AGL Antikörper (AA 357-387)

Produktnummer ABIN1882062

Dieses Anti-AGL-Antikörper ist ein Kaninchen Polyklonal-Antikörper zur Detektion von AGL in WB und IF. Geeignet für Human. Dieses Primary Antibody wurde in 10+ Publikationen zitiert.

Kurzübersicht für AGL Antikörper (AA 357-387) (ABIN1882062)

Target: AGL (Amylo-alpha-1, 6-Glucosidase, 4-alpha-Glucanotransferase (AGL))

Reaktivität: Human

Wirt: Kaninchen

Klonalität: Polyklonal

Konjugat: Dieser AGL Antikörper ist unkonjugiert

Applikation: Western Blotting (WB), Immunofluorescence (IF)

Klon: RB4976

Produktdetails anti-AGL Antikörper

Bindungsspezifität: AA 357-387

Aufreinigung: 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 357-387 amino acids from the Central region of human AGL.

Isotyp: Ig Fraction

Anwendungsinformationen

Applikationshinweise: IF: 1:10~50. WB: 1:1000

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Format: Liquid

Buffer: Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.

Konservierungsmittel: Sodium azide

Vorsichtsmaßnahmen: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Lagerung: 4 °C,-20 °C

Haltbarkeit: 6 months

Referenzen für anti-AGL Antikörper (ABIN1882062)

Irimia, Tagliabracci, Meyer, Segvich, DePaoli-Roach, Roach: "Muscle glycogen remodeling and glycogen phosphate metabolism following exhaustive exercise of wild type and laforin knockout mice." in: The Journal of biological chemistry, (2015) (PubMed).

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).

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).

Tagliabracci, Girard, Segvich, Meyer, Turnbull, Zhao, Minassian, Depaoli-Roach, Roach: "Abnormal metabolism of glycogen phosphate as a cause for Lafora disease." in: The Journal of biological chemistry, Vol. 283, Issue 49, pp. 33816-25, (2008) (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).

Horinishi, Okubo, Tang, Hui, To, Mabuchi, Okada, Mabuchi, Murase: "Mutational and haplotype analysis of AGL in patients with glycogen storage disease type III." in: Journal of human genetics, Vol. 47, Issue 2, pp. 55-9, (2002) (PubMed).

Bao, Dawson, Chen: "Human glycogen debranching enzyme gene (AGL): complete structural organization and characterization of the 5' flanking region." in: Genomics, Vol. 38, Issue 2, pp. 155-65, (1997) (PubMed).

Hansen, Lundin, Markussen, Thorsby: "T cell receptor usage by HLA-DQw8-specific T cell clones." in: International immunology, Vol. 4, Issue 8, pp. 931-4, (1992) (PubMed).

Yang, Ding, Enghild, Bao, Chen: "Molecular cloning and nucleotide sequence of cDNA encoding human muscle glycogen debranching enzyme." in: The Journal of biological chemistry, Vol. 267, Issue 13, pp. 9294-9, (1992) (PubMed).

Details zu AGL

Target: AGL (Amylo-alpha-1, 6-Glucosidase, 4-alpha-Glucanotransferase (AGL))

Andere Bezeichnung: AGL

Hintergrund: 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.

Molekulargewicht: 174764

NCBI Accession: NP_000019, NP_000633, NP_000634, NP_000635, NP_000636, NP_000637

UniProt: P35573

Pathways: Cellular Glucan Metabolic Process