FLT3 (Ab_591) Antibody
- Known as:
- FLT3 (Ab_591) Antibody
- Catalog number:
- E021187-1
- Product Quantity:
- 50ug
- Category:
- Antibodies
- Supplier:
- EnoGene
- Gene target:
- FLT3 (Ab_591) Antibody
Related genes to: FLT3 (Ab_591) Antibody
- Gene:
- FLT3 NIH gene
- Name:
- fms related tyrosine kinase 3
- Previous symbol:
- -
- Synonyms:
- STK1, FLK2, CD135
- Chromosome:
- 13q12.2
- Locus Type:
- gene with protein product
- Date approved:
- 1990-07-30
- Date modifiied:
- 2019-04-23
Related products to: FLT3 (Ab_591) Antibody
Related articles to: FLT3 (Ab_591) Antibody
- In order to investigate the synergistic antibacterial effects of the novel FLT3 inhibitor G-749 in combination with colistin against Escherichia coli (E. coli). - Source: PubMed
Pan TianleLiu LianHuang RuyueWang MiFei ChenzhongLiu Yingchun - To date, the treatment of acute myeloid leukaemia (AML) remains a major challenge in hematologic malignancies, particularly among elderly patients who are unfit for intensive chemotherapy. Venetoclax, a BCL-2 inhibitor, in combination with azacitidine, has significantly improved the prognosis and survival of this patient population. However, approximately 30% of patients do not respond to venetoclax-based combination regimens, and most initial responders eventually experience relapse. Therefore, resistance to venetoclax has become a critical bottleneck limiting its long-term clinical benefits. A thorough understanding of the underlying resistance mechanisms and the development of novel strategies to overcome resistance are central to improving survival outcomes in elderly AML patients. The resistance mechanisms of venetoclax are complex and multifaceted, including genetic drivers such as TP53 mutations, FLT3-ITD, and NRAS/KRAS mutations, as well as the upregulation of anti-apoptotic proteins (e.g., MCL-1, BCL-xL), metabolic reprogramming, and altered cellular differentiation states. In response to these factors, emerging therapeutic strategies are rapidly evolving toward precision-based and combination approaches, including combinations with targeted agents (e.g., IDH2 inhibitors, FLT3 inhibitors), MCL-1 inhibitors, optimization of current dosing regimens (e.g., DEC3-VEN), and the development of novel modalities (e.g., antibody-drug conjugates, CAR-T cell therapy). Focusing on the disease characteristics of elderly AML, this narrative review summarizes the clinical efficacy of venetoclax, critically examines the multifaceted mechanisms of venetoclax resistance, and discusses current and emerging therapeutic strategies to overcome this resistance. The goal is to inform clinical practice and guide future translational research. KEY POINTS: This review elucidates the current mechanism of action, therapeutic effects, and limitations of venetoclax, focusing on its use and combination regimens in the specific patient population of elderly individuals with AML who are not suitable for intensive therapy, as well as strategies to overcome resistance, and provides future perspectives for addressing venetoclax resistance. - Source: PubMed
Zhang JinlinLiu JileZhao MohanZhang XiaoyuLiu LinlinLi MengnanCao ChangzeZhang RuiZhao Mingfeng - - Source: PubMed
Pratz Keith W - The prognostic relevance of IDH1 mutations remains unclear in acute myeloid leukemia (AML). This study, representing the first Turkish AML cohort characterized for IDH1 mutations, aimed to determine the frequency of IDH1, FLT3 and NPM1 mutations and to describe the associated clinical characteristics. We retrospectively analyzed clinical, cytogenetic, and molecular data for 57 AML patients. Bone marrow aspirates were evaluated cytogenetically using G-banding, and molecular mutations were assessed by PCR or NGS (MiSeq-Illumina). IDH1 mutations were detected in 7% of patients; FLT3 and NPM1 mutations were detected in 38.6% and 19.3% of patients, respectively. A significant positive correlation existed between IDH1 and NPM1 mutations (r = 0.388, = 0.003). Overall mortality was 56.1% and remission was achieved in 43.9%. Older age ( = 0.029) and comorbidities ( = 0.009) were significantly linked to mortality. Mortality was 100% in the four IDH1-mutant patients and significantly higher in NPM1-mutant patients. Overall survival was shorter in IDH1-mutants, although the difference did not reach statistical significance (log-rank = 0.057). Relapse occurred in 26.3%, rising to 50% in the IDH1-mutated subgroup. In this limited cohort, IDH1-mutant cases were associated with shorter overall survival and higher mortality; however, the small number of IDH1-mutant patients ( = 4) precludes definitive prognostic conclusions. Outcomes in NPM1-mutated patients were also less favorable than typically expected, possibly related to co-occurring IDH1 mutations. These descriptive findings characterize the molecular landscape of AML in an underrepresented Turkish population and may provide a foundation for larger, multicenter studies rather than confirming a prognostic role for these mutations. - Source: PubMed
Publication date: 2026/07/24
Catma YunusErdem SimgeAday AynurBayrak Tokac AysegulGuzel Mastanzade MetbanOzbalak MuratYonal Hindilerden IpekYenerel Mustafa NuriNalcaci MelihaOzturk SukruKalayoglu Besisik Sevgi - Indolo[2,3-]quinoxalines, along with their -substituted derivatives, exhibit pronounced anticancer activity, although the mechanisms of their biological action may vary. Herein, a panel of sixty-five 6-(2-aminoethyl)-6-indolo[2,3-]quinoxaline derivatives comprising eight series with distinct amine moieties connected to the tetracyclic indoloquinoxaline core via a dimethylene linker was evaluated as drug-like candidates for kinase binding and cytotoxic activity. The ADME (Absorption, Distribution, Metabolism, and Excretion) properties of the compounds included in this set were preliminarily determined using the SwissADME tool. Analysis revealed that the library of quinoxaline derivatives largely complies with the drug-likeness rule for kinase-targeted compounds. As part of the biological screening, the compounds were initially tested on two cell lines MonoMac-6 and THP-1 (both derived from patients with acute monocytic leukemia) using sunitinib, a known antitumor agent acting as a multi-target receptor tyrosine kinase inhibitor, as a reference compound. Compound , which demonstrated the highest activity in the cytotoxicity analysis (IC = 1.9 and 3.5 μM for the MonoMac-6 and THP-1 cell lines, respectively), was screened using the Eurofins DiscoverX scanEDGE panel, comprising 97 distinct kinases representing all known kinase families. Subsequently, the compound was tested using the Eurofins DiscoverX scanTK™ panel, covering 135 distinct receptor and non-receptor tyrosine kinases. Based on initial screening results, compound exhibits relatively high binding activity against fourteen tyrosine kinases, including TYK2, ZAP70, eight mutant forms of ABL1, two mutant forms of FLT3, and one mutant form of ALK, and demonstrates relatively high binding selectivity with respect to non-mutant tyrosine kinases (S-score: 0.024). Secondary screening of nine selected analogs of compound led to the identification of compound , which demonstrates relatively high binding affinity for FLT3 (D835V) (K = 0.41 μM). Molecular modeling suggested modes of binding interaction of the compounds and in the FLT3 (D835V) catalytic site. Our results demonstrate that 6-(2-aminoethyl)-6-indolo[2,3-]quinoxaline derivatives could be potential candidates for developing anticancer drugs. - Source: PubMed
Publication date: 2026/08/12
Schepetkin Igor AUvarov Alexander VEvriinov Egor AKhlebnikov Andrei I