Detection of JAM‑C (CD323) in B16‑F1 Mouse Cell Line by Flow Cytometry.
B16‑F1 mouse melanoma cell line was stained with Rat Anti-Mouse JAM‑C (CD323) APC‑conjugated Monoclonal Antibody (Catalog # FAB7050A, filled histogram) or isotype control antibody (Catalog # IC013A, open histogram). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze.
12 months from date of receipt, 2 to 8 °C as supplied.
JAM-C (Junctional Adhesion Molecule-C), also known as JAM-3 and JAM-2, is a 40-45 kDa member of
the JAM family, IgSF of molecules. It is
a type I transmembrane glycoprotein that is further classified as a classical
JAM with a short cytoplasmic tail vs. non-classical JAMs that contain long
cytoplasmic tails. Mature mouse JAM-C is
289 amino acids (aa) in length, and contains a 212 aa extracellular
region. This region possesses one
N-terminal V-type and one C2-type Ig-like domain (aa 30-241). In human, JAM-C is perhaps best known as a
component of the epithelial cell tight junction. In concert with two other transmembrane
protein types (claudins and occludin) in-cis,
JAM-C forms an intercellular barrier complex that restricts paracellular
permeability. In mouse, however, this
application may not apply, as endothelium, rather than epithelium, appears to
be site of maximum expression. In this
locale, JAM-C is suggested to regulate neutrophil exodus from the blood, and
provide a barrier against reverse migration back into the vasculature. In any event, binding partners for JAM-C in-trans include JAM-B, Mac-1, alpha x beta 2
and JAM-C itself. Cells known to
express JAM-C in mouse do not necessarily mirror those expressing JAM-C in
human. Mouse cells known to contain
JAM-C are limited in type and include endothelium, high endothelial venules,
fibroblasts, hematopoietic stem cells, Schwann cells involved in myelination,
and neurons of an Aδ (or pain sensing)
phenotype. The extracellular domain of
mouse JAM-C shares 96% and 87% aa sequence identity with the extracellular
domains of rat and human JAM-C, respectively.
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Cells were pre-gated with live/dead and FSC-A/W to exclude dead cells and cell doublets. The single cell suspension was isolated from lung of a WT B6 mouse and stained with the JAM-C (CD323) APC-conjugated antibody (1:100) for 30 minutes. Cells were analyzed by flow cytometer.