ACOX1 Antibody (YA10065)
(Synonyms: ACOX, ACOX1, Peroxisomal acyl-coenzyme A oxidase 1, AOX, Palmitoyl-CoA oxidase, Peroxisomal fatty acyl-CoA oxidase, Straight-chain acyl-CoA oxidase, SCOX)ACOX1 Antibody (YA10065) is a Mouse-derived and non-conjugated IgG1 Monoclonal antibody, targeting to ACOX1.
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Host:
Mouse
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Isotype:
IgG
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Application:
WB, IHC-P, ICC/IF
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Reactivity :
Human
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Formulation:
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% sodium azide.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
|---|---|---|---|
| Dilution Ratio | 1:1000-2000 | 1:100-200 | 1:10-50 |
Product Details
ACOX1 Antibody (YA10065) is a Mouse-derived and non-conjugated IgG1 Monoclonal antibody, targeting to ACOX1.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman
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Observed Molecular WeightObserved band size: 74 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 74 kDa
Purified recombinant protein of human ACOX1.
Endogenous
affinity purified.
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% sodium azide.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
ACOX1 is involved in the initial and rate-limiting step of peroxisomal beta-oxidation of straight-chain saturated and unsaturated very-long-chain fatty acids (VLCFAs). Catalyzes the desaturation of fatty acyl-CoAs that have a saturated bond between C2 and C3 (2,3-saturated acyl-CoA) to 2-trans-enoyl-CoAs ((2E)-enoyl-CoAs), and donates electrons directly to molecular oxygen (O(2)), thereby producing hydrogen peroxide (H(2)O(2)). May play a role in peroxisomal beta-oxidation step in polyunsaturated fatty acids (PUFAs) biosynthesis. Possibly regulates systemic levels of docosahexaenoic acid (DHA, C22:6n-3) through a process involving endoplasmic reticulum desaturation and elongation of alpha-linolenic acid (ALA, C18:3n-3) to form tetracosahexaenoic acid (THA, C24:6n-3), which is then beta-oxidized to DHA in peroxisomes (Probable). Involved in VLCFA-dependent hepatic-to-adipose tissue inter-organ signaling in response to diet. Through hepatic beta-oxidation of THA, may regulate THA systemic levels and THA-dependent activation of FFAR4 signaling in adipocytes, limiting adipose tissue thermogenesis (By similarity)[1][2][3][4][5][6].
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Subcellular Localization
Peroxisome
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Expression
Tissue_Specificity: Widely expressed with highest levels of isoform 1 and isoform 2 detected in testis. Isoform 1 is expressed at higher levels than isoform 2 in liver and kidney while isoform 2 levels are higher in brain, lung, muscle, white adipose tissue and testis. Levels are almost equal in heart. -
Isoforms & Post-Translational Modification
ACOX1 has 3 isoforms, Q15067-1: amino acid length is 660, molecular weight is 74424 Da (predicted); Q15067-2: amino acid length is 660, molecular weight is 74668 Da (predicted); Q15067-3: amino acid length is 622, molecular weight is 70136 Da (predicted).
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Subunit
Homodimer.
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SwissProt ID
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Synonyms
ACOX, ACOX1, Peroxisomal acyl-coenzyme A oxidase 1, AOX, Palmitoyl-CoA oxidase, Peroxisomal fatty acyl-CoA oxidase, Straight-chain acyl-CoA oxidase, SCOX
Documentation
References
[1]. Ferdinandusse S, et al. Identification of the peroxisomal beta-oxidation enzymes involved in the degradation of long-chain dicarboxylic acids. J Lipid Res. 2004 Jun;45(6):1104-11. [Content Brief]
[2]. Ferdinandusse S, et al. Clinical, biochemical, and mutational spectrum of peroxisomal acyl-coenzyme A oxidase deficiency. Hum Mutat. 2007 Sep;28(9):904-12. [Content Brief]
[3]. Oaxaca-Castillo D, et al. Biochemical characterization of two functional human liver acyl-CoA oxidase isoforms 1a and 1b encoded by a single gene. Biochem Biophys Res Commun. 2007 Aug 24;360(2):314-9. [Content Brief]
[4]. Chung HL, et al. Loss- or Gain-of-Function Mutations in ACOX1 Cause Axonal Loss via Different Mechanisms. Neuron. 2020 May 20;106(4):589-606.e6. [Content Brief]
[5]. Morita A, et al. Novel ACOX1 mutations in two siblings with peroxisomal acyl-CoA oxidase deficiency. Brain Dev. 2021 Mar;43(3):475-481. [Content Brief]
[6]. Chu R, et al. Overexpression and characterization of the human peroxisomal acyl-CoA oxidase in insect cells. J Biol Chem. 1995 Mar 3;270(9):4908-15. [Content Brief]
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