Human LAMP-2/CD107b PE-conjugated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: LAMP-2/CD107b

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 human LAMP-2 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 small amount of O-linked glycosylation (2, 3). Alternate splicing generates a human LAMP-2 isoform (LAMP-2B) with a substituted juxtamembrane lumenal region, transmembrane segment, and cytoplasmic tail (4). Within the lumenal domain, human LAMP-2 shares approximately 64% aa sequence identity with mouse and rat LAMP-2. LAMP-2 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).

Product Datasheets

Related Research Areas

• Common Macrophage Markers
• Granulocyte Markers
• Isolation, Culture, and Identification of Natural Killer Cells
• Lysosomal Enzymes