Raf1 (ca)
- Known as:
- Raf1 (ca)
- Catalog number:
- 000648A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- Raf1 ()
Related genes to: Raf1 (ca)
- Gene:
- RAF1 NIH gene
- Name:
- Raf-1 proto-oncogene, serine/threonine kinase
- Previous symbol:
- -
- Synonyms:
- Raf-1, c-Raf, CRAF
- Chromosome:
- 3p25.2
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2019-04-23
Related products to: Raf1 (ca)
Related articles to: Raf1 (ca)
- BAP1 (BRCA 1-associated protein 1)-inactivated melanocytic tumor (BIMT) is a melanocytic neoplasm characterized histologically by large epithelioid cells and is commonly associated with a conventional nevus component. The defining molecular alteration is inactivation of the BAP1 gene. Initiating mutations in BIMT include BRAF p.V600E, or less commonly RAS mutations and fusions involving RAF1. In this article, we report a case of BIMT with a BAP1 mutation and a novel PDZRN3::BRAF fusion. Histologic examination revealed an intradermal melanocytic neoplasm with nests and single units of large, atypical epithelioid cells with abundant amphophilic-eosinophilic cytoplasm, well-defined cell borders, large vesicular nuclei, and prominent nucleoli. Frequent binucleated and multinucleated melanocytes were present. There was no associated conventional nevus component. Scattered mitotic activity were identified. No evidence of maturation, necrosis, or lymphovascular or perineural invasion was seen. The lesional cells were immunoreactive for SOX10, Melan A, and HMB45 (focal, minimal, and weak), and were negative for PRAME. There was patchy loss of expression of p16 and complete loss of BAP1 expression. Molecular analysis demonstrated BAP1 mutation and a novel fusion involving PDZRN3::BRAF. Our finding expands our current understanding of the molecular landscape and pathogenesis of BIMT. - Source: PubMed
Publication date: 2026/04/17
Yu YanhongSabljic ThomasCapo-Chichi Jose-MarioKamil Zaid Saeed - This study aimed to describe the clinical manifestations and genetic variants of Noonan syndrome in a Colombian pediatric population and to identify the genes most frequently associated with specific phenotypic features. - Source: PubMed
Publication date: 2026/04/16
Martínez Rueda Silvia CDel Pilar Montilla MariaBaquero CarolinaGómez SusanaLopera Maria VictoriaZuluaga Nora AlejandraForero Adriana CarolinaGiraldo GustavoPineda Trujillo NicolásMartínez Juan CamiloDurán Ventura PaolaAlfaro Juan Manuel - This study aimed to assess the detection rate and spectrum of pathogenic variants (PVs) and candidate variants (variants of uncertain significance, VUS) in AVM patients. - Source: PubMed
Publication date: 2026/04/16
Schmidt Vanessa FSchanze DennyBrill RichardLoeser Julius HUller WibkeDoppler MichaelCangir ÖzlemHengst SusanneVielsmeier VeronikaPech MaciejObereisenbuchner FlorianSchirren MirjamSint AlenaPuhr-Westerheide DanielDeniz SinanWeiß Jakob B WHäberle BeateHartel AlexandraFröba-Pohl AlexandraHaehl JuliaHolm AnnegretSporns Peter BScherf ThomasRicke JensLassmann SilkeSeidensticker MaxWohlgemuth Walter AKimm Melanie AZenker MartinWildgruber MoritzKapp Friedrich G - The stability and activity of CRAF/Raf1 kinase are stringently regulated by heat shock protein 90 (Hsp90). Hsp90-mediated client folding and maturation are governed by its co-chaperones, but their functionality in chaperoning CRAF kinase to support signaling under physiological conditions remains poorly understood. Here, we show that Hsp70/Hsp90 organizing protein (HOP) associates with CRAF kinase tomaintain its activity and facilitates MAPK pathway activation. This activation is mediated by TPR2A-2B-DP2 domain of HOP and requires efficient binding to Hsp90. Although Cdc37 recruits Hsp90, it cannot compensate for HOP function. Downregulation of HOP/Sti1 in yeast and mammalian cell culture significantly reduces the CRAF signaling. Our data suggest that Hsp90 is recruited to CRAF in two distinct steps: first during folding/maturation via HOP and Cdc37, and later during activation mediated by HOP. Therefore, HOP is a regulator of CRAF kinase during activation of MAPK pathway and serves as a modulator of growth signaling beyond its client folding and maturation function. - Source: PubMed
Publication date: 2026/04/14
Gayen NilanjanMitra SahanaRoy SomeshMandal Atin K - Loss of epithelial polarity is a critical driver of tumor progression; however, how core polarity regulators interface with oncogenic signaling pathways in hepatocellular carcinoma (HCC) remains incompletely defined. LLGL scribble cell polarity complex component 1 (LLGL1) is an evolutionarily conserved polarity protein with well-established tumor-suppressive roles in multiple epithelial malignancies. Nevertheless, how LLGL1 loss shapes oncogenic signaling outputs and cellular phenotypes in HCC remains unclear. In this study, we investigated the consequences of LLGL1 knockout (KO) in epithelial-like Huh-7 HCC cells. LLGL1 loss resulted in enhanced proliferative capacity and increased clonogenic potential, accompanied by altered cell-cycle distribution characterized by reduced G1-phase and increased S-phase fractions ( < 0.001). At the signaling level, LLGL1 KO cells displayed potentiated EGFR-driven RAS/MAPK pathway activation, with increased EGFR phosphorylation, enhanced downstream RAF1-MEK-ERK-RSK signaling, elevated EGFR abundance, and selective modulation of RAF1 protein levels. Functionally, LLGL1 loss markedly enhanced migratory and invasive behavior ( < 0.0001). Despite increased motility, LLGL1 KO cells exhibited remodeling of epithelial-mesenchymal transition (EMT)-associated markers without evidence of a classical EMT program. Collectively, these findings position LLGL1 loss as a central factor associated with altered MAPK signaling, EMT marker remodeling, and tumor-promoting cellular phenotypes in HCC. - Source: PubMed
Publication date: 2026/03/24
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