Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all species
Show all synonyms
Select your species and application
anti-Human ARAF Antibodies:
anti-Mouse (Murine) ARAF Antibodies:
anti-Rat (Rattus) ARAF Antibodies:
Go to our pre-filtered search.
different isoforms of Araf may participate in similar developmental processes but by regulating different signaling pathways
The constitutive or induced re-localization of A-Raf to the plasma membrane compromises its ability to efficiently sequester and inactivate MST2, thus rendering cells susceptible to apoptosis
This review discusses the regulation of A-Raf protein expression, and the roles of A-Raf in apoptosis and cancer, with a special focus on its role in resistance to Raf inhibitors. [review]
analysis of FGFR2-PPHLN1 fusion and ARAF mutations in intrahepatic cholangiocarcinoma
Aberrant expression of A-, B-, and C-RAF, and COT is frequent in PTC; increased expression of COT is correlated with recurrence of PTC.
Dimerization of the kinase ARAF promotes MAPK pathway activation and cell migration.
The study identifies somatic activating ARAF mutations in Langerhans cell histiocytosis.
Galpha12-ARAF-ERK pathway stimulates RFFL transcription through the transcription factor c-Myc.
show that Araf antagonizes mesendoderm induction and patterning activity of Nodal/Smad2 signals in vertebrate embryos by directly inhibiting Smad2 signalling
study investigated role of ARAF in cancer cell signaling and examined the role of ARAF in mediating paradoxical activation of the MAPK pathway in cells treated with RAF inhibitors; ARAF seems to stabilize BRAF:CRAF complexes in cells treated with RAF inhibitors and regulate cell signaling in a subtle manner to ensure signaling efficiency
Ras pathway activation via EGF treatment induced strong binding between B-Raf and C-Raf and a low level of binding between B-Raf and A-Raf.
hnRNP H blocks MST2-mediated apoptosis in cancer cells by regulating A-Raf transcription.
In a two-hybrid screen of human fetal liver cDNA library, TH1 was detected as a new interaction partner of A-Raf; this specific interaction may have played a critical role in the activation of A-Raf.
A-Raf kinase is negatively regulated by trihydrophobin 1
mutation analysis of the conserved regions in the ARAF gene in human colorectal adenocarcinoma
A-Raf residues are identified that bind to specific phosphoinositides, possibly as a mechanism to localize the enzyme to particular membrane microdomains rich in these phospholipids.
These data reveal that B-RAF is an important mediator of neuronal survival, migration, and dendrite formation and that A-RAF cannot fully compensate for these functions.
Positive regulation of A-RAF by phosphorylation of isoform-specific hinge segment and identification of novel phosphorylation sites.
A-Raf interacts with MEK1 and activates MEK1 by phosphorylation.
PKM1 interacts with A-Raf, an upstream regulator of the MEK/ERK pathway, and that this interaction contributes to MEK1 phosphorylation by A-Raf.
A- and B-Raf ablation in chondrocytes does not alter skeletal development, whereas ablation of C-Raf decreases hypertrophic chondrocyte apoptosis and impairs vascularization of the growth plate. However, ablation of C-Raf does not impair phosphate-induced ERK1/2 phosphorylation in vitro, but leads to rickets by decreasing VEGF protein stability.
A-Raf promotes osteoblasts differentiation in response to mechanical stress.
DA-Raf-dependent inhibition of the Ras-ERK signaling pathway in alveolar epithelial 2 cells is required for alveolar formation via triggering MMP2 activation followed by myofibroblast differentiation.
Expression of Araf in the mouse nucleus accumbens is modulated by a sequence variant (B2 SINE indel) in the 3' UTR of Comt (catechol-O-methyltransferase).
the binding of 14-3-3gamma to Raf indicates the critical role of this protein in ischemia-induced apoptosis and the changes in signal transduction in astrocytes in culture.
Raf-1 and A-Raf have a combined role in controlling physiological transient ERK activation and in maintenance of cell cycle progression at its usual rate.
This proto-oncogene belongs to the RAF subfamily of the Ser/Thr protein kinase family, and maybe involved in cell growth and development. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
serine/threonine protein kinase ARAF standard form
, serine/threonine-protein kinase A-Raf
, v-raf murine sarcoma 3611 viral oncogene homolog
, v-raf murine sarcoma 3611 viral oncogene-like protein
, serine/threonine protein kinase ARAF
, serine/threonine-protein kinase A-Raf-like
, A-Raf proto-oncogene serine/threonine-protein kinase
, Oncogene ARAF1
, Ras-binding protein DA-Raf
, proto-oncogene A-Raf-1
, proto-oncogene Pks
, v-raf murine sarcoma 3611 viral oncogene homolog 1
, proto-oncogene A-Raf
, raf-related oncogene
, Raf related protein
, Ras-binding protein
, v-raf oncogene homolog 1 (murine sarcoma 3611 virus)