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Rabbit polyclonal RAF1 antibody (A0223)
Supplier: ABclonal Inc.
Recommended applications: WB,IF
WB 1:500 – 1:2000 IF 1:50 – 1:200
Recommended protocols: check protocols
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Check alternative names for the antibodyExpand
RAF1 antibody,CRAF antibody,NS5 antibody,Raf-1 antibody,c-Raf antibody
c Raf antibody|C-raf antibody|C-Raf proto-oncogene, serine/threonine kinase antibody|CMD1NN antibody|Craf 1 transforming gene antibody|cRaf antibody|Craf1 transforming gene antibody|EC 22.214.171.124 antibody|kinase Raf1 antibody|Murine sarcoma 3611 oncogene 1 antibody|NS5 antibody|Oncogene MIL antibody|Oncogene RAF1 antibody|OTTHUMP00000160218 antibody|OTTHUMP00000207813 antibody|OTTHUMP00000209389 antibody|Protein kinase raf 1 antibody|Proto-oncogene c-RAF antibody|Raf 1 antibody|Raf 1 proto oncogene serine/threonine kinase antibody|RAF antibody|Raf proto oncogene serine/threonine protein kinase antibody|RAF proto-oncogene serine/threonine-protein kinase antibody|RAF-1 antibody|RAF1 antibody|RAF1_HUMAN antibody|Similar to murine leukemia viral (V-raf-1) oncogene homolog 1 antibody|TRANSFORMING REPLICATION-DEFECTIVE MURINE RETROVIRUS 3611-MSV antibody|v raf 1 murine leukemia viral oncogene homolog 1 antibody|v-raf murine sarcoma viral oncogene homolog 1 antibody|v-raf-1 murine leukemia viral oncogene-like protein 1 antibody|vraf1 murine leukemia viral oncogene homolog 1 antibody|Anti-Raf1 antibody (ab137435)
SCBT cat No: sc-81513|sc-271929|sc-271928|sc-101791|sc-21833|sc-12358|sc-28005|sc-16807|sc-16806|sc-28006|sc-81705|sc-46667|sc-25419|sc-8251|sc-376451|sc-166267|
Rabbit polyclonal RAF1 antibody
|Catalogue No.|| |
Human, Mouse, Rat
Recombinant protein of human RAF1
|Recommended dilution|| |
WB 1:500 – 1:2000
|Molecular weight|| |
Predicted: 73kDa/Observed: Refer to Figures
RAF1 antibody was tube-contained.
RAF1 antibody was purified using affinity purification.
Store at -20 Celsius degree. Avoid freeze / thaw cycles.
|Alternative antibody names|| |
RAF1 antibody,CRAF antibody,NS5 antibody,Raf-1 antibody,c-Raf antibody
|Database links|| |
|Protein names|| |
|Protein 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.
|Protein tissue specificity|| |
In skeletal muscle, isoform 1 is more abundant than isoform 2.
|Protein sequence and domain|| |
Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. RAF subfamily.; Contains 1 phorbol-ester/DAG-type zinc finger.; Contains 1 protein kinase domain.; Contains 1 RBD (Ras-binding) domain.
|Protein post-translational modifications|| |
Phosphorylation at Thr-269, Ser-338, Tyr-341, Thr-491 and Ser-494 results in its activation. Phosphorylation at Ser-29, Ser-43, Ser-289, Ser-296, Ser-301 and Ser-642 by MAPK1/ERK2 results in its inactivation. Phosphorylation at Ser-259 induces the interaction with YWHAZ and inactivates kinase activity. Dephosphorylation of Ser-259 by the complex containing protein phosphatase 1, SHOC2 and M-Ras/MRAS relieves inactivation, leading to stimulate RAF1 activity. Phosphorylation at Ser-338 by PAK1 and PAK7/PAK5 and Ser-339 by PAK1 is required for its mitochondrial localization. Phosphorylation at Ser-621 in response to growth factor treatment stabilizes the protein, possibly by preventing proteasomal degradation. Phosphorylation at Ser-289, Ser-296, Ser-301, Ser-338 and Ser-621 are somehow linked to the methylation potential of cells. Treatment of cells with HGF in the presence of the methylation inhibitor 5′-methylthioadenosine (MTA) results in increased phosphorylation at Ser-338 and Ser-621 and decreased phosphorylation at Ser-296, Ser-301 and Ser-338. Dephosphorylation at Ser-338 by PPP5C results in a activity decrease.; Methylated at Arg-563 in response to EGF treatment. This modification leads to destabilization of the protein, possibly through proteasomal degradation.
|Protein 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.
A-Raf, B-Raf and RAF1 (Raf-1) are the main effectors recruited by GTP-bound Ras to activate the MEK-MAP kinase pathway (1). Activation of RAF1 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 RAF1 at Ser338 and the Src family phosphorylates Tyr341 to induce RAF1 activity (3,4). Ser338 of RAF1 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 RAF1 (Ser259 and Ser621) can be phosphorylated by Akt and AMPK, respectively (6,7). While A-Raf, B-Raf and RAF1 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 RAF1 (8,9). The B-Raf mutation V600E results in elevated kinase activity and is commonly found in malignant melanoma (10). Six residues of RAF1 (Ser29, Ser43, Ser289, Ser296, Ser301 and Ser642) become hyperphosphorylated in a manner consistent with RAF1 inactivation. The hyperphosphorylation of these six sites is dependent on downstream MEK signaling and renders RAF1 unresponsive to subsequent activation events (11).
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|Product type|| |
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