Recombinant Human ALPPL2 cell lysate

Manipulating ALPPL2 activity and function holds promise for modulating cellular processes and disease outcomes, potentially offering new therapeutic avenues for metabolic disorders, liver diseases, and lipid-related conditions.

Dysregulation or deficiency of ALPPL2 has been associated with metabolic disorders, liver diseases, and dyslipidemia, highlighting its contribution to the pathogenesis of these conditions.

ALPPL2 may serve as a potential diagnostic biomarker for specific diseases, providing insights into disease progression and therapeutic response, and it could be explored as a therapeutic target for developing interventions in certain pathological contexts.

ALPPL2 participates in cellular processes such as lipid metabolism, cell signaling, and membrane dynamics, and it interacts with other proteins and molecules involved in these processes.

ALPPL2 expression and activity are influenced by various physiological and pathological stimuli, including hormonal regulation, nutrient availability, and disease conditions.

ALPPL2 exhibits a specific expression pattern, with higher levels in certain tissues such as the liver, kidney, and intestine, and it is primarily localized to the plasma membrane or specific subcellular compartments.

ALPPL2 regulates downstream signaling pathways and molecular targets involved in lipid metabolism, cell proliferation, and cell survival, influencing cellular processes such as lipid signaling, membrane trafficking, and cell growth.

ALPPL2 is involved in the metabolism and turnover of its substrates, including lipid molecules and membrane components, playing important roles in cellular lipid homeostasis and membrane remodeling.

ALPPL2 expression is controlled by transcriptional regulators, signaling pathways, and epigenetic modifications that respond to specific cellular signals and environmental cues.

ALPPL2 activity can be modulated by specific factors, such as hormones or lipid-binding proteins, and inhibitors that target its catalytic site or affect its membrane association, leading to altered enzymatic activity and cellular functions.