There are 6+ publications for this product available. The Rabbit Polyclonal anti-AGL antibody has been validated for WB and IF. It is suitable to detect AGL in samples from Human.
This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
Immunogen
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
Reactivity: Human
WB, IF, EIA
Host: Rabbit
Polyclonal
unconjugated
Application Notes
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.
Preservative
Sodium azide
Precaution of Use
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
4 °C,-20 °C
Storage Comment
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.
Expiry Date
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." in: 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." in: 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." in: 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." in: 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." in: 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." in: 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.