CASP9 polyclonal antibody
- Known as:
- CASP9 pab (anti-)
- Catalog number:
- PAB9830
- Product Quantity:
- 100 ug
- Category:
- -
- Supplier:
- Abno
- Gene target:
- CASP9 polyclonal antibody
Related genes to: CASP9 polyclonal antibody
- Gene:
- CASP9 NIH gene
- Name:
- caspase 9
- Previous symbol:
- -
- Synonyms:
- MCH6, ICE-LAP6, APAF-3, PPP1R56
- Chromosome:
- 1p36.21
- Locus Type:
- gene with protein product
- Date approved:
- 1996-11-11
- Date modifiied:
- 2016-04-25
Related products to: CASP9 polyclonal antibody
Related articles to: CASP9 polyclonal antibody
- Chemotherapy drugs serve as one of the primary treatments for gastric cancer. However, challenges, including drug resistance and adverse side effects of the chemotherapy drugs like cisplatin, limit their efficacy. Long non-coding RNAs (lncRNAs) have been increasingly recognized as important regulators in oncogenesis and drug response. In this study, the potential effect of the long non-coding RNA LINC00162 (PICSAR) on modulating the chemosensitivity of gastric cancer cells to cisplatin was investigated. Furthermore, the impact of the LINC00162 silencing on cellular responses was evaluated under two conditions: after the siRNA-mediated silencing of the LINC00162 alone, and after combined treatment with cisplatin. - Source: PubMed
Publication date: 2026/04/19
Hosseini Seyed AliMokhtarzadeh Amir AliGhorbian SaeidBaradaran BehzadAhmadizadeh Changiz - Low back pain caused by intervertebral disc degeneration (IVDD), a common orthopedic disease in middle-aged and elderly populations, burdens patients' quality of life and work capacity. IVDD is closely associated with nucleus pulposus cell apoptosis and autophagy, mediated by BCL2, CASP3, CASP8, and CASP9. Although Duhuo alleviates inflammation and delays IVDD, its molecular mechanism remains unclear. We used bioinformatics to identify IVDD-related apoptotic/autophagic pathways and Duhuo's therapeutic mechanisms via network pharmacology. Bioinformatic analysis showed high expression of NLRP3, IL6, AKT1, and MMP9 in IVDD patients, with key cellular processes including senescence, apoptosis, autophagy, and ferroptosis, critical signaling pathways (HIF-1, FoxO, and PI3K-Akt), and main immune cells (T cells and Th17 cells). Network pharmacology identified Duhuo's main active components (ammidin, isoimperatorin, β-sitosterol, O-acetylcolumbianetin, and angelol D) and 23 potential targets, among which BCL2, CASP3, CASP8, CASP9, ERR1, and PTGS1 are crucial. Enrichment analysis indicated Duhuo prevents IVDD by regulating apoptosis, autophagy, HIF-1, and PI3K-Akt pathways, and molecular docking confirmed β-sitosterol effectively binds key targets. This study identifies IVDD's molecular basis and establishes a mechanism for targeted regulation of nucleus pulposus cell apoptosis/autophagy to prevent IVDD progression. - Source: PubMed
Yan QianLiu FeiXu ZhiweiZhang ChiYang LeiWu XiaofeiJiang ChenChen FengLi Zhifa - Chemotherapeutic proteasomal inhibitors Bortezomib (BTZ, reversible inhibitor) and Carfilzomib (CFZ, irreversible inhibitor) are established frontline therapies for multiple myeloma (MM). However, their on-target versus off-target bystander effects in the bloodstream are not clearly known. To elucidate the acute adverse effects of intravenous proteasomal inhibition, we studied some of the key cell types of blood microvasculature: barrier endothelial cells, peripheral blood mononuclear cells (PBMC)s and multiple myeloma (MM1.S) cells. BTZ, but not CFZ, is cytotoxic to microvascular endothelial cells from lung or brain at 100 nM concentration. In human pulmonary microvascular endothelial cell (HPMEC)s, BTZ induces multiple stress pathways: proteotoxic stress, endoplasmic reticulum (ER) stress, and mitochondrial reactive oxygen species (ROS) accumulation. This is associated with activation of apoptotic caspase (CASP)9 (mediator of intrinsic-apoptosis), CASP8 (mediator of extrinsic-apoptosis) and CASP3 (terminal executioner of apoptosis). BTZ-treated HPMECs significantly die and lose vascular barrier function by 24 hours post treatment. These events occur independently of external cues. When we compared 100 nM of BTZ to 250 nM of CFZ (1:2.5 being the ratio of concentration in patients), both compounds elicit comparable cytotoxicity, but elevated ER stress and apoptotic markers are driven by BTZ. Both compounds kill multiple myeloma cells comparably. PBMCs resist drug-mediated changes. Neither inhibitor elicits inflammatory response from HPMECs, MM1.S cells or PBMCs, demonstrating that proteasomal inhibition-mediated death is not inflammatory. As MM is an inflammatory cancer, the natural microvascular environment of patients contains inflammatory cytokines. To model this, we tested the effect of exogenously added tumor necrosis factor alpha (TNF), a key inflammatory cytokine found in MM patients or supernatants from drug-treated MM1.S or PBMCs on HPMECs. Exogenously added TNF or cell-free supernatant from proteasomal inhibitor-treated immune or multiple myeloma cells combined with TNF, further compromises the cellular integrity of HPMECs when compared to drug alone conditions. Physiological levels of TNF enhance stress response in both BTZ- and CFZ-treated cells. This indicates that although proteasomal inhibition is not inflammatory, TNF present in the microvascular environment synergizes with the drugs to compromise endothelial function. Our observations provide an explanation for how microvascular damage potentially underlies tissue injury driven by Bortezomib or Carfilzomib. - Source: PubMed
