When Recombinant Human MCAM/CD146 Fc Chimera is immobilizedat 1 μg/mL, 100 μL/well, Recombinant Human Galectin-3 (Catalog # 8259-GA) binds with an ED50 of 0.25‑1.25 ug/mL.
Recombinant Human MCAM/CD146 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human MCAM/CD146 Fc Chimera is immobilized at 1 μg/mL, 100 μL/well, it binds Recombinant Human Galectin-3
(Catalog #
8259-GA). The
concentration
of Recombinant Human Galectin-3 that
produces 50% of the optimal binding response is 0.25‑1.25 μg/mL.
Source
Mouse myeloma cell line, NS0-derived human MCAM/CD146 protein
Human MCAM/CD146 (Val24-Gly559) Accession # AAA20922
>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
87 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
108-124 kDa, reducing condtions
Publications
Read Publications using 9709-MA in the following applications:
Melanoma
cell adhesion molecule (MCAM), also known as MUC18 or CD146, is a putative
adhesion molecule that belongs to the immunoglobulin superfamily (IgSF) (1). MCAM is an approximately 113 kDa type I
transmembrane glycoprotein that contains a 536 amino acid (aa) extracellular
domain (ECD), a 24 aa transmembrane domain, and a 63 aa cytoplasmic domain. Two
MCAM splice variants have been observed, which vary in the length of their
cytoplasmic tail (2). The ECD of human MCAM contains 2 IgV and 3 IgC2 domains
and shares 74% and 73% identity with mouse and rat, respectively. MCAM was originally described as a marker of
malignant potential in melanoma and was reported to promote both invasion and
metastasis (3). Since then, expression
has been detected in endothelial cells throughout the body and MCAM has been
shown to be involved multiple cellular events including adhesion, migration,
proliferation and differentiation (4, 5). Additionally, MCAM has been
implicated in recruitment of activated T cells to inflammatory sites and is
up-regulated in various inflammatory diseases (5, 6). Inhibiting MCAM signaling has been suggested
as a potential therapy for diverse diseases including inflammatory bowel
disease and ovarian cancer (7, 8). As
a cellular adhesion molecule (CAM), MCAM functions as a molecular mediator to
facilitate inter-cellular interactions of homotypic or heterotypic cells, or to
intervene in interactions of cell-to-extracellular matrix for responding to
physiological signal (9). MCAM has also been shown to be the functional ligand
for Galectin-3 on endothelial cell surfaces (9).
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