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ACOX1 Protein, Mouse, Recombinant (Myc)
Catalog No. TMPH-02825
Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. First enzyme of the fatty acid beta-oxidation pathway.; Shows highest activity against medium-chain fatty acyl-CoAs and activity decreases with increasing chain length.; Is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs. Is twice as active as isoform 1 against 16-hydroxy-palmitoyl-CoA and is 25% more active against 1,16-hexadecanodioyl-CoA.
ACOX1 Protein, Mouse, Recombinant (Myc)
Catalog No. TMPH-02825
Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. First enzyme of the fatty acid beta-oxidation pathway.; Shows highest activity against medium-chain fatty acyl-CoAs and activity decreases with increasing chain length.; Is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs. Is twice as active as isoform 1 against 16-hydroxy-palmitoyl-CoA and is 25% more active against 1,16-hexadecanodioyl-CoA.
| Pack Size | Price | Availability | Quantity |
|---|---|---|---|
| 20 μg | $360 | 20 days | |
| 100 μg | $678 | 20 days | |
| 1 mg | $2,300 | 20 days |
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| Biological Activity | Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first. |
| Description | Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. First enzyme of the fatty acid beta-oxidation pathway.; Shows highest activity against medium-chain fatty acyl-CoAs and activity decreases with increasing chain length.; Is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs. Is twice as active as isoform 1 against 16-hydroxy-palmitoyl-CoA and is 25% more active against 1,16-hexadecanodioyl-CoA. |
| Species | Mouse |
| Expression System | E. coli |
| Tag | C-Myc |
| Accession Number | Q9R0H0 |
| Synonyms | Straight-chain acyl-CoA oxidase,Peroxisomal fatty acyl-CoA oxidase,Peroxisomal acyl-coenzyme A oxidase 1,Palmitoyl-CoA oxidase,EC:1.3.3.6,AOX |
| Amino Acid | MNPDLRKERAAATFNPELITHILDGSPENTRRRREIENLILNDPDFQHEDYNFLTRSQRYEVAVKKSATMVKKMREFGIADPEEIMWFKKLHMVNFVEPVGLNYSMFIPTLLNQGTTAQQEKWMHPSQELQIIGTYAQTEMGHGTHLRGLETTATYDPKTQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITRGECYGLHAFVVPIREIGTHKPLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFVRSFLVGSAAQSLSKACTIAIRYSAVRRQSEIKRSEPEPQILDFQTQQYKLFPLLATAYAFHFLGRYIKETYMRINESIGQGDLSELPELHALTAGLKAFTTWTANAGIEECRMACGGHGYSHSSGIPNIYVTFTPACTFEGENTVMMLQTARFLMKIYDQVQSGKLVGGMVSYLNDLPSQRIQPQQVAVWPTLVDINSLDSLTEAYKLRAARLVEIAAKNLQAQVSHRKSKEVAWNLTSVDLVRASEAHCHYVTVKVFADKLPKIQDRAVQAVLRNLCLLYSLYGISQKGGDFLEGNIITGAQMSQVNSRILELLTVTRPNAVALVDAFDFKDVTLGSVLGRYDGNVYENLFEWAKKSPLNKTEVHESYYKHLKPLQSKL |
| Construction | 1-661 aa |
| Protein Purity | > 85% as determined by SDS-PAGE. |
| Molecular Weight | 76.2 kDa (predicted) |
| Formulation | Tris-based buffer, 50% glycerol |
| Reconstitution | A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information. |
| Stability & Storage | Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots. |
| Shipping | In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice. |
| Research Background | Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. First enzyme of the fatty acid beta-oxidation pathway.; Shows highest activity against medium-chain fatty acyl-CoAs and activity decreases with increasing chain length.; Is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs. Is twice as active as isoform 1 against 16-hydroxy-palmitoyl-CoA and is 25% more active against 1,16-hexadecanodioyl-CoA. |
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