KIF1A antibody - N-terminal region (ARP33900_P050)
- Known as:
- KIF1A (anti-) - N-terminal region (ARP33900_P050)
- Catalog number:
- arp33900_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- KIF1A antibody - N-terminal region (ARP33900_P050)
Related genes to: KIF1A antibody - N-terminal region (ARP33900_P050)
- Gene:
- KIF1A NIH gene
- Name:
- kinesin family member 1A
- Previous symbol:
- ATSV, C2orf20, SPG30
- Synonyms:
- UNC104
- Chromosome:
- 2q37.3
- Locus Type:
- gene with protein product
- Date approved:
- 1995-12-18
- Date modifiied:
- 2019-04-23
Related products to: KIF1A antibody - N-terminal region (ARP33900_P050)
Related articles to: KIF1A antibody - N-terminal region (ARP33900_P050)
- Alternations of DNA methylation occur in aging, which is regulated by DNA methyltransferases (DNMTs). In this study, we show that even though the transcription of DNMT1, the only enzyme that maintains DNA methylation in the mammalian genome, is reported to be decreased in an age-dependent manner, the decrease of mRNA does not result in a decrease of its protein. Instead, DNMT1 protein is increased in aged mouse tissues, which is responsible for the methylation of genes related to macroautophagy/autophagy, senescence repression, and melanin synthesis and transport in aged organs, resulting in a decline of autophagy, an increase of senescence in those organs, and a decrease in melanin production in hair follicles (canities) in response to ionizing radiation (IR). Genetic deletion and inhibition of DNMT1 can reverse these processes. The interaction of DNMT1 with ATG7 through its CXXC domain is essential for its degradation, and treatment with senolytics also downregulates DNMT1 in aged organs, supporting two feedback loops between them.: 4-OHT, 4-hydroxytamoxifen; ChIP, chromatinimmunoprecipitation; D, dasatinib; D-gal, D-galactose; DCT/Trp-2, dopachrometautomerase; DMRs, differentially methylated regions; DNAm, DNA methylation; DNMTs,DNA methyltransferases; DSBs, double-stranded breaks; ETO, etoposide; GST, glutathione-S-transferase; HEK293T,human embryonic kidney 293T; HEM, human epidermal melanocytes; Hydr, hydralazine;IP, immunoprecipitation; IR, ionizingradiation; KIF1A, kinesin family member 1A; M, methylated; MmIMCD3,mouse inner-medullary collecting duct 3; MITF, melanocyte inducingtranscription factor; MSP, methylation specific PCR; NCBI, national center for biotechnologyinformation; N-me, N-methyladenosine; PBMCs, peripheral blood mononuclear cells;Pro, proliferating; Q, quercetin; Rapa, rapamycin; RRBS, reduced representationbisulfite sequencing; RT, reverse transcription; SA-GLB1/β-Gal, senescence-associatedgalactosidase beta 1; SASP, senescence-associated secretory phenotype; Sen, senescent; SNP, single nucleotidepolymorphism; TYR, tyrosinase; TYRP1/Trp-1, tyrosinase related protein 1; UHRF1,ubiquitin like with PHD and ring finger domains 1; UM, unmethylated; UTR, untranslatedregion; WGBS, whole-genome bisulfite sequencing. - Source: PubMed
Publication date: 2026/05/28
Li LuMao XinyueLi Linda XiaoyanXiao HuapingLou ZhenkunLiu HongboZhou Julie XiaYao LiLi Xiaogang - The AWC olfactory neuron pair specifies asymmetric subtypes, AWC and AWC, through stochastic and coordinated cell signaling events. UNC-104/kinesin-3 (KIF1A) and UNC-116/kinesin-1 motor proteins act in the AWC cell to regulate the synaptic localization of the TIR-1/SARM1-assembled calcium signaling complex in the AWC cell to promote AWC. However, the molecular mechanism in the AWC cell that acts non-cell autonomously to control synaptic TIR-1 calcium signaling to promote AWC remains unclear. Here, we show that JIP-1, a conserved c-Jun N-terminal kinase (JNK)-interacting protein 1, mediates the synaptic localization of TIR-1 in the AWC axon to specify the AWC subtype. A loss-of-function mutant, identified from an unbiased forward genetic screen, has reduced localization of TIR-1 at synapses in the AWC axon and accumulation of TIR-1 in the AWC cell body. mutants significantly enhance the 2AWC phenotype of a hypomorphic mutant. JIP-1, like UNC-104 and UNC-116, mainly acts non-cell autonomously in AWC to specify the AWC subtype. Our findings provide mechanistic insights into how cell-specific Ca signaling proteins, such as TIR-1, target synaptic regions via intercellular signaling to promote neuronal diversification. - Source: PubMed
Publication date: 2026/05/05
Hsieh Yi-WenYuan ShengyaoYang JunSiete CesarChuang Chiou-Fen - KIF1A-associated neurological disorder (KAND) is a rare hereditary condition caused by KIF1A variants, affecting axonal transport and presenting with a wide clinical spectrum, including hereditary spastic paraplegia. This case of childhood-onset KAND reveals FTLD-TDP43 with motor neuron disease pathology emerging late in the disease course, suggesting that HSP and FTLD-MND share a pathological continuum through a TDP-43-related pathway and expanding the clinicopathological spectrum of KAND. - Source: PubMed
Saito RieHasegawa ArikaTakahashi TetsuyaKoike RyokoHara NorikazuGabdulkhaev RamilKoh KishinKawakami AkioTakiyama YoshihisaIkeuchi TakeshiKakita Akiyoshi - Colon cancer (CC) is a highly prevalent malignant tumor with a high mortality rate worldwide. Despite recent advancements in diagnosis and treatment, the overall prognosis for patients remains poor, especially for those with metastasis. Exploring key genes associated with the prognosis of patients with colon cancer, establishing effective molecular models, and validating their functions are necessary to optimize patient management and develop novel therapeutic strategies. This study aimed to reveal the role of the key gene SERPINE1 in the progression of colon cancer and its potential clinical application value through bioinformatics analysis and experimental validation. - Source: PubMed
Publication date: 2026/05/05
Li XinLi NanaWang YujieHan QixiangLi XiaodongTu QiushiSun BoshiYang HaoGao Yuan - Product inhibition is a common regulatory feature of ATPases, in which the hydrolysis product suppresses further enzymatic activity. Kinesins are microtubule-dependent ATPases that typically undergo inhibition by ADP, the product of ATP hydrolysis. Here, we show that the Caenorhabditis elegans kinesin-3 KLP-6 is unusually resistant to product inhibition by ADP and continues to move along microtubules at an unreduced speed even in the presence of high ADP concentrations. Kinetic measurements of the Michaelis constant for Mg·ATP (K) and the inhibition constant for Mg·ADP (K) revealed a K/K ratio of 44.9 for KLP-6, markedly higher than the ratio of 1.3 for the well-studied kinesin-3 KIF1A, indicating substantially greater selectivity for ATP over ADP. Sequence comparison identified a unique region in the α2a helix of KLP-6. Replacing this segment with the corresponding KIF1A sequence abolished the elevated ATP/ADP selectivity, demonstrating that this region is required for resistance to product inhibition. Molecular dynamics simulations further showed that the α2a helix is less conformationally stable in the ADP-bound state than in the ATP-bound state, providing a structural basis for nucleotide discrimination. Together, our findings reveal a molecular mechanism underlying nucleotide selectivity in kinesins. - Source: PubMed
Publication date: 2026/05/05
Kita TomokiWatanabe TaiseiNiwa Shinsuke