Antibody data
- Antibody Data
- Antigen structure
- References [4]
- Comments [0]
- Validations [0]
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- Product number
- ABIN361882 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Pyruvate Dehydrogenase Kinase, Isozyme 1 (PDK1) (pSer241) antibody
- Antibody type
- Polyclonal
- Antigen
- Peptide sequence around phosphorylation site of pSer241 (A-N-S (p) -F-V) derived from Human PDK1. Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates.
- Description
- The antibody was affinity-purified from rabbit antiserum by affinity-chromatography usingepitope-specific phosphopeptide. The antibody against non-phosphopeptide was removedby chromatogramphy using non-phosphopeptide corresponding to the phosphorylation site.
- Reactivity
- Human, Mouse, Rat
- Host
- Rabbit
- Epitope
- pSer241
- Isotype
- IgG
- Vial size
- 100 μL
- Concentration
- 1 mg/mL
- Storage
- Store at -20°C for long term preservation (recommended). Store at 4°C for short term use.
Submitted references Phosphoinositide-dependent phosphorylation of PDK1 regulates nuclear translocation.
Nuclear translocation of 3'-phosphoinositide-dependent protein kinase 1 (PDK-1): a potential regulatory mechanism for PDK-1 function.
Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3.
Insulin stimulates increased catalytic activity of phosphoinositide-dependent kinase-1 by a phosphorylation-dependent mechanism.
Scheid MP, Parsons M, Woodgett JR
Molecular and cellular biology 2005 Mar;25(6):2347-63
Molecular and cellular biology 2005 Mar;25(6):2347-63
Nuclear translocation of 3'-phosphoinositide-dependent protein kinase 1 (PDK-1): a potential regulatory mechanism for PDK-1 function.
Lim MA, Kikani CK, Wick MJ, Dong LQ
Proceedings of the National Academy of Sciences of the United States of America 2003 Nov 25;100(24):14006-11
Proceedings of the National Academy of Sciences of the United States of America 2003 Nov 25;100(24):14006-11
Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3.
Sato S, Fujita N, Tsuruo T
The Journal of biological chemistry 2002 Oct 18;277(42):39360-7
The Journal of biological chemistry 2002 Oct 18;277(42):39360-7
Insulin stimulates increased catalytic activity of phosphoinositide-dependent kinase-1 by a phosphorylation-dependent mechanism.
Chen H, Nystrom FH, Dong LQ, Li Y, Song S, Liu F, Quon MJ
Biochemistry 2001 Oct 2;40(39):11851-9
Biochemistry 2001 Oct 2;40(39):11851-9
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