CADM1/IGSF4A Protein, Mouse (377a.a, HEK293, His)

CADM1/IGSF4A proteins coordinate Ca(2+)-independent homophilic and heterophilic cell adhesion with CADM3 and NECTIN3. Interaction with CRTAM enhances NK cell cytotoxicity and CD8+ T cell function. CADM1/IGSF4A Protein, Mouse (377a.a, HEK293, His) is the recombinant mouse-derived CADM1/IGSF4A protein, expressed by HEK293 , with C-His labeled tag. The total length of CADM1/IGSF4A Protein, Mouse (377a.a, HEK293, His) is 377 a.a., with molecular weight of ~38.5 kDa.

CADM1/IGSF4A Protein orchestrates homophilic cell-cell adhesion in a Ca(2+)-independent manner, as substantiated by multiple studies. Furthermore, it engages in heterophilic cell-cell adhesion with CADM3 and NECTIN3, independent of calcium levels. Its interaction with CRTAM not only fosters natural killer (NK) cell cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+ T-cells but also facilitates NK cell-mediated rejection of tumors expressing CADM1 in vivo. In mast cells, CADM1 may play a role in attachment to and communication with nerves, being indispensable for the development and survival of mast cells in vivo. The protein's involvement extends to regulating the retention of activated CD8+ T-cells within the draining lymph node and influencing the intestinal retention of intraepithelial CD4+ CD8+ T-cells. Additionally, CADM1 acts as a synaptic cell adhesion molecule, contributing to dendritic spine formation and synapse assembly, while potentially influencing neuronal migration, axon growth, pathfinding, and fasciculation. Its diverse roles also encompass participation in spermatogenesis, including the adhesion of spermatocytes and spermatids to Sertoli cells and their differentiation into mature spermatozoa. The intricate network of CADM1 interactions involves homodimerization, association with FARP1, CRTAM, EPB41L3/DAL1, MPP2, MPP3, and PALS2, providing a comprehensive framework for understanding its multifaceted contributions.

Mouse

HEK293

C-His

Q8R5M8 (M1-H377)

54725  [NCBI]

Approximately 38.5 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.