HIV_1 Gag p24
- Known as:
- HIV_1 Gag p24
- Catalog number:
- 05-005
- Product Quantity:
- 20ug
- Category:
- -
- Supplier:
- Sceti K.K.
- Gene target:
- HIV_1 Gag p24
Related products to: HIV_1 Gag p24
13 X Anti INT HIV mAb25 kDa brain-specific protein,Homo sapiens,Human,p24,p25-alpha,TPPP,TPPP,TPPP_p25,TPPP1,Tubulin polymerization-promoting protein5H9 antigen,CD9,CD9 antigen,Cell growth-inhibiting gene 2 protein,GIG2,Homo sapiens,Human,Leukocyte antigen MIC3,MIC3,Motility-related protein,MRP-1,p24,Tetraspanin-29,TSPAN29,Tspan-2960S ribosomal protein L3,HIV-1 TAR RNA-binding protein B,Homo sapiens,Human,OK_SW-cl.32,RPL3,TARBP-BA-h HERV K Gag prot IgG1 100uA-HIV-1 env gp120 mono 100µgA-HIV-1 GAG p55 IgG fr mAb 10AccBS I Enzyme GAG^CGG PrototypeBsrB IActive HIV-2 Protease Recombinant (GST-tagged)Active HIV-2 Protease Recombinant (GST-tagged)AGFG1{HIV-1 Rev binding protein}rabbit.pAbAGFG2{HIV-1 Rev binding protein-like}rabbit.pAbAnserine human HIV-1 Tat interactive protein 2 mAbAnserine anti - anti-human HIV-1 Tat interactive protein 2 mAbAnthranilyl-HIV Protease Substrate 98% C43H65N13O11 CAS: 133233-38-2 Related articles to: HIV_1 Gag p24
- Venous thromboembolism (VTE) is an important complication in elderly patients with cancer, yet traditional clinical scoring systems insufficiently capture its molecular heterogeneity. This study aimed to construct a VTE-related molecular risk stratification framework for elderly cancer patients, identify molecular features that remain stable across datasets, and clarify the potential inflammation-coagulation interaction mechanisms underlying high-risk states. - Source: PubMed
Publication date: 2026/06/10
Wu JieHu BaojiShao LingyiWang JinhuoWang YujiaWang LukunJu YueGuo Jianrong - Isoginkgetin (ISO) is a natural flavonoid with potential anticancer effects. However, the anticancer mechanisms of ISO in gastric cancer remain insufficiently explored. - Source: PubMed
Li LinenZhu HuilingCao KunChen Hao - The P-TEFb transcriptional kinase complex regulates the pause release checkpoint step in transcription by RNA polymerase II (RNAPII). We sought to identify hypoxia-specific interactions that could direct P-TEFb activity to hypoxia-responsive genes. Using a biochemical purification approach, we discovered a hypoxia-specific, chromatin-associated interaction between the P-TEFb subunit cyclin T1 (CCNT1), nuclear localized mitochondrial chaperone Tim8-Tim13 complexes, and the hypoxia-inducible, DNA binding transcription factor BHLHE40. This interaction is confirmed across multiple human cell lines. Tim8-Tim13 complex disruption and BHLHE40 silencing both impair the transcriptional response to acute hypoxia. HIF is not involved in the CCNT1/BHLHE40/Tim8-Tim13 interaction, and neither genetic HIF-1β knockout nor pharmacological HIF-2α inhibition (belzutifan) eliminates BHLHE40 expression. Finally, BHLHE40 depletion compromises the proliferation of 786-O clear cell renal carcinoma cells, which constitutively express HIF-2α and hypoxia-responsive genes. Together, these findings reveal a partially HIF-independent regulatory axis, in which Tim8-Tim13 complexes and BHLHE40 modulate P-TEFb activity in the transcriptional response to hypoxia. - Source: PubMed
Publication date: 2026/05/20
Soliman Shimaa Hassan AbdelAzizDe Fabritiis SimoneIwanaszko MartaLin Lawrence AustinDas MadhurimaGold SarahAndersen Grant DavidChakrabarty Ram PChandel Navdeep SShilatifard Ali - Hexim proteins are key RNA-dependent regulators of eukaryotic transcription through 7SK-dependent sequestration and inactivation of the kinase P-TEFb (Cdk9-CyclinT1/2) in the 7SK RNP. P-TEFb activity drives release of RNA polymerase II from promoter-proximal pausing for eukaryotic and HIV-1 transcription. The molecular mechanism by which 7SK binding overcomes an intrinsic Hexim autoinhibition for subsequent P-TEFb inactivation has remained unresolved. Here, using NMR and biophysical methods we demonstrate that Hexim1 homodimer engages two high-affinity sites on 7SK RNA. This dual-site binding triggers a conformational rearrangement in Hexim1's disordered central region that unmasks the Cdk9-binding site, which is otherwise sequestered within an inter-monomer dimer interface. These findings reveal how Hexim autoinhibition dictates its specificity for 7SK RNA and prevents premature P-TEFb inhibition in the absence of 7SK, thereby providing a mechanistic understanding of Hexim/P-TEFb assembly into the 7SK RNP and further considerations for understanding Hexim-Tat competition during viral transcription. - Source: PubMed
Publication date: 2026/01/15
Yang YuanMurrali Maria GraziaGalvan SabrinaWang YaqiangStephen ChristineAjjampore NehaWang XiaoyuFeigon Juli - Activated immune cells are highly susceptible to human immunodeficiency virus (HIV) infection. Vitamin D (VitD) induces antimicrobial responses and reduces cellular activation. We investigated VitD effects on HIV-1 replication, glucose uptake, and gene regulation using computational and in vitro approaches. CD4 T cells from healthy male donors were treated with VitD and infected with HIV-1. After 72 h, p24 protein was measured to assess viral replication. VitD effects on anti- and pro-HIV genes were analyzed by a Boolean network model based on curated databases and the literature. CCR5 and CXCR4 coreceptor expression, AKT phosphorylation, and glucose uptake were evaluated by flow cytometry, and expression of some model-identified genes was quantified by qPCR. VitD reduced p24 by 53.2% ( = 0.0078). Boolean network modeling predicted that VitD upregulates antiviral, migration, and cell-differentiation related genes, while downregulating genes related to cellular activation, proliferation, glucose metabolism, and HIV replication, notably and . In vitro, VitD reduced AKT phosphorylation by 26.6% ( = 0.0156), transcription of by 22.7% ( = 0.0391), and glucose uptake by 22.8% ( = 0.0039) without affecting classic antiviral genes or coreceptor expression. These findings suggest an anti-HIV effect of VitD, mediated through AKT and glucose metabolism downmodulation, both involved in cell activation and HIV-1 replication. - Source: PubMed
Publication date: 2025/03/18
Loaiza John DGómez Jose FernandoMuñoz-Escudero DanielGonzalez Sandra MEubank Timothy KyleRugeles Maria TRodríguez-Perea Ana LucíaAguilar-Jimenez Wbeimar