The mouse monoclonal antibody EM-53 recognizes RLTPR / CARMIL2, a protein playing a role in actin filament elongation.
RLTPR/CARMIL2 (RGD motif, leucine rich repeats, tropomodulin domain and proline-rich containing; capping protein regulator and myosin 1 linker 2), also known as LRRC16C, is a cytosolic protein, which with high affinity binds CAPZA2 (capping protein muscle actin Z-line alpha 2) and decreases CAPZA2 affinity for actin barbed ends. RLTPR/CARMIL2 increases the rate of actin filament elongation from seeds in the presence of CAPZA2, however, seems unable to nucleate filaments. Its interaction with CAPZA2 is essential for lamellipodial protrusion and cell translocation. RLTPR/CARMIL2 is crucial for T cell costimulation via CD28 and this property seems to be independent on its actin-uncapping function. The lack of functional RLTPR/CARMIL2 molecules impeded the differentiation toward Th1 and Th17 fates of both human and murine CD4+ T cells and leads to combined immunodeficiency. Expression of RLTPR/CARMIL2 was also detected in human and murine B cells, but it seems not to be involved in BCR-mediated signaling.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: Capping protein regulator and myosin 1 linker 2; Capping protein, Arp2/3 and myosin-I linker protein 2; F-actin-uncapping protein RLTPR; leucine rich repeat containing 16C; Leucine-rich repeat-containing protein 16C; RGD motif, leucine rich repeats, tropomodulin domain and proline-rich containing; RGD, leucine-rich repeat, tropomodulin and proline-rich containing protein; RGD, leucine-rich repeat, tropomodulin and proline-rich-containing protein
Gene Aliases: CARMIL2; CARMIL2b; CG1399-PB; D130029J02Rik; Gm585; LRRC16C; RLTPR