HIV_1 Gag p55
- Known as:
- HIV_1 Gag p55
- Catalog number:
- 05-010
- Product Quantity:
- 100ug
- Category:
- -
- Supplier:
- Sceti K.K.
- Gene target:
- HIV_1 Gag p55
Related products to: HIV_1 Gag p55
13 X Anti INT HIV mAb26S proteasome non-ATPase regulatory subunit 12,26S proteasome regulatory subunit p55,26S proteasome regulatory subunit RPN5,Homo sapiens,Human,PSMD1226S proteasome non-ATPase regulatory subunit 12,26S proteasome regulatory subunit p55,26S proteasome regulatory subunit RPN5,Mouse,Mus musculus,Psmd1226S Proteasome regulatory subunit p55 Lysate55 kDa erythrocyte membrane protein,Bos taurus,Bovine,EMP55,Membrane protein, palmitoylated 1,MPP1,p5555 kDa erythrocyte membrane protein,Chicken,EMP55,Gallus gallus,Membrane protein, palmitoylated 1,MPP1,p55,RCJMB04_22d955 kDa erythrocyte membrane protein,DXS552E,EMP55,Homo sapiens,Human,Membrane protein, palmitoylated 1,MPP1,p5555 kDa erythrocyte membrane protein,Membrane protein, palmitoylated 1,Mouse,Mpp1,Mus musculus,p5560S 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) Related articles to: HIV_1 Gag p55
- 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 - Cyclin-dependent kinase 9 (CDK9) plays a pivotal role in promoting oncogenic transcriptional pathways, significantly contributing to the development and progression of cancer. Given the unique biostability of d-amino acid, the development of d-amino acid-containing peptides (DAACPs) is a promising strategy for cancer treatment. Currently, no DAACPs inhibitor targeting CDK9-cyclin T1 have been reported. Here, we reported the identification of a novel, highly potent, selective and stable DAACPs inhibitor (peptide-5) targeting CDK9-cyclin T1 interaction. Peptide-5 showed nanomolar inhibitory effect against CDK9-cyclin T1 (IC = 4.16 ± 0.11 nM). Molecular dynamics (MD) simulation exhibited that peptide-5 stably bound to CDK9. Peptide-5 showed good inhibitory activity against multiple types of prostate cancer cells and demonstrated good biostability in mouse serum. Moreover, peptide-5 suppresses the tumor growth in DU145 cell-derived xenografts nude mice. These data suggest that peptide-5 is a potent antitumor candidate for further research. - Source: PubMed
Publication date: 2025/01/06
Xu ZhenGeng YifeiGuan LixiaNiu Miao-MiaoXu CenYang LiLiang Sudong