Antibody data
- Antibody Data
- Antigen structure
- References [6]
- Comments [0]
- Validations [0]
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- Product number
- ABIN361883 - Provider product page
- Provider
- antibodies-online
- Proper citation
- Antibodies-Online Cat#ABIN361883, RRID:AB_10953112
- Product name
- anti-V-Raf-1 Murine Leukemia Viral Oncogene Homolog 1 (RAF1) (pSer259) antibody
- Antibody type
- Polyclonal
- Antigen
- Peptide sequence around phosphorylation site of pSer259 (S-T-S (p) -T-P) derived from Human Raf1. Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates.
- Description
- The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatogramphy using non-phosphopeptide corresponding to the phosphorylation site.
- Reactivity
- Human, Mouse, Rat
- Host
- Rabbit
- Epitope
- pSer259
- Isotype
- IgG
- Vial size
- 50 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 Prognostic impact of Raf-1 and p-Raf-1 expressions for poor survival rate in non-small cell lung cancer.
Regulation of Raf-1 by direct feedback phosphorylation.
Novel C-Raf phosphorylation sites: serine 296 and 301 participate in Raf regulation.
Positive and negative regulation of Raf kinase activity and function by phosphorylation.
The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338.
Molecular imprinting.
Qiu ZX, Wang L, Han J, Liu D, Huang W, Altaf K, Qiu XS, Javed MA, Zheng J, Chen BJ, Li WM
Cancer science 2012 Oct;103(10):1774-9
Cancer science 2012 Oct;103(10):1774-9
Regulation of Raf-1 by direct feedback phosphorylation.
Dougherty MK, Müller J, Ritt DA, Zhou M, Zhou XZ, Copeland TD, Conrads TP, Veenstra TD, Lu KP, Morrison DK
Molecular cell 2005 Jan 21;17(2):215-24
Molecular cell 2005 Jan 21;17(2):215-24
Novel C-Raf phosphorylation sites: serine 296 and 301 participate in Raf regulation.
Hekman M, Fischer A, Wennogle LP, Wang YK, Campbell SL, Rapp UR
FEBS letters 2005 Jan 17;579(2):464-8
FEBS letters 2005 Jan 17;579(2):464-8
Positive and negative regulation of Raf kinase activity and function by phosphorylation.
Chong H, Lee J, Guan KL
The EMBO journal 2001 Jul 16;20(14):3716-27
The EMBO journal 2001 Jul 16;20(14):3716-27
The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338.
King AJ, Sun H, Diaz B, Barnard D, Miao W, Bagrodia S, Marshall MS
Nature 1998 Nov 12;396(6707):180-3
Nature 1998 Nov 12;396(6707):180-3
Molecular imprinting.
Mosbach K
Trends in biochemical sciences 1994 Jan;19(1):9-14
Trends in biochemical sciences 1994 Jan;19(1):9-14
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