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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
MLXIP antibody detects MLX-interacting protein, a glucose responsive transcriptional regulator that links cellular metabolic status to gene expression programs controlling growth, proliferation, and nutrient utilization. The UniProt recommended name is MLX-interacting protein (MLXIP). MLXIP belongs to the basic helix-loop-helix leucine zipper family and functions primarily as a transcriptional cofactor for the MLX network, a nutrient sensing system that integrates carbohydrate availability with metabolic and biosynthetic output. Through these regulatory activities, MLXIP influences glycolysis, amino acid metabolism, stress adaptation, and anabolic growth pathways.
MLXIP antibody identifies a protein of approximately 415 amino acids that localizes to both cytoplasmic and nuclear compartments depending on glucose levels. Under low nutrient conditions, MLXIP is largely cytoplasmic and remains transcriptionally inactive. When glucose availability increases, MLXIP becomes activated through carbohydrate derived metabolites, including glucose 6 phosphate, and translocates into the nucleus where it binds MLX to form a functional transcription complex. This MLX-MLXIP complex directly regulates carbohydrate response element containing genes involved in glycolysis, glucose transport, lipogenesis, and biosynthetic pathways required for cell growth.
The MLXIP gene is located on chromosome 12q24.31 and is expressed broadly across metabolic, proliferative, and endocrine tissues, including liver, skeletal muscle, pancreas, adipose tissue, and developing organs. Its expression pattern reflects its role as a metabolic sensor capable of adjusting transcriptional output in response to nutrient availability. In hepatocytes, MLXIP contributes to regulation of glycolytic and lipogenic gene programs and works in parallel with other nutrient responsive factors, such as ChREBP, to control glucose utilization. In skeletal muscle, MLXIP participates in transcriptional responses to exercise induced energy demand and nutrient recovery. In endocrine tissues, MLXIP helps integrate glucose signals into hormone secretion and metabolic coupling mechanisms.
At the molecular level, MLXIP contains a basic helix-loop-helix leucine zipper domain that mediates dimerization with MLX and binding to specific carbohydrate response motifs within target promoters. It also contains regulatory regions responsive to intracellular metabolites that influence nuclear translocation and DNA binding. MLXIP activity is enhanced in the presence of glucose derived metabolites, making it a key transcriptional effector of nutrient flux. Through these mechanisms, MLXIP coordinates metabolic responses important for anabolic growth, energy allocation, and maintenance of metabolic homeostasis.
MLXIP also participates in stress response pathways. Under metabolic stress, oxidative stress, or nutrient deprivation, MLXIP expression or activity may be reduced, leading to shifts in target gene expression that favor protective metabolic states. MLXIP interacts with additional transcriptional regulators involved in cell survival, mitochondrial adaptation, and cellular redox control. Because MLXIP responds to both nutrient availability and metabolic stress, it functions as a nodal point linking environmental cues to transcriptional networks that preserve cellular integrity and energy balance.
Pathologically, dysregulation of MLXIP has been associated with metabolic disease, cancer, and disorders involving altered nutrient sensing. Elevated MLXIP activity has been observed in several tumor types where increased glucose uptake fuels proliferation. In these contexts, MLXIP supports biosynthetic demands by driving expression of genes involved in glycolysis, amino acid metabolism, and lipid synthesis. MLXIP also contributes to metabolic rewiring in cancer cells, enabling adaptation to fluctuating nutrient landscapes within the tumor microenvironment. Conversely, impaired MLXIP function can contribute to metabolic dysfunction, affecting insulin sensitivity, hepatic lipid metabolism, and energy balance.
In metabolic disease research, MLXIP has been examined for its role in hepatic steatosis, glucose intolerance, and adipocyte biology. Increased carbohydrate flux can enhance MLXIP mediated transcriptional programs that promote lipid synthesis and storage. Inflammation and nutrient stress may modulate MLXIP activity, further linking it to systemic metabolic regulation. MLXIP has also been implicated in proliferation and differentiation pathways in endocrine and epithelial tissues, supporting its broader involvement in growth control.
As nutrient sensing and metabolic transcriptional control continue to rise in scientific importance, MLXIP has become a key molecule of interest. Its responsiveness to glucose derived metabolites and its ability to modulate gene programs central to metabolic adaptation make it relevant to studies of diabetes, obesity, cancer biology, and cellular stress responses. Research using MLXIP antibody supports detailed examination of MLX driven transcription networks, metabolic gene regulation, and nutrient responsive signaling pathways.
MLXIP antibody is validated for use in relevant research applications to detect MLX-interacting protein expression and study its roles in metabolic regulation, transcriptional control, and nutrient sensing. NSJ Bioreagents provides MLXIP antibody reagents optimized for studies in metabolism, endocrinology, oncology, and cellular stress biology.
Optimal dilution of the MLXIP antibody should be determined by the researcher.
Recombinant human protein (amino acids H88-P348) was used as the immunogen for the MLXIP antibody.
After reconstitution, the MLXIP antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
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