and LAMP-2C) with a substituted juxtamembrane lumenal
region, transmembrane segment, and cytoplasmic tail (4). Within the lumenal
domain, mouse LAMP-2 shares approximately 64% and 81% aa sequence identity with human
and rat LAMP-2, repectively. LAMP-2 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, LAMP-2 is expressed in the membranes of intracellular granules that
contain effector molecules such as perforin, granzymes, eicosanoids, and
histamine (8-10). Up‑regulated LAMP-2 at the plasma membrane serves as an
indicator of cell activation of CD8+ T
cells, mast cells, monocytes, and platelets (9-12). LAMP-2 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.
Lichter-Konecki, U. et al. (1999) Differentiation 65:43.
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.
Chaperone Mediated Autophagy (CMA) does it all! By Christina Towers, PhD. The degradation of cellular proteins is a critical step of both regulation and quality control and results in the turn over and recycling of critical amino acids. The two main mechanisms o... Read full blog post.
LAMP2 - a marker of lysosomes and late endosomes Lysosomes are membrane-bound organelles responsible for the degradation of various biological macromolecules. Vesicles containing hydrolytic enzymes bud from the Golgi and fuse with endosomes to form the mature lysosome capable of breaking down va... Read full blog post.
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