TIM-4/TIMD-4 Protein, Mouse (HEK293, His)

TIM-4/TIMD-4 Protein, a phosphatidylserine receptor, regulates the immune response through diverse roles. It participates in apoptotic cell phagocytosis and modulates T-cell function. In T-cell activation, it induces cell cycle arrest in naive T-cells while enhancing activated T-cell proliferation through AKT1 and ERK1/2 phosphorylation. TIM-4/TIMD-4 plays a pivotal role in efferocytosis, directly binding to apoptotic cell phosphatidylserine for engulfment. Additionally, it promotes autophagy by suppressing NLRP3 inflammasome activity via the STK11/PRKAA1 pathway in a phosphatidylserine-dependent mechanism. The protein's homodimer formation contributes to its multifaceted immune regulation. TIM-4/TIMD-4 Protein, Mouse (HEK293, His) is the recombinant mouse-derived TIM-4/TIMD-4 protein, expressed by HEK293, with C-His labeled tag. The total length of TIM-4/TIMD-4 Protein, Mouse (HEK293, His) is 257 a.a., with molecular weight of 60-70 kDa.

TIM-4/TIMD-4 Protein acts as a phosphatidylserine receptor with diverse roles in the immune response, participating in both the phagocytosis of apoptotic cells and the regulation of T-cell function. Its involvement in T-cell activation is bimodal, as it decreases the activation of naive T-cells by inducing cell cycle arrest while concurrently enhancing the proliferation of activated T-cells through the activation of AKT1 and ERK1/2 phosphorylations and subsequent signaling pathways. Additionally, TIM-4/TIMD-4 plays a pivotal role in efferocytosis, the process of phagocytosis of apoptotic cells, by directly binding to phosphatidylserine on apoptotic cells, thereby facilitating their engulfment by phagocytes. This function is distinctive, as other engulfment receptors like MERTK are more efficient in recognizing and mediating the ingestion of apoptotic cells. Furthermore, TIM-4/TIMD-4 promotes the autophagy process by suppressing NLRP3 inflammasome activity through the activation of the STK11/PRKAA1 pathway in a phosphatidylserine-dependent mechanism. The protein forms homodimers, contributing to its multifaceted roles in immune regulation.

Mouse

HEK293

C-His

Q6U7R4/NP_848874.3 (A23-T279)

276891  [NCBI]

60-70 kDa

Greater than 90% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.