ABL2 (Human) Recombinant Protein (Q01)
- Known as:
- ABL2 (Human) Recombinant Protein (Q01)
- Catalog number:
- H00000027-Q01-25
- Product Quantity:
- 25 ug
- Category:
- -
- Supplier:
- Abno
- Gene target:
- ABL2 (Human) Recombinant Protein (Q01)
Related genes to: ABL2 (Human) Recombinant Protein (Q01)
- Gene:
- ABL2 NIH gene
- Name:
- ABL proto-oncogene 2, non-receptor tyrosine kinase
- Previous symbol:
- ABLL
- Synonyms:
- ARG
- Chromosome:
- 1q25.2
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2016-04-25
Related products to: ABL2 (Human) Recombinant Protein (Q01)
Related articles to: ABL2 (Human) Recombinant Protein (Q01)
- Nucleic acid therapeutics offer promise for precision cancer treatment, but are limited by inaccurate target selection and inefficient delivery. This work presents a therapeutic platform combining dual machine learning models (LASSO and RSF)-based miRNA target screening with a modular biomimetic nanocarrier system. Systematic screening and experimental validation identify miR-873 as a previously uncharacterized tumor-suppressive miRNA in prostate cancer, and miR-20a as oncogenic. Mechanistic studies reveal that they regulate HNRNPK and ABL2, modulating pathways involved in proliferation and metastasis. Then, the biomimetic nanocarrier, engineered with prostate cancer cell-derived endoplasmic reticulum membrane (ERM), is successfully developed for cytosolic co-delivery of miR-873 mimic and miR-20a inhibitor in prostate cancer, achieving significant and synergistic suppression of tumor proliferation and metastasis both in vitro and in vivo. Besides, co-loading with docetaxel further enhances antitumor effects, underscoring its potential for combination therapies to inhibit cancer progression. These findings highlight both the therapeutic synergy of rationally selected miRNA combinations and the platform's versatility for precision cancer treatment. - Source: PubMed
Publication date: 2026/08/19
Xu HangMin PengxiangFu YanbinSun GeWu HuiPan MengqiaoZhao ChaoxianLi JiatongWu YingXu YingGu BinPan JiahuaZhang LinLiu Peifeng - The function of the NHS gene that is responsible for Nance-Horan Syndrome has remained elusive at the cellular level. Using CRISPR/Cas9, we inactivated the NHS gene in MCF10A cells and characterized the isoforms expressed in these cells. NHS KO cells displayed reduced migration persistence, a phenotype that was fully rescued by the long isoform 1 (i1) that contains an N-terminal WAVE Homology Domain (WHD), but only partially rescued by the short isoform two (i2), which does not. Patient mutations resulting in NHS proteins truncated at their C-terminus also reduced the ability of NHS i1 to rescue migration persistence. Using Tandem Affinity Purification (TAP) of NHS i1 and mass spectrometry, we identified as major NHS partners all subunits of the WAVE Regulatory Complex (WRC) except WAVE subunits themselves, indicating that the WHD of NHS assembles a WAVE Shell Complex (WSC). The Arp2/3 complex and the Nucleation Promoting Factor (NPF) WAVE that activates it are critical for migration persistence. To investigate the role of the NHS-containing WSC, we performed TAP of the ABI1 subunit in parental and NHS KO cells and identified differential partners associated with ABI1 only in parental cells, but not in NHS KO cells. The most abundant of these were the WIPF2/N-WASP complex, which together with the kinase ABL2, was also critical for migration persistence. These results suggest that NHS controls cell migration by remodeling NPF complexes and their higher order assembly. - Source: PubMed
Publication date: 2026/08/13
Tsydenzhapova EkaterinaFokin Artem IDavid Nicolas BRocques NathaliePolesskaya AnnaHaddad ImanVinh JoëlleGuérois RaphaëlGautreau Alexis M - Enteroviruses, including Coxsackievirus B3 (CVB3), are significant human pathogens that cause severe diseases, such as viral myocarditis, pancreatitis, and encephalitis. ABL proto-oncogene 2 (ABL2), a non-receptor tyrosine-protein kinase, regulates diverse physiological processes and participates in virus infection; however, its role in enterovirus infection remains uncharacterized. Here, we demonstrate a novel host-virus interaction: enteroviruses degrade ABL2 via the ubiquitin-proteasome system through their non-structural protein 2B. Furthermore, ABL2 functions as an antiviral restriction factor during enterovirus infection, specifically inhibiting the early stages of viral replication. Mechanistically, ABL2 directly interacts with RAC1, a Rho family GTPase, and downregulates RAC1 protein levels, thereby suppressing RAC1-dependent activation of the PI3K/AKT signaling pathway. In summary, our study reveals a post-translational mechanism by which enteroviruses evade host antiviral defenses, providing a rationale for therapeutic development against enteroviral diseases. - Source: PubMed
Publication date: 2026/08/11
Yuan MengranQiao XiaorongWang HuaChen NuoWang YanLi YuhanZhou XiaoxiangJi ZengjunShen Hongxing - [This retracts the article DOI: 10.2147/DDDT.S93104.]. - Source: PubMed
Publication date: 2026/07/09
- Dysfunction of vascular endothelial cells (VECs) is a common feature of both psoriasis and diabetes. Comorbidity of these two conditions increases the risk of diabetic foot ulcer (DFU), yet the shared mechanisms remain unclear. - Source: PubMed
Publication date: 2026/04/13
Xu JiaxinZhang XinZhang TianyuanWang GangLi Qingyang