Recombinant Mouse LAMP-2/CD107b Fc Chimera Protein, CF Summary
Accession # P17047.2
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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 500 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.
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 at 109-122 kDa and 210-240 kDa, respectively.
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).
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