Sulf2 Blocking Peptide
- Known as:
- Sulf2 Blocking Peptide
- Catalog number:
- x1853b
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Exalpha
- Gene target:
- Sulf2 Blocking Peptide
Related genes to: Sulf2 Blocking Peptide
- Gene:
- SULF2 NIH gene
- Name:
- sulfatase 2
- Previous symbol:
- -
- Synonyms:
- KIAA1247, HSULF-2, SULF-2
- Chromosome:
- 20q13.12
- Locus Type:
- gene with protein product
- Date approved:
- 2004-01-26
- Date modifiied:
- 2016-04-25
Related products to: Sulf2 Blocking Peptide
Related articles to: Sulf2 Blocking Peptide
- - Source: PubMed
Publication date: 2026/09/24
Vicente Carolina MLima Marcelo ANader Helena BToma Leny - Pathways controlling cardiac cell behavior share a common dependency on heparan sulfate proteoglycans (HSPGs), which tightly regulate signaling at extracellular locations. This signaling is essential for cardiac development, yet how HSPGs are regulated in the forming heart is unknown. The epicardium is a rich source of HSPG-dependent signaling and cellular progenitors. We hypothesized that extracellular heparan sulfate modifiers, 6--endosulfatases, orchestrate progenitor cell behavior to support cardiogenesis. - Source: PubMed
Publication date: 2026/08/25
Redpath Andia NLupu Irina-ElenaHaffreingue LouisDang Quang MMcCracken Ian RCarsana Tamaravan Kuppevelt Toin HVieira Joaquim MiguelSmart Nicola - The amino acid sequence requirements that instruct the modification of proteins with chondroitin sulfate (CS) have been unknown, precluding predictions or opportunities for precise protein engineering. This study identified an essential amino acid motif for CS addition, the "CS-sequon" (EDQDDKDGGDFSGWGG), by comparing the secreted sulfatases SULF1 and SULF2, where only SULF2 is CS-modified. A cluster of seven amino acids plus a nearby tryptophan are critical for CS attachment; inserting the CS-sequon into SULF1 enabled it to gain CS modification. This sequon recruits the activity of the CS-initiating xylosyltransferase to the peptide modification site and CS addition enhances SULF1/2 extracellular abundance and enzymatic activity. These findings were validated across human and non-human cells and in Drosophila, providing a foundational resource for engineering CS modifications into proteins. - Source: PubMed
Publication date: 2026/07/16
Takeda-Uchimura YoshikoIshihara-Aoki MayumiMoriya AyanoNishitsuji KazuchikaMizumoto ShujiIkezaki MidoriTakechi-Haraya YukiNakato ErikoLemjabbar-Alaoui HassanAllain FabriceIhara YoshitoYamada ShuheiTiemeyer MichaelNakato HiroshiAoki KazuhiroUchimura Kenji - Heparan sulfate proteoglycans are central modulators of cell-cell communication, largely through the information encoded in their sulfation patterns. Among extracellular regulators of this 'heparan sulfate code', the endosulfatases SULF1 and SULF2 have emerged as unique enzymes with the capacity to selectively remove 6-O-sulfate groups from heparan sulfate (HS) glucosamine residues. This activity distinguishes them from canonical lysosomal sulfatases and positions them as critical editors of HS from the extracellular matrix and cell-surface. Recent biochemical studies have highlighted their distinctive domain organization, extensive post-translational modifications, and finely tuned substrate specificity, revealing that 6-O-desulfation is a non-random, highly regulated process. Functionally, SULFs influence major signaling pathways and thereby participate in diverse biological processes, such as development, tissue homeostasis, injury repair, inflammation, and tumor progression. Accumulating evidence also implicates SULF1 and SULF2 in disease pathogenesis and highlights them as promising, yet underexplored, therapeutic targets. In the present review, we provide an updated perspective on SULF biology, emphasizing recent advances in functional characterization, their roles as extracellular 'code editors', and the therapeutic opportunities that may arise from targeting their activity. We also address several key questions that remain unresolved and that are needed to understand this complex mechanism of regulation. - Source: PubMed
Boustany Rebecca-JoeVallet Sylvain DAwad YaraGout EvelyneWild RebekkaVivès Romain R - Long-term survival of lung transplant recipients remains limited by chronic lung allograft dysfunction (CLAD). CLAD is only diagnosed following a persistent and substantial decline in lung function, after which irreversible damage to the lungs has occurred, limiting opportunities to effectively intervene at an early stage. There is a critical need for earlier detection prior to its clinical manifestation. The immunological drivers of CLAD remain unclear, limiting the development of predictive biomarkers and new therapies. - Source: PubMed
Publication date: 2026/06/23
Iacono GiuliaBegka ChristinaCardwell BaileyDaunt CarmelChatzis RoxannePattaroni CelineButler AlanaMacowan MatthewLevvey BronwynSnell Gregory IWestall Glen PMarsland Benjamin J