GLI1 Antibody
- Known as:
- GLI1 Antibody
- Catalog number:
- 46-849
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- Prosci
- Gene target:
- GLI1 Antibody
Related genes to: GLI1 Antibody
- Gene:
- GLI1 NIH gene
- Name:
- GLI family zinc finger 1
- Previous symbol:
- GLI
- Synonyms:
- -
- Chromosome:
- 12q13.3
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2016-01-15
Related products to: GLI1 Antibody
Related articles to: GLI1 Antibody
- Recent studies have found that the reticulophagy pathway is able to clear excess endoplasmic reticulum to protect cells from endoplasmic reticulum stress-induced damage. The role of reticulophagy in prostate cancer is still unknown. Key genes of reticulophagy were studied. Subsequently, the ULK3 and CAMK2B mRNA levels were confirmed. ULK3 and CAMK2B expression were elevated in prostate cancer tissues. The silencing of ULK3 inhibited prostate cancer cell vitality. The overexpression of ULK3 had the opposite effect. ULK3 was able to enhance the CAMK2B protein expression by promoting the entry of GLI1 into the nucleus, thereby upregulating the level of reticulophagy. Knockdown of CAMK2B could inhibit reticulophagy induced by ULK3. Further experiments showed that ULK3 phosphorylated GLI1, promoted its nuclear entry and binding to the CAMK2B promoter to enhance CAMK2B expression. Down-regulation of ULK3 inhibited the growth of prostate cancer vitality in vivo. This study confirmed that ULK3 promoted the prostate cancer by upregulating GLI1/CAMK2B-induced reticulophagy. - Source: PubMed
Publication date: 2026/06/15
Wang Qin-QuanSun ChenWu Jin-HuaYu Dong-DongZhou Hui-Liang - -altered mesenchymal tumors represent a recently defined group of neoplasms molecularly characterized by gene fusions or amplifications. Although initially thought to share similar molecular alterations, including pericytoma with fusion, plexiform fibromyxoma, and gastroblastoma, these tumors are now recognized as distinct entities with specific clinicopathological features. Histologically, -altered mesenchymal tumors typically exhibit a multinodular growth pattern composed of relatively uniform epithelioid-to-ovoid cells arranged in nested formations. These nests are supported by a delicate arborizing capillary network and are often embedded in a myxoid stroma. Immunohistochemically, variable positivity for CD56, S100, CD10, smooth muscle actin, cyclin D1, and p16 has been reported. GLI1 immunohistochemistry is both highly sensitive and specific, serving as a valuable diagnostic marker in the appropriate context. Some -amplified tumors may show co-amplification of neighboring genes, including , and , which can result in variable immunoreactivity depending on amplicon size. These tumors can arise at a broad range of anatomical sites and occur across all age groups. Although -altered mesenchymal neoplasms were initially considered indolent, malignant cases with metastatic potential have been reported. Necrosis, high mitotic index, and large tumor size are associated with an increased risk of metastasis. Tumors with amplification generally demonstrate worse clinical outcomes than those driven by fusions. Definitive diagnosis requires molecular confirmation via next-generation sequencing and/or fluorescence in situ hybridization. Accurate recognition of -altered mesenchymal tumors has important diagnostic, prognostic, and therapeutic implications. Herein, we describe the clinicopathologic features of GLI1-altered neoplasms, including their molecular findings and the differential diagnosis with other tumors exhibiting overlapping morphology and immunoprofile. - Source: PubMed
Publication date: 2026/07/13
Rivas-Hernández RaquelGiner FranciscoPrados ElenaClaramunt ReyesLópez RaquelFernández AntonioMayordomo EmparLópez-Guerrero José AntonioNavarro SamuelLlombart-Bosch AntonioMachado Isidro - Peripheral nerve injury (PNI) is characterized by limited regenerative capacity and incomplete functional recovery. Schwann cells (SCs) are essential for nerve repair, but their clinical application is constrained by limited availability. Ectomesenchymal stem cells (EMSCs), derived from neural crest lineage, represent a promising alternative; however, their inefficient differentiation into SC-like cells remains a key limitation. This study investigated whether activation of Hedgehog signaling via Sonic hedgehog (Shh) could enhance SC-like differentiation and improve nerve regeneration. - Source: PubMed
Publication date: 2026/06/24
Zhang DengxinBian RuxiMa YaqiongYuan HuiqingWu XuechaoTang HongZhao Feifei - Fibrostenosis is a common and disabling complication of Crohn's disease (CD) with no reliable early biomarkers, limited treatment options and high postoperative recurrence. - Source: PubMed
Publication date: 2026/07/08
Wang DanshuZhao XiangyuYang QidiZhu DehaoLiao YijingZhao YizhouSun SishenWang JiaxinZhuang HaimingZhang ShuowenWang XinyuChe TianyiLi MingjiGu YubeiSun JingWu NingboYe YouqiongMao RenZhang YaoZou Duowu - Carpenter syndrome, caused by biallelic mutations in MEGF8 or RAB23, manifests with craniosynostosis through incompletely defined mechanisms. While both genes encode negative regulators of Hedgehog (Hh) signaling, we demonstrate that MEGF8 maintains cranial suture patency through a distinct, Hh-independent pathway. Loss of MEGF8 disrupts ubiquitination and lysosomal degradation of BMPR1A, leading to BMPR1A accumulation and hyperactivation of canonical BMP-SMAD1/5/9 signaling, which accelerates osteogenic differentiation of cranial mesenchyme. Using Megf8 mutant mice, we show tissue-specific specialization: limb defects are Hh-dependent and rescued by SMO inhibition, whereas craniosynostosis is BMP-driven and refractory to Hh blockade, with BMP type I receptor inhibition selectively rescuing the cranial phenotype. Comparative analyses reveal that MEGF8 and RAB23 promote osteogenic differentiation through distinct mechanisms-MEGF8 via ubiquitin-mediated BMPR1A turnover and BMP-SMAD activation, RAB23 through FGF-ERK signaling-despite both affecting GLI1-mediated transcription. Reintroduction of human MEGF8 in MEGF8-knockdown cells restores BMPR1A protein levels, validating the specificity of MEGF8-mediated BMPR1A regulation. These findings suggest that MEGF8 modulates BMP signaling post-transcriptionally, establishes tissue-specific regulatory mechanisms in syndromic disorders, and demonstrates how divergent pathways converge on shared phenotypes, with implications for pathway-specific therapeutic strategies. - Source: PubMed
Publication date: 2026/07/03
Hwangbo KoeunPark JihyunRho HyunjinWoo Dong-CheolSung Young HoonKim Soo-HyunSong JaewhanKo Hyuk Wan