Il existe 6+ publications pour ce produit.
L’anticorps anti-AGL Polyclonal Lapin est utilisé pour la détection de AGL dans des échantillons de Humain. Il a été validé pour WB et IF.
This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
Immunogène
This AGL antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1479-1510 amino acids from the C-terminal region of human AGL.
AGL
Reactivité: Humain
WB, IHC, ICC, IP
Hôte: Lapin
Polyclonal
unconjugated
Indications d'application
IF: 1:10~50. IF: 1:10~50. WB: 1:1000. WB: 1:8000
Restrictions
For Research Use only
Format
Liquid
Buffer
Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
Agent conservateur
Sodium azide
Précaution d'utilisation
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Stock
4 °C,-20 °C
Stockage commentaire
Maintain refrigerated at 2-8 °C for up to 6 months. For long term storage store at -20 °C in small aliquots to prevent freeze-thaw cycles.
Date de péremption
6 months
Guin, Ru, Agarwal, Ritterson Lew, Owens, Comi, Theodorescu: "Loss of glycogen debranching enzyme AGL drives bladder tumor growth via induction of hyaluronic acid synthesis." dans: Clinical cancer research : an official journal of the American Association for Cancer Research, (2015) (PubMed).
Liu, Zeng, Ma, Baba, Zheng, Liu, Wang: "Laforin-malin complex degrades polyglucosan bodies in concert with glycogen debranching enzyme and brain isoform glycogen phosphorylase." dans: Molecular neurobiology, Vol. 49, Issue 2, pp. 645-57, (2014) (PubMed).
Zhu, Shen, Zhu, Coorey, Nguyen, Barthelmes, Gillies: "Anti-retinal antibodies in patients with macular telangiectasia type 2." dans: Investigative ophthalmology & visual science, Vol. 54, Issue 8, pp. 5675-83, (2013) (PubMed).
DePaoli-Roach, Tagliabracci, Segvich, Meyer, Irimia, Roach: "Genetic depletion of the malin E3 ubiquitin ligase in mice leads to lafora bodies and the accumulation of insoluble laforin." dans: The Journal of biological chemistry, Vol. 285, Issue 33, pp. 25372-81, (2010) (PubMed).
Parker, Kong, Walsh, Salajegheh, Moghadaszadeh, Amato, Nazareno, Lin, Krastins, Sarracino, Beggs, Pinkus, Greenberg: "Fast-twitch sarcomeric and glycolytic enzyme protein loss in inclusion body myositis." dans: Muscle & nerve, Vol. 39, Issue 6, pp. 739-53, (2009) (PubMed).
Cheng, Zhang, Gentry, Worby, Dixon, Saltiel: "A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's disease." dans: Genes & development, Vol. 21, Issue 19, pp. 2399-409, (2007) (PubMed).
AGL is a glycogen debrancher enzyme which is involved in glycogen degradation. This enzyme has two independent catalytic activities which occur at different sites on the protein: a 4-alpha-glucotransferase activity and a amylo-1,6-glucosidase activity. Mutations in the AGL gene are associated with glycogen storage disease although a wide range of enzymatic and clinical variability occurs which may be due to tissue-specific alternative splicing.