SAT1 Antibodies

Structure of SAT1

SAT1 is a protein with a molecular weight of approximately 38 kDa. There are slight differences in this molecular weight among different species, mainly due to minor changes in the amino acid sequence.

This protein is composed of approximately 170 amino acids and forms a typical acetyltransferase folding structure. The core structure of the SAT1 protein contains A highly conserved acetyl-CoA binding site, which fulfills its catalytic function through arginine and aspartic acid residues. Its tertiary structure forms a hydrophobic channel for binding polyamine substrates (such as spermidine and spermidine). The crucial histidine residue at position 136 serves as a catalytic base, directly participating in the acetyl group transfer reaction, while aspartic acid at position 100 is responsible for stabilizing the transition state intermediate.

Fig. 1 Association of SAT1 with ferroptosis, immunotherapy, and chemoradiotherapy.¹

Key structural properties of SAT1:

• Typical folded structure of acetyltransferase
• Conserved acetyl-CoA binding pocket
• Arginine and aspartic acid residues constitute the catalytic center
• Hydrophobic channels are responsible for specifically recognizing polyamine substrates (such as spermidine and spermidine)
• Key histidine residues (such as His136) act as catalytic bases to participate in acetyl transfer

Functions of SAT1

The main function of the SAT1 gene-encoded protein (spermidine/spermidine acetyltransferase) is to regulate the balance of polyamine metabolism within cells. In addition, it is widely involved in key physiological and pathological processes such as cell proliferation, apoptosis, oxidative stress response and immune regulation.

The acetylation reaction catalyzed by SAT1 significantly reduces the positive charge carried by polyamines, affecting their interactions with nucleic acids and proteins. This mechanism plays a crucial role in maintaining cellular homeostasis and responding to internal and external stimuli.

Applications of SAT1 and SAT1 Antibody in Literature

1. Murthy, Divya, et al. "Cancer-associated fibroblast-derived acetate promotes pancreatic cancer development by altering polyamine metabolism via the ACSS2–SP1–SAT1 axis." Nature cell biology 26.4 (2024): 613-627. https://doi.org/10.1038/s41556-024-01372-4

The article indicates that pancreatic cancer-related fibroblasts regulate tumor metabolism by secreting acetic acid. Among them, ACSS2-mediated exogenous acetic acid promotes the acetylation of the K19 site of the SP1 protein, enhancing its stability and transcriptional activity, thereby upregulating SAT1 expression, maintaining polyamine homeostasis, and promoting the survival of cancer cells in an acidic microenvironment. Inhibiting the ACSS2-SP1-SAT1 axis can reduce tumor burden.

2. Tian, Wenwen, et al. "Autophagy Deficiency Induced by SAT1 Potentiates Tumor Progression in Triple‐Negative Breast Cancer." Advanced Science 11.36 (2024): 2309903. https://doi.org/10.1002/advs.202309903

The article indicates that high expression of SAT1 in triple-negative breast cancer predicts a poor prognosis. JUN activates SAT1 through transcription. The SAT1 protein binds and stabilizes YBX1 through HERC5 deubiquitination. Subsequently, m5C modification is used to maintain the stability of mTOR and inhibit autophagy, promoting tumor progression. Targeting the SAT1/YBX1/mTOR axis may become a new therapeutic strategy.

3. Zheng, Cuimiao, et al. "A noncanonical role of SAT1 enables anchorage independence and peritoneal metastasis in ovarian cancer." Nature Communications 16.1 (2025): 3174. https://doi.org/10.1038/s41467-025-58525-8

The article indicates that SAT1 promotes peritoneal metastasis of ovarian cancer through non-classical functions. SAT1 is highly expressed in ascites tumor cells. It acquires nuclear acetyl-CoA through reduction-carboxylation and acetylates H3K27 to enhance the transcription of mitose-related genes, maintaining anchor-independent survival and inhibiting mitotic death. Inhibiting SAT1 can reduce the transfer burden.

4. Dang, Yini, et al. "FTH1-and SAT1-induced astrocytic ferroptosis is involved in Alzheimer's disease: evidence from single-cell transcriptomic analysis." Pharmaceuticals 15.10 (2022): 1177. https://doi.org/10.3390/ph15101177

The article indicates that through scRNA-seq analysis, it was found that SAT1 and FTH1 jointly serve as the hub genes of ferroptosis in astrocytes. Changes in their expression affect ferroptosis activity and are associated with emotional cognitive function impairment and serum iron concentration in AD mice, suggesting that SAT1 may be involved in the pathological process of AD.

5. Yang, Huihuang, et al. "SAT1/ALOX15 signaling pathway is involved in ferroptosis after skeletal muscle contusion." International Journal of Molecular Sciences 25.20 (2024): 11317. https://doi.org/10.3390/ijms252011317

The article indicates that SAT1 mediates ferroptosis by regulating the expression of ALOX15 after skeletal muscle contusion, promotes lipid peroxidation and affects the repair process. Inhibiting SAT1 can alleviate cell damage induced by iron overload and provide a new target for treatment.

Creative Biolabs: SAT1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality SAT1 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom SAT1 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 SAT1 antibodies, custom preparations, or technical support, contact us at email.