CMRF35-like molecule 1 Protein, Rat (Myc, His-SUMO)

CMRF35-like molecule 1 (CLM-1) Protein serves as an inhibitory receptor for myeloid and mast cells, crucial in immune homeostasis by regulating various immune responses. CLM-1 positively modulates macrophage-mediated efferocytosis by recognizing phosphatidylserine on apoptotic cells. It inhibits dendritic cell-mediated efferocytosis and Fc epsilon receptor-dependent mast cell activation. CLM-1 may act as a coreceptor for IL-4, enhancing IL-4- and IL-13-induced signaling. Additionally, it negatively regulates TLR signaling and inhibits osteoclast formation while inducing macrophage cell death. The protein interacts with PTPN6/SHP-1 and associates with IL4R. CMRF35-like molecule 1 Protein, Rat (Myc, His-SUMO) is the recombinant rat-derived CMRF35-like molecule 1 protein, expressed by E. coli, with N-His, C-Myc, N-SUMO labeled tag. The total length of CMRF35-like molecule 1 Protein, Rat (Myc, His-SUMO) is 163 a.a., with molecular weight of ~38.3 kDa.

CMRF35-like molecule 1 (CLM-1) protein serves as an inhibitory receptor for myeloid cells and mast cells, playing a crucial role in immune homeostasis by modulating various immune responses. CLM-1 positively regulates the phagocytosis of apoptotic cells, known as efferocytosis, through the recognition and binding of phosphatidylserine (PS) on the surface of apoptotic cells. This activity promotes macrophage-mediated efferocytosis while inhibiting dendritic cell-mediated efferocytosis. Furthermore, CLM-1 negatively regulates Fc epsilon receptor-dependent mast cell activation and allergic responses by binding to ceramide and sphingomyelin as ligands. It may also function as a coreceptor for interleukin 4 (IL-4), interacting with and regulating IL-4 receptor alpha-mediated responses, thereby augmenting IL-4- and IL-13-induced signaling. In addition, CLM-1 negatively regulates Toll-like receptor (TLR) signaling by activating phosphatases PTPN6/SHP-1 and PTPN11/SHP-2. Beyond its immunomodulatory functions, CLM-1 inhibits osteoclast formation and induces macrophage cell death upon engagement. The protein interacts with PTPN6/SHP-1 in a tyrosine phosphorylation-dependent manner and associates with IL4R.

Rat

E. coli

N-His;C-Myc;N-SUMO

Q566E6 (19A-181S)

287818  [NCBI]

AQDPVTGPEEVSGYEQGSLTVWCRYGSWWKDYSKYWCRGPKRSSCEIRVETDASERLVKENHVSIRDDQTNFTFTVTMEDLRMSDAGIYWCGITKAGYDHMFKVHVSINPVPTTPTTTSTTTIFTVTTTVKETSTLSTQTSHYSDNRYDSGGVGDGNGFLDLS

Approximately 38.3 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.