Protein,Flt3 Ligand Human, Sf9
- Known as:
- Protein,Flt3 Ligand Human, Sf9
- Catalog number:
- 45236
- Product Quantity:
- 0.01 mg
- Category:
- -
- Supplier:
- GenWay
- Gene target:
- Protein Flt3 Ligand Human Sf9
Related genes to: Protein,Flt3 Ligand Human, Sf9
- 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: Protein,Flt3 Ligand Human, Sf9
Related articles to: Protein,Flt3 Ligand Human, Sf9
- Since the discovery of cytotoxic agents in the mid-20th century, acute leukemia has consistently served as a model for oncology research. As the Human Genome Project and subsequent genomic profiling elucidated the landscape of somatic mutations and cytogenetic aberrations driving leukemogenesis, the development of molecularly targeted therapies has dramatically accelerated, yielding significant improvements in patient outcomes. In acute myeloid leukemia (AML), the emergence of selective inhibitors targeting high-frequency alterations such as FLT3, NPM1, and IDH1/2 has redefined the standard of care, demonstrating superior efficacy when combined with conventional intensive chemotherapy or hypomethylating agents. Simultaneously, for acute lymphoblastic leukemia (ALL), in addition to the significant improvements achieved by tyrosine kinase inhibitors (TKIs) for BCR-ABL-positive ALL, the advent of CD19- or CD22-targeted monoclonal antibodies and CAR-T cell therapies has marked an epoch-making milestone, representing a major paradigm shift in the management of relapsed or refractory cases. Bridging these two distinct lineages, menin inhibitors have emerged as a novel class of agents targeting a common pathogenic mechanism in KMT2A-rearranged AML/ALL and NPM1-mutated AML, exhibiting promising antileukemic activity across these subtypes. In this review, we describe the evolution of leukemia therapy-highlighting historical trajectory across AML, APL, and ALL from uniform cytotoxic chemotherapy to molecularly targeted agents, antibody-based therapies, and chemo-free paradigms, while outlining future perspectives for precision hematology. - Source: PubMed
Publication date: 2026/09/06
Hosono NaokoIda NaokoYamauchi Takahiro - ATP-site resistance mutations, exemplified by T315I in BCR::ABL1, limit the durability of kinase inhibitor therapy in hematological malignancies. Allosteric sites outside the catalytic cleft offer an alternative: ligands that bind regulatory pockets can stabilize inactive conformations and retain activity against mutations that defeat ATP-site drugs. Several reviews have addressed this principle across the kinome, but none has applied a hematology-focused druggability appraisal anchored in the BCR::ABL1/asciminib precedent. This review fills that gap with two contributions: mechanistic evidence that crizotinib engages BCR::ABL1 through a putative dual ATP-site/myristoyl-pocket mechanism, supported by indirect evidence and pending direct structural confirmation; and a hypothesis linking recurrent synonymous mutations in non-receptor tyrosine kinases to transiently structured regulatory regions, as a strategy for identifying latent allosteric sites Asciminib is the proof of concept. It binds the MBP of ABL1, locking the kinase in an autoinhibited-like state without competing for ATP. In the ASCEMBL trial, it achieved a major molecular response rate of 25.5% at 24 weeks versus 13.2% for bosutinib in heavily pretreated CML, with better tolerability-the first regulatory-site inhibitor approved for a hematological malignancy. The question is whether this can extends further. Dual-site strategies may raise the barrier to resistance, but the structural and biochemical validation remains incomplete for FLT3, JAK2, and BTK. Asciminib resistance is already real: A337V and P465S mutations reduce binding, and bypass signaling adds another layer. Each approved allosteric agent-asciminib, trametinib, and ivosidenib-required extensive structural and functional validation before reaching the clinic; structural prediction alone is not enough. - Source: PubMed
Publication date: 2026/09/06
Marx AilieCohen MaorRuthardt MartinMahajna Jamal - Despite advances in acute myeloid leukemia (AML) therapy, outcomes remain poor. CD123 overexpression influences proliferation and enhanced survival of leukemic cells. Its impact on the outcome is still debatable. This study aimed to assess CD123 overexpression frequency in pediatric AML, its relation with disease features, and its impact on outcomes. - Source: PubMed
Publication date: 2026/08/21
Mohammed MonaSidhom ImanEl-Sharkawy NahlaHammad MahmoudSalama MaramSoliman SoniaYassin DinaSalem SherineHamdy NayeraElnashar AmrAbouelnaga SherifAhmed SoniaElhemaly AhmedElhaddad Alaa - FMS-like tyrosine kinase 3 (FLT3) internal tandem duplication (FLT3-ITD) is a well-characterized genetic alteration associated with poor prognosis in acute myeloid leukemia (AML). Although FLT3 inhibitors, such as gilteritinib and quizartinib, initially show clinical efficacy, resistance frequently emerges because of secondary mutations. Through a kinase inhibitor library screen, we identified XL999, which exhibits potent antileukemic activity across diverse FLT3-mutant AML cell lines and primary patient samples. Mechanistically, biochemical and molecular docking analyses revealed that XL999 directly binds to FLT3-ITD, potentially independent of the common F691 resistance site, thereby suppressing downstream signaling pathways to induce cell cycle arrest and apoptosis. In preclinical mouse models harboring refractory FLT3-ITD-D835Y or ITD-F691L mutations, oral administration of XL999 effectively reduced the leukemic burden across the peripheral blood, spleen, and bone marrow, significantly prolonging survival compared with gilteritinib and quizartinib, with no overt systemic toxicity observed in short-term mouse tolerability studies. Furthermore, XL999 demonstrated robust efficacy in patient-derived xenograft models, complemented by a favorable oral bioavailability profile. Together, these findings suggest that XL999 may represent an orally bioavailable FLT3 inhibitor with the potential to overcome clinically relevant secondary resistance mutations in FLT3-ITD-positive AML, supporting its further investigation as a therapeutic candidate. - Source: PubMed
Publication date: 2026/09/04
Wang ShiyangZhang YvyinZhong ZhiweiHe JiajunFan JiaqiXiang QiYang FangfangZhang YupingWang ShunqingWang Peihong - Clonal hematopoiesis of indeterminate potential (CHIP) is a precursor condition characterized by the expansion of mutant hematopoietic stem and progenitor cell (HSPC) clones that increases the risk of hematologic malignancies. Although genome-wide association studies have identified multiple non-coding loci associated with CHIP susceptibility, their mechanisms remain unclear. We hypothesized that CHIP risk variants alter enhancer activity in HSPCs. To test this, we screened 1,374 non-coding variants from 51 CHIP-associated loci using a Massively Parallel Reporter Assay (MPRA) in the CD34+ fraction of MUTZ-3 cells. We identified 87 regulatory variants across 32 loci. Targeted genome editing in hematopoietic cells and complementary reporter assays in primary human HSPCs validated enhancer activity for variants regulating NKD2, FLT3, and MSI2. Functional studies demonstrated that increased MSI2 expression, modeling the effect of the CHIP risk allele, promotes clonal expansion of TET2-deficient HSPCs, providing a mechanistic link between inherited non-coding variation and CHIP clonal expansion. - Source: PubMed
Publication date: 2026/09/03
Nguyen TrieuJeejan JessicaIwasaki TakeshiKales SusanChakraborty JoyeetaYanase ChieShekhar ArunaKwasniak DominikaHegde AditiVoit RichardWeinstock JoshuaStengel Kristy RIto KeisukeTewhey RyanNandakumar Satish K