ACSL1 Antibody
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Product Specs
Buffer
PBS with 0.1% Sodium Azide, 50% Glycerol, pH 7.3. Store at -20°C. Avoid freeze-thaw cycles.
Lead Time
Typically, we can ship products within 1-3 business days of receiving your order. Delivery time may vary depending on the purchasing method or location. For specific delivery information, please consult your local distributors.
Synonyms
ACSL1; FACL1; FACL2; LACS; LACS1; LACS2; Long-chain-fatty-acid--CoA ligase 1; Acyl-CoA synthetase 1; ACS1; Arachidonate--CoA ligase; Long-chain acyl-CoA synthetase 1; LACS 1; Long-chain acyl-CoA synthetase 2; LACS 2; Long-chain fatty acid-CoA ligase 2; Palmitoyl-CoA ligase 1; Palmitoyl-CoA ligase 2; Phytanate--CoA ligase
Target Names
Uniprot No.
Target Background
Function
ACSL1 catalyzes the conversion of long-chain fatty acids into their active form, acyl-CoAs. This process is crucial for both the synthesis of cellular lipids and their degradation via beta-oxidation. ACSL1 exhibits a preference for palmitoleate, oleate, and linoleate as substrates. Notably, it activates arachidonate more effectively than epoxyeicosatrienoic acids (EETs) or hydroxyeicosatrienoic acids (HETEs).
Gene References Into Functions
- Research suggests that the expression of ACSL1, ACSL4, and ACSL5 is regulated by ER signaling pathways. Moreover, ACSL5 has emerged as a potential novel biomarker for predicting the prognosis of breast cancer patients. PMID: 28498416
- A study identified a genetic variant in the 3'-UTR region of the ACSL1 gene (rs8086) that may significantly influence the outcomes of stage II/III colon cancer patients. Specifically, patients with the T/T genotype exhibited a significantly higher risk of tumor recurrence compared to those carrying at least one C allele. PMID: 27992526
- The mRNA levels of ACSL1 were found to be positively associated with those of HBXIP in clinical breast cancer tissues. This suggests that the oncoprotein HBXIP can up-regulate ACSL1 by activating the transcription factor Sp1 in breast cancer. PMID: 28132807
- Evidence in humans indicates that ACSL1 SNPs are associated with fasting glucose, diabetes, and subclinical atherosclerosis. PMID: 26711138
- The SRE motif in ACSL1 plays a crucial role in SREBP2-mediated activation of C-ACSL1 gene transcription. PMID: 26728456
- ACSL1 serves as a programmable mediator of insulin sensitivity and cellular lipid content. PMID: 25915184
- The cell surface protein CD36/FAT directly facilitates fatty acid transport across the plasma membrane, while the intracellular acyl-CoA synthetases FATP4 and ACSL1 indirectly enhance fatty acid uptake through metabolic trapping. PMID: 24503477
- Data indicate that the expression of miR-205 is negatively correlated with that of ACSL1 in clinical hepatocellular carcinoma (HCC) tissues. PMID: 24462768
- Long-chain acyl-CoA synthetase 1 (ACSL1) plays a role in the suppression of palmitate-induced cytokine production by eicosapentaenoic acid. PMID: 23433401
- Findings suggest that the ACSL1 gene polymorphism rs6552828 is not associated with elite endurance athletic status in Caucasians. However, a marginal association appears to exist for the Chinese (Han) male population. PMID: 22829935
- Data show that the ACSL1 rs9997745 polymorphism influences metabolic syndrome risk, potentially through disruptions in fatty acid metabolism. This effect is modulated by dietary fat consumption, particularly PUFA intake, suggesting novel gene-nutrient interactions. PMID: 20176858
- Based on homology, two new isoforms for ACSL1 were predicted and characterized. One isoform represents a switch of the Phe- to the Tyr-Gate domain motif, while the other results from the exclusion of both motifs. PMID: 16834775
Database Links
Protein Families
ATP-dependent AMP-binding enzyme family
Subcellular Location
Mitochondrion outer membrane; Single-pass type III membrane protein. Peroxisome membrane; Single-pass type III membrane protein. Microsome membrane; Single-pass type III membrane protein. Endoplasmic reticulum membrane; Single-pass type III membrane protein.
Tissue Specificity
Highly expressed in liver, heart, skeletal muscle, kidney and erythroid cells, and to a lesser extent in brain, lung, placenta and pancreas.
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