Application
Dot blot analysis of Phospho-RAF1-S296 Pab (Cat.AP3291a) on nitrocellulose membrane. Dot blot analysis of Phospho-RAC1-S71 Pab (Cat.AP3290a) on nitrocellulose membrane. 50ng of Phospho-peptide or Non Phospho-peptide per dot were adsorbed. Antibodies working concentration was 0.5ug per ml.| Product Name | Phospho-RAF1-S296 Antibody |
|---|---|
| Antibody Type | Primary Antibodies |
| Antigen Alias | RAF1; RAF; RAF proto-oncogene serine/threonine-protein kinase; Proto-oncogene c-RAF; Raf-1 |
| Modification | p-S296 |
| Clonality | Polyclonal |
|---|---|
| Isotype | Ig |
| Host Species | Rabbit |
| Tested Applications | DB |
| DB:1:500 |
|
| Species Reactivity | Human |
| Concentration | 1mg/ml |
| Gene Synonyms | RAF |
|---|---|
| Alternative Names | RAF1 RAF RAF proto-oncogene serine/threonine-protein kinase Proto-oncogene c-RAF Raf-1 |
| Molecular Weight(MW) | 73052 Da |
| Function | Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2- antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation |
| Tissue Specificity | In skeletal muscle, isoform 1 is more abundant than isoform 2 |
| Cellular Localization | Cytoplasm. Cell membrane. Mitochondrion. Nucleus. Note=Colocalizes with RGS14 and BRAF in both the cytoplasm and membranes. Phosphorylation at Ser-259 impairs its membrane accumulation. Recruited to the cell membrane by the active Ras protein. Phosphorylation at Ser-338 and Ser-339 by PAK1 is required for its mitochondrial localization. Retinoic acid- induced Ser-621 phosphorylated form of RAF1 is predominantly localized at the nucleus |
| Entrez Gene | 5894 |
|---|
Application
Dot blot analysis of Phospho-RAF1-S296 Pab (Cat.AP3291a) on nitrocellulose membrane. Dot blot analysis of Phospho-RAC1-S71 Pab (Cat.AP3290a) on nitrocellulose membrane. 50ng of Phospho-peptide or Non Phospho-peptide per dot were adsorbed. Antibodies working concentration was 0.5ug per ml.| Application Notes | DB:1:500 |
|---|
| Form | Liquid |
|---|---|
| Storage Instructions | For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles. |
| Storage Buffer | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is first purified by protein A affinity chromatography. Then, the antibody fraction is peptide affinity purified in a 2-step procedure with peptides. The antibody is eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS. |