Publication date: 2026/05/19
Sawant PrajaktaWolf HannahMathew AleenaBensalel JohannaGallego-Delgado JulioMandal Pratyusha - Trichinella spiralis is a zoonotic nematode responsible for trichinellosis, a disease with significant public health and economic implications. The current treatment of trichinellosis has limited efficacy, so the development of novel therapeutic agents is essential for effective parasite control. Scorpion venoms contain active compounds, including antimicrobial peptides (AMPs), which have efficacy against a variety of microbes principally through membrane destruction. In this study, the in vitro anti-parasitic effects of Smp24 and Smp43, scorpion venom-derived AMPs, were evaluated against T. spiralis through toxicity assays, ultrastructural analysis, molecular docking, and gene expression profiling. In vitro toxicity assays demonstrated significant inhibitory effects of Smp24 and Smp43 (0-100 μg/mL) against adult worms and muscle larvae in a dose-dose-time dependent manner. Ultrastructural SEM analysis after treatment of either Smp24 or Smp43 at LC concentrations for 48 h revealed extensive morphological and structural damage in treated parasites, including disruption of the cuticle, indicating a direct cytotoxic effect. Molecular docking studies predicted strong binding interactions between Smp24, Smp43, and T. spiralis thymidylate synthase, suggesting inhibition of DNA synthesis as a potential mechanism of action. Moreover, gene expression revealed significant upregulation in apoptosis-related genes (Casp3, Casp9, P53) and downregulation of oncogene marker (Ras) in both T. spiralis adult worms and muscle larvae after treatment with the LC of Smps peptides, indicating the induction of apoptosis. These findings highlight the potent antiparasitic activity of Smp24 and Smp43 through multiple mechanisms, including direct toxicity, thymidylate synthase inhibition, and apoptotic cell death, suggesting they are promising candidates for controlling T. spiralis infections. - Source: PubMed
Publication date: 2026/06/05
Ibrahim Hala Abdel-Fattah MHussein Ahmed A AAbdelmaksoud Hagar FAl-Awadhi Rana MElnahas Shorouk M MSaleh Abdulrahman MMegahed Fayed Attia KoutbAbdel-Rahman Mohamed AAyed Aya S - Triphenyl phosphate (TPhP), a typical kind of organophosphate ester, is a potential threat to the environment and human health. Although it can be absorbed and accumulates in zebrafish muscle tissue, the potential effects on muscle tissue are still far from being studied. Thus, this study investigated the potential mechanism of TPhP-induced muscle damage in zebrafish, focusing on oxidative stress and apoptosis. Elevated TPhP exposure concentration caused muscle tissue damage. TPhP could increase the activities of enzymes such as superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPX), and glutathione S-transferase (GST) involved in antioxidant effects in muscle tissue. Accordingly, oxidative stress caused by TPhP exposure also increased the levels of malondialdehyde (MDA), protein carbonyls, and 8-hydroxy-2'-deoxyguanosine (8-OHdG) in zebrafish muscle tissue, indicating that TPhP caused lipid peroxidation, protein oxidation, and DNA damage. In addition, TPhP exposure transcriptionally upregulated the nuclear factor E2-related factor 2 (nrf2)--Kelch-like ECH-associated protein 1 (keap1)--antioxidant response element (ARE) (Nrf2-Keap1-ARE) signaling pathway, as evidenced by increased mRNA levels of downstream genes including nrf2, nicotinamide adenine dinucleotide phosphate hydrogen (NADPH) quinone oxidoreductase 1 (nqo1), heme oxygenase 1 (ho1), glutamate-cysteine ligase catalyst subunit (gclc), and modifier subunit (gclm). Concurrent transcriptional changes were also observed in apoptosis-related genes such as tumor protein p53 (tp53), bcl2-associated X protein (bax), B-cell lymphoma 2 (bcl2), casp3, and casp9, suggesting a potential link to apoptotic responses. Moreover, high-concentration TPhP exposure increased uncoupling protein 2 (ucp2) gene expression, revealing a regulatory role for ucp2 in regulating oxidative stress. These findings not only provide histological and molecular evidence for the toxic effects of TPhP on zebrafish muscle tissue but also emphasize the urgency of conducting a comprehensive environmental risk assessment of TPhP to inform safety standards and risk management measures. - Source: PubMed
Publication date: 2026/06/05
Li YangWang BinLiu YuqingSu LijuanLi ShuhanShen ChangxinChen JianqiuYang LikunLiu Yanhua