OLFM4 Protein, Human (HEK293, His)

OLFM4 Protein is implicated in potentially promoting the proliferation of pancreatic cancer cells by facilitating the transition from the S to G2/M phase, underscoring its potential role in the cell cycle dynamics of cancerous cells. Conversely, in myeloid leukemic cell lines, OLFM4 inhibits cell growth while inducing cell differentiation and apoptosis, indicating its dual role in distinct cellular contexts. Additionally, it may contribute to the inhibition of EIF4EBP1 phosphorylation/deactivation, suggesting a potential role in modulating protein translation processes. OLFM4 is known to facilitate cell adhesion, possibly through interactions with cell surface lectins and cadherin. Structurally, OLFM4 exists as a homomultimer with disulfide linkages. It interacts with NDUFA13 and exhibits binding affinity to cell surface lectins, including locutions ricinus communis agglutinin I, concanavalin-A, and wheat germ agglutinin, along with cadherin. The multifaceted functions and interactions of OLFM4 highlight its significance in cellular processes with implications in cancer progression and cell adhesion. Further research is crucial to unravel the precise molecular mechanisms through which OLFM4 modulates diverse cellular functions.