GDE / AGL | Glycogen debranching enzyme
AS09 454 | clonality:polyclonal | host:rabbit | reactivity:human, mouse, rabbit, rat
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|Recommended dilution||5 ĩg (IP), 1 : 2000 (WB)|
|Expected | apparent MW||
|Confirmed reactivity||Human, Mouse, Rabbit,Rat|
|Not reactive in||No confirmed exceptions from predicted reactivity are currently known.|
|Additional information||Samples used to test this antibody were: muscle and liver homogenates, purified glycogen. This antiboy will recogize glycogen phosphorylase from both liver and muscle. It has been used in ICC on human primary myotubes.|
|Selected references||Oldenburg et al. (2016). CD44 and RHAMM are essential for rapid growth of bladder cancer driven by loss of Glycogen Debranching Enzyme (AGL). BMC Cancer. 2016 Sep 5;16:713. doi: 10.1186/s12885-016-2756-5.
Pagliarani et al. (2014). Glycogen storage disease type III: A novel Agl knockout mouse model. Biochim Biophys Acta. 2014 Aug 1. pii: S0925-4439(14)00250-6. doi: 10.1016/j.bbadis.2014.07.029.
(1) rat liver homogenate (50 µg of total protein), (2) GDE IP from 500 µg rat liver homogenate (3) GDE IP from 10 µg purified rat liver glycogen (see Parker et al, BBRC 2007) were resuspended into SDS PAGE sample buffer, boiled, electrophoresed on a pre-cast 4-15% gradient gel (Invitrogen, CA, USA) and transferred to PVDF membrane. Following blocking in 5% milk / PBST, membranes were probed with GDE antibodies (diluted 1/2000) for 1h at room temperature with rocking, followed by washing in 3 times for 5 min in PBS-T at room temperature with agitation. Blots were incubated in secondary antibody (Protein-G coupled to horse radish peroxidase conjugated – Bio-Rad) diluted 1:3000 for 1h at room temperature with agitation. The blots were washed as above and developed for 5 min with ECL (Invitrogen, CA, USA). Images were detected using the Fuji LAS-3000 system.
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