ST6GALNAC5 Blocking Peptide, Blocking Peptides
- Known as:
- ST6GALNAC5 Blocking Peptide, Blocking Peptides
- Catalog number:
- 33R-1167
- Product Quantity:
- 100 ug
- Category:
- -
- Supplier:
- Fitzgerald
- Gene target:
- ST6GALNAC5 Blocking Peptide Peptides
Related genes to: ST6GALNAC5 Blocking Peptide, Blocking Peptides
- Gene:
- ST6GALNAC5 NIH gene
- Name:
- ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 5
- Previous symbol:
- SIAT7E
- Synonyms:
- MGC3184, ST6GalNAcV
- Chromosome:
- 1p31.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-12-05
- Date modifiied:
- 2016-04-29
Related products to: ST6GALNAC5 Blocking Peptide, Blocking Peptides
Related articles to: ST6GALNAC5 Blocking Peptide, Blocking Peptides
- Triple-negative breast cancer (TNBC) is associated with a high risk of brain metastases (BMs). Although systemic therapies have improved extracranial disease control, the central nervous system (CNS) remains less accessible to numerous agents. As a result, this limited drug penetration makes brain metastases (BMs) remain common in TNBC, which are a leading cause of serious symptoms. This review summarizes recent key advances in triple-negative breast cancer brain metastases (TNBC-BMs), including epidemiology, prognostic stratification, biological mechanisms of CNS tropism and treatment resistance, and evolving management strategies. We discuss potential mechanisms of brain colonization, including the FOXC1-CXCR4 axis, ST6GALNAC5-related interactions with the blood-brain barrier (BBB), and the bidirectional crosstalk between metastatic cells and the brain microenvironment, particularly astrocytes and microglia. Furthermore, we evaluate the evolving clinical management, emphasizing the transition from whole-brain radiotherapy (WBRT) toward more selective local approaches such as stereotactic radiotherapy (SRS) and hippocampal sparing techniques. Concurrently, we examine the integration of CNS active systemic therapy across specific molecular subsets. This review systematically distinguishes standard-of-care interventions from investigational strategies, ultimately underscoring critical evidence gaps within the TNBC-BM landscape. - Source: PubMed
Publication date: 2026/04/07
Yang HongliZhao YangWang YueMa XiaoyuanLing JinmeiZeng XianyiLi ZihuangLiao Guixiang - Cognitive resilience in Alzheimer's disease (AD) requires the maintenance of synaptic integrity despite progressive pathological insults. Reactive astrocytes can switch between neuroprotective and neurotoxic states, and their maladaptive transition significantly accelerates neurodegeneration, yet the molecular drivers of this shift remain elusive. Here, using published single-nucleus transcriptomic data, we identified the sialyltransferase St6galnac5 as a candidate regulator associated with reactive, pro-inflammatory astrocyte states. We further show that astrocyte-specific, AAV-mediated knockdown of St6galnac5 in female 3xTg-AD mice improves spatial learning, memory and anxiety-like behaviors. Neuropathological assessment revealed that this functional recovery was underpinned by a marked reduction in amyloid-β and tau pathologies, alongside the preservation of synaptic integrity. Consistent with a shift toward a less inflammatory astrocyte state, St6galnac5 knockdown decreased A1-associated markers and increased A2-associated markers in vitro and alleviated neurite outgrowth deficits in neuron-astrocyte co-culture. Together, our findings identify St6galnac5 as a critical molecular switch driving astrocytic dysfunction in AD, and further propose that targeted inhibition of this sialylation pathway represents a viable strategy to bolster astrocytic resilience and slow disease progression. - Source: PubMed
Publication date: 2026/03/19
Xue ChunhongChen ChenZou XiaoqiongLi ShiyingLv YehuaLiu Wei - Dysregulated expression of long non-coding RNAs (lncRNAs) has been shown to play a critical role in the tumorigenicity of clear cell renal cell carcinoma (ccRCC). Meanwhile, sialylation plays a pivotal role in cancer progression and in modulating the tumor immune microenvironment. However, how sialylation-immune-related lncRNAs (SIRLs) influence tumor immune microenvironment and progression of ccRCC remains unclear. - Source: PubMed
Publication date: 2026/01/16
