The RAF1 Polyclonal Antibody (PAC021464) is a valuable tool for researchers studying RAF1, a key molecule in the Ras signaling pathway involved in cell growth and differentiation. This antibody, generated in rabbits, exhibits high reactivity with human samples and is validated for use in Western blot applications. By binding specifically to the RAF1 protein, this antibody allows for the detection and analysis of RAF1 expression in a wide range of cell types, making it an excellent choice for studies in cancer research and signal transduction pathways.
RAF1 plays a crucial role in promoting cell proliferation and survival, making it a potential target for therapeutic interventions in cancer and other diseases characterized by dysregulated cell growth. By investigating the function of RAF1, researchers can gain insights into the molecular mechanisms underlying tumorigenesis and potentially identify novel targets for drug development. The RAF1 Polyclonal Antibody is a valuable tool for unraveling the complex roles of RAF1 in cell signaling and disease progression.
Antibody Name:
Raf1 Antibody (PACO21464)
Antibody SKU:
PACO21464
Size:
100ul
Host Species:
Rabbit
Tested Applications:
ELISA, WB
Recommended Dilutions:
ELISA:1:2000-1:10000, WB:1:500-1:1000
Species Reactivity:
Rat
Immunogen:
Peptide sequence around aa. 641-645(T-S-P-R-L ) derived from Rat Raf-1.
Form:
Liquid
Storage Buffer:
Supplied at 1.0mg/mL in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Purification Method:
Antibodies were produced by immunizing rabbits with synthetic peptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific peptide
Clonality:
Polyclonal
Isotype:
IgG
Conjugate:
Non-conjugated
Western blot analysis of extract from mouse brain tissue and C6 cells using Raf-1 Antibody.
Background:
A-Raf, B-Raf and c-Raf (Raf-1) are the main effectors recruited by GTP-bound Ras to activate the MEK-MAP kinase pathway (1). Activation of c-Raf is the best understood and involves phosphorylation at multiple activating sites including Ser338, Tyr341, Thr491, Ser494, Ser497 and Ser499 (2). p21-activated protein kinase (PAK) has been shown to phosphorylate c-Raf at Ser338 and the Src family phosphorylates Tyr341 to induce c-Raf activity (3,4). Ser338 of c-Raf corresponds to similar sites in A-Raf (Ser299) and B-Raf (Ser445), although this site is constitutively phosphorylated in B-Raf (5). Inhibitory 14-3-3 binding sites on c-Raf (Ser259 and Ser621) can be phosphorylated by Akt and AMPK, respectively (6,7). While A-Raf, B-Raf and c-Raf are similar in sequence and function, differential regulation has been observed (8). Of particular interest, B-Raf contains three consensus Akt phosphorylation sites (Ser364, Ser428 and Thr439) and lacks a site equivalent to Tyr341 of c-Raf (8,9). The B-Raf mutation V600E results in elevated kinase activity and is commonly found in malignant melanoma (10). Six residues of c-Raf (Ser29, Ser43, Ser289, Ser296, Ser301 and Ser642) become hyperphosphorylated in a manner consistent with c-Raf inactivation. The hyperphosphorylation of these six sites is dependent on downstream MEK signaling and renders c-Raf unresponsive to Chong, H. et al. (2001) EMBO J. 20, 3716-3727. Fabian, J.R. et al. (1993) Mol. Cell Biol. 13, 7170-7179.
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. 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 (). Phosphorylates TNNT2/cardiac muscle troponin T.
UniProt Protein Details:
NCBI Summary:
acts as a mitogenic protein kinase; mutant forms may play a role in transformation [RGD, Feb 2006]