PASK Antibodies

Background

The PASK gene encodes a serine/threonine protein kinase, which serves as a key receptor for cellular metabolic status and senses intracellular energy changes and regulates metabolic balance through its PAS domain. It can regulate key physiological processes such as insulin secretion, glycogen metabolism and mitochondrial biosynthesis based on the availability of nutrients (such as glucose). This gene was identified in the early 21st century. Its unique dual-kinase domain (one for substrate phosphorylation and the other for self-regulation) provides an important model for studying the energy sensing mechanism. The activity regulation mechanism of PASK and its role in metabolic diseases have become an important research direction in the current field of signal transduction and metabolic regulation, providing a molecular basis for understanding how cells coordinate the relationship between energy supply and demand.

Structure Function Application Advantage Our Products

Structure of PASK

PASK is a serine/threonine protein kinase with a molecular weight of approximately 150-160 kDa. This protein contains the N-terminal PAS domain and the C-terminal kinase domain, and has highly conserved sequence characteristics in different mammals.

Species	Human	Mouse	Rat	Bovine
Molecular Weight (kDa)	155	153	154	155
Primary Structural Differences	Contains 1253 amino acids, two-domain architecture	The sequence similarity of PAS domains reaches 95%	Highly conservative kinase domain structure	Structure of domain and human are basically identical

The PAS domain of the PASK protein is responsible for sensing the cell's energy state, while the kinase domain performs phosphorylation functions. The two domains regulate each other through allosteric mechanisms: after the PAS domain senses changes in metabolites, it induces conformational changes in kinases, thereby regulating their catalytic activity. This unique dual-domain architecture enables PASK to precisely coordinate cellular metabolism and energy balance, playing a core role in glucose sensing and mitochondrial function regulation.

Fig. 1 The crystal structure of the PAS domain of PASK.¹

Key structural properties of PASK:

Unique dual-domain architecture (PAS sensing domain and kinase catalytic domain)
PAS structure domain as a sensing module of intracellular metabolites
Kinase domains perform substrate phosphorylation functions
Allosteric regulatory mechanisms between dual domains control kinase activity

Functions of PASK

The core function of the PASK gene is to serve as a sensor for the energy state of cells. However, it is also widely involved in the regulation of various physiological processes, including metabolic adaptation, autophagy and developmental regulation.

Function	Description
Energy perception	The PAS domain senses the changes in the levels of metabolites such as NADPH and ATP within cells to respond to nutritional availability.
Metabolic regulation	Phosphorylates downstream targets and regulates metabolic pathways such as glycogen synthesis, glucose uptake and mitochondrial biosynthesis.
Adaptation to hypoxia	Regulating gene expression under hypoxic conditions helps cells adapt to energy stress states and maintain metabolic homeostasis.
Autophagy regulation	Through the interaction of pathways such as mTOR, it affects the autophagy process of cells, coordinates energy balance and eliminates damaged components.
Developmental support	Regulate cell differentiation and tissue construction at specific stages of embryonic development to ensure energy supply and signal integration during the development process.

The activity of PASK is strictly controlled by its dual-domain allosteric regulatory mechanism: after the PAS domain senses metabolic signals, it induces conformational changes in the kinase domain, thereby precisely initiating or inhibiting its phosphorylation function. This unique regulatory mode enables PASK to effectively integrate multiple nutritional signals and play a core role in maintaining metabolic homeostasis.

Applications of PASK and PASK Antibody in Literature

1. Zhang, Dan-dan, et al. "Per-Arnt-Sim Kinase (PASK): An emerging regulator of mammalian glucose and lipid metabolism." Nutrients 7.9 (2015): 7437-7450. https://doi.org/10.3390/nu7095347

The article indicates that the nutrition-sensing kinase PASK regulates glycolipid metabolism. Inhibiting PASK can improve obesity and insulin resistance caused by a high-fat diet, making it a potential new therapeutic target for metabolic syndrome.

2. Hurtado-Carneiro, Verónica, et al. "Preventing oxidative stress in the liver: an opportunity for glp-1 and/or pask." Antioxidants 10.12 (2021): 2028. https://doi.org/10.3390/antiox10122028

The article indicates that research has found that inhibiting PASK can improve metabolic abnormalities caused by high-fat diets by regulating signals such as AMPK/mTOR, and work in synergy with GLP-1 to alleviate liver oxidative stress.

3. Xiao, Michael, et al. "PASK links cellular energy metabolism with a mitotic self-renewal network to establish differentiation competence." Elife 12 (2023): e81717. https://doi.org/10.7554/eLife.81717

Research has found that stem cells activate PASK through glutamine metabolism and promote its entry into the nucleus, thereby inhibiting the self-renewal factor Pax7, generating heterogeneity and initiating differentiation, and driving muscle regeneration.

4. Kikani, Chintan K., et al. "Pask integrates hormonal signaling with histone modification via Wdr5 phosphorylation to drive myogenesis." Elife 5 (2016): e17985. https://doi.org/10.7554/eLife.17985

The article indicates that PASK converts the inhibitory histone marker H3K4me1 into the activating H3K4me3 by phosphorylating Wdr5, thereby opening up the expression of differentiation genes (such as sarcoplasmin) and initiating cell differentiation.

5. Pérez-García, Ana, et al. "Storage and utilization of glycogen by mouse liver during adaptation to nutritional changes are GLP-1 and PASK dependent." Nutrients 13.8 (2021): 2552. https://doi.org/10.3390/nu13082552

Research has found that Exendin-4 (a GLP-1 analogue) inhibits PASK by simulating the fasting effect, alters the balance of metabolic enzymes in the liver, and leads to abnormal accumulation of glycogen in the liver even in a fasting state.

Creative Biolabs: PASK Antibodies for Research

Creative Biolabs specializes in the production of high-quality PASK antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

Custom PASK Antibody Development: Tailor-made solutions to meet specific research requirements.
Bulk Production: Large-scale antibody manufacturing for industry partners.
Technical Support: Expert consultation for protocol optimization and troubleshooting.
Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our PASK antibodies, custom preparations, or technical support, contact us at email.

Reference

Zhang, Dan-dan, et al. "Per-Arnt-Sim Kinase (PASK): An emerging regulator of mammalian glucose and lipid metabolism." Nutrients 7.9 (2015): 7437-7450. https://doi.org/10.3390/nu7095347