Dai ZiranZhou HaoFeng ZihaoZhang MingxiaoAi ZheyuHuang GaoweiCen JunjieLiang YanpingWei JinhuanChen WeiLuo JunhangChen Zhenhua - The two sialyltransferases in the ST6GALNAC subfamily (EC 2.4.99.-; CAZy family GT29), ST6GalNAc5 and ST6GalNAc6, catalyze the formation of the linkage from the sialic acid moiety to the C6 position of N-acetylgalactosamine (GalNAc) as well as to N-acetylglucosamine (GlcNAc), and are known as α-2,6-sialyltransferases. This activity is interesting for the synthesis of the disialylated oligosaccharide disialyllacto-N-tetraose (DSLNT). Human sialyltransferases ST6GalNAc5 and ST6GalNAc6 produced in HEK293 cells are commercially available at a smaller scale. In this study, we demonstrated that ST6GalNAc5 and ST6GalNAc6 can be functionally expressed in Pichia pastoris X-33. The level of ST6GalNAc5 and ST6GalNAc6 expression and activity largely depended on the type of construct, as well as on expression conditions, namely temperature, methanol feeding regime, and supplements. Insertion of a (GGGS)₂ linker peptide between the gene and the α secretion factor improved the secretion of active enzyme in P. pastoris X-33. The use of media supplemented with MgCl and Casamino acids led to increased cell growth and, importantly, enhanced ST6GalNAc5 and ST6GalNAc6 production. Under optimized conditions, the P. pastoris X-33 strain could secrete up to 10 mg of active sialyltransferase protein per liter of culture. Compared to their wild-type counterparts, mutants of ST6GalNAc5 and ST6GalNAc6 devoid of N-glycosylation sites exhibited reduced enzymatic activity and stability. Apart from contributing to successful P. pastoris expression, our findings also contribute to a deeper understanding of the role of N-glycosylation in the activity and stability of sialyltransferases. KEY POINTS: • Expression of functional human ST6GalNAc5 and ST6GalNAc6 in Pichia pastoris • Mutants devoid of N-glycosylations lack activity • Media supplementation with MgCl2 and Casamino acids improves expression. - Source: PubMed
Publication date: 2025/10/15
Krasnoselska GannaLengyel MartonMatwiejuk MartinVuillemin MarleneMolnar-Gabor DoraMeyer Anne SZeuner Birgitte - Ganglio-series glycosphingolipids (ganglio-GSLs) are biologically important glycolipids comprising a glycan of a ganglio-series nature and a lipid called ceramide. The glycan component often contains one or more sialic acid residues. Accesses to structurally defined ganglio-GSLs remain limited due to their structural complexity and synthetic challenges, hindering both functional studies and therapeutic applications. To overcome the challenges, we report herein a scalable chemoenzymatic total synthesis strategy for the construction of the most comprehensive library of ganglio-GSLs to date. A chiral pool approach was developed for synthesizing simple glycosylsphingosines with desired sphingosine lengths (d18:1 or d20:1) from inexpensive d-xylose. Complex glycosylsphingosines were prepared using enzyme assembly synthetic map (EASyMap)-guided streamlined one-pot multienzyme (OPME) and stepwise OPME (StOPMe) glycosylation strategies facilitated by designing mutants with improved catalytic efficiencies for two key glycosyltransferases (CjCgtA and human ST6GALNAC5). Ganglio-GSLs containing a terminal primary amino group were then prepared by chemical acylation, enabling their covalent immobilization on magnetic beads to form a novel comprehensive ganglio-GSL-bead library encompassing 0-, a-, b-, and c-series ganglio-GSLs including structures containing up to five sialic acid residues with different (α2-3/6/8) sialyl linkages. Multiplex binding assays revealed that ganglio-GSLs exhibit distinctive interactions with glycan-binding proteins including plant lectins, antiganglioside antibodies, bacterial toxins, galectins, and human and mouse siglecs. The integration of streamlined chemoenzymatic total synthesis strategies, glycosyltransferase engineering, covalent immobilization of GSL analogs, and a multiplex assay platform enables synthesis and high-throughput studies of previously difficult-to-obtain ganglio-GSLs. It is broadly applicable to help advance glycobiology and develop GSL-based diagnostics and therapeutics. - Source: PubMed
Publication date: 2025/09/29
Gucchait ArinFu JingxinZhang LiboAgrahari Anand KumarZheng ZiminYang XiaohongYu HaiYang XiaoxiaoVarki AjitChen Xi