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ACADL Antibody (N-term)

Affinity Purified Rabbit Polyclonal Antibody (Pab)

     
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  • 1 - ACADL Antibody (N-term) AP13134a
    Western blot analysis of lysates from HepG2 cell line and mouse kidney, rat spleen tissue lysates(from left to right), using ACADL Antibody (N-term)(Cat. #AP13134a). AP13134a was diluted at 1:1000 at each lane. A goat anti-rabbit IgG H&L(HRP) at 1:5000 dilution was used as the secondary antibody. Lysates at 35ug per lane.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession P28330
Other Accession NP_001599.1
Reactivity Human, Rat, Mouse
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 47656 Da
Antigen Region 14-43 aa
Additional Information
Gene ID 33
Other Names Long-chain specific acyl-CoA dehydrogenase, mitochondrial, LCAD, ACADL
Target/Specificity This ACADL antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 14-43 amino acids from the N-terminal region of human ACADL.
Dilution WB~~1:1000
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsACADL Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name ACADL (HGNC:88)
Function Long-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation (FAO), breaking down fatty acids into acetyl- CoA and allowing the production of energy from fats (PubMed:17564966, PubMed:24591516, PubMed:32389575). The first step of FAO consists in the proR-proR stereospecific alpha, beta-dehydrogenation of fatty acyl- CoA thioesters using the electron transfer flavoprotein (ETF) as their physiologic electron acceptor, resulting in the formation of trans-2- enoyl-CoA ((2E)-enoyl-CoA) (PubMed:17564966, PubMed:21237683). Among the different mitochondrial acyl-CoA dehydrogenases, long-chain specific acyl-CoA dehydrogenase activity overlaps with that of ACADV and ACAD9, acting on saturated and unsaturated acyl-CoAs with 6 to 24 carbons with a preference for 8 to 18 carbons long primary chains (PubMed:17564966, PubMed:21237683, PubMed:8823175). Plays a primary role in FAO in tissues where it is the main long-chain ACAD expressed, such as the lung, specifically in type 2 alveolar cells (responsible for surfactant production) (PubMed:17564966, PubMed:24591516). Probably responsible for beta-oxidation of bulky substrates including branched chain fatty acyl-CoAs and sterol derivatives thanks to its enlarged substrate-binding cavity (PubMed:38839792).
Cellular Location Mitochondrion matrix {ECO:0000250|UniProtKB:P15650}
Tissue Location Expressed at mRNA and protein levels in lungs, where it localizes specifically in alveolar epithelial cells (alveolar type II pneumocytes) (PubMed:17564966, PubMed:24591516). Also expressed at mRNA levels in prostate, thyroid gland, kidney, heart and muscle (PubMed:17564966).
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

The protein encoded by this gene belongs to the acyl-CoA dehydrogenase family, which is a family of mitochondrial flavoenzymes involved in fatty acid and branched chain amino-acid metabolism. This protein is one of the four enzymes that catalyze the initial step of mitochondrial beta-oxidation of straight-chain fatty acid. Defects in this gene are the cause of long-chain acyl-CoA dehydrogenase (LCAD) deficiency, leading to nonketotic hypoglycemia.

REFERENCES

Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)
Maher, A.C., et al. Mol. Genet. Metab. 100(2):163-167(2010)
Illig, T., et al. Nat. Genet. 42(2):137-141(2010)
Talmud, P.J., et al. Am. J. Hum. Genet. 85(5):628-642(2009)
Lu, Y., et al. J. Lipid Res. 49(12):2582-2589(2008)

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