Phospho-Smad1 (Ser463/465)/ Smad5 (Ser463/465)/ Smad9 (Ser465/467) Antibody #9511
We recommend the following alternatives
- WB
- IP
- ChIP
Inquiry Info. # 9511
Please see our recommended alternatives.
Supporting Data
| REACTIVITY | H M R Mi |
| SENSITIVITY | Endogenous |
| MW (kDa) | 60 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- ChIP-Chromatin Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mi-Mink
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
| Chromatin IP | 1:50 |
Storage
Protocol
Specificity / Sensitivity
Phospho-Smad1 (Ser463/465)/Smad5 (Ser463/465)/Smad9 (Ser465/467) Antibody detects endogenous levels of Smad1 only when phosphorylated at serine 463 and serine 465, as well as Smad5 and Smad9 (Smad8) only when phosphorylated at the equivalent sites. The antibody does not cross-react with other Smad-related proteins.
Species Reactivity:
Human, Mouse, Rat, Mink
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser463/465 of human Smad5. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Bone morphogenetic proteins (BMPs) constitute a large family of signaling molecules that regulate a wide range of critical processes including morphogenesis, cell-fate determination, proliferation, differentiation, and apoptosis (1,2). BMP receptors are members of the TGF-β superfamily of Ser/Thr kinase receptors. Ligand binding induces multimerization, autophosphorylation, and activation of these receptors (3-5). They subsequently phosphorylate SMAD1 at Ser463 and Ser465 in the carboxy-terminal motif SSXS, as well as SMAD5 and SMAD9 (SMAD8) at their corresponding sites. These phosphorylated SMADs dimerize with the coactivating SMAD4 and translocate to the nucleus, where they regulate the transcription of target genes (5). MAP kinases and CDKs 8 and 9 are also reported to phosphorylate residues in the linker region of SMAD1, including Ser206. Phosphorylation of SMAD1 at Ser206 recruits Smurf1 to the linker region and leads to the degradation of SMAD1 (6). Phosphorylation at this site also promotes SMAD1 transcriptional activity by recruiting YAP to the linker region (7).
- Hogan, B.L. (1996) Genes Dev 10, 1580-94.
- Hoodless, P.A. et al. (1996) Cell 85, 489-500.
- Klemm, J.D. et al. (1998) Annu Rev Immunol 16, 569-92.
- Kretzschmar, M. et al. (1997) Genes Dev 11, 984-95.
- Whitman, M. (1998) Genes Dev 12, 2445-62.
- Sapkota, G. et al. (2007) Mol Cell 25, 441-54.
- Alarcón, C. et al. (2009) Cell 139, 757-69.
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