Ask about this productRelated genes to: SCUBE2 Blocking Peptide
- Gene:
- SCUBE2 NIH gene
- Name:
- signal peptide, CUB domain and EGF like domain containing 2
- Previous symbol:
- -
- Synonyms:
- Cegf1, Cegb1, FLJ16792
- Chromosome:
- 11p15.4
- Locus Type:
- gene with protein product
- Date approved:
- 2004-05-19
- Date modifiied:
- 2016-04-25
Related products to: SCUBE2 Blocking Peptide
Related articles to: SCUBE2 Blocking Peptide
- Estrogen receptor (ER)-low human epidermal growth factor receptor 2 (HER2)-negative breast cancer shares similar pathological and molecular features with triple-negative breast cancer, yet the utility of the 21-gene assay in this population remains uncertain. This study aimed to evaluate the distribution and molecular drivers of the 21-gene recurrence score (RS) in early breast cancer with low, intermediate, and high ER expression. - Source: PubMed
Publication date: 2026/04/30
Li ShuaiHuang JiahuiZhu YifeiHong JinZhu SijiGao WeiqiHuang OuHe JianrongChen WeiguoLi YafenChen XiaosongShen KunweiWu Jiayi - SCUBE1 and SCUBE2 are vascular-associated proteins involved in endothelial processes. Although these molecules have been investigated in several vascular and inflammatory disorders, their potential involvement in pediatric immunoglobulin A vasculitis (IgAV) has not yet been elucidated. IgAV is the most common systemic vasculitis of childhood, characterized by leukocytoclastic vasculitis and immune complex deposition, yet its biomarker profile remains incompletely understood. We explored the association of SCUBE proteins with inflammatory markers in pediatric IgAV. - Source: PubMed
Publication date: 2026/03/06
Bayir Gulbahar KurtDemir FerhatKarahan Suleyman CanerKalyoncu Mukaddes - Rare brain disorders often present with changes in brain volume, and variation in brain volume is known to be highly heritable. Recent work studying brain volume variation has largely focused on common variants and structural variants. Rare variants often have large effect sizes and clearer connections to biological mechanisms, but the role of rare variants has not been extensively studied. We performed rare-variant gene aggregation analysis for total brain volume and 43 regional brain volume phenotypes (n = 50,061) to identify genes associated with brain volume variation through loss-of-function and missense variants. We identified and replicated mutations in DISP1 and SCUBE2 that were associated with reduced cerebellar volume and suggest that this was mediated by modifying sonic hedgehog signaling. Additionally, we found an association between mutations in PTEN and macrocephaly that are likely mediated through the PI3K/mTOR pathway and hypothesize that mutations in FA2H influence cerebral white matter volume. Further, we identified 7 genes associated with volume variation in the population and rare brain diseases in ClinVar, supporting the role of mutations in these genes causing diseases and related subclinical phenotypes. Overall, we showed that rare-variant analysis can provide clarity on the biological processes connecting brain volume and disease. - Source: PubMed
Publication date: 2026/02/12
Wightman Douglas PMaciel Bernardo A P CBrouwer Rachel Mvan den Heuvel Martijn PPosthuma Danielle - Accumulating evidence has revealed that epithelial-mesenchymal transition (EMT) plays a crucial role in tumor progression and the immune microenvironment, which further results in a high rate of recurrence and metastasis. The EMT immune signaling pathway provides a great perspective for designing personalized therapies. - Source: PubMed
Publication date: 2026/01/19
Liang WeiWang Zi-YingShao Quan-FengLi Yuan-YuanZhu BeiQin Xi-HuChen Wei-Xian - Sonic hedgehog (Shh) morphogens are lipidated proteins that firmly attach to the outer plasma membrane (PM) of the cells that produce them. The process by which Shh is solubilized requires the transmembrane protein Dispatched1 (Disp), the soluble glycoprotein Scube2, the proteolytic removal of lipidated peptide termini, and the use of soluble lipoproteins (LPPs) as Shh transporters. However, their molecular interplay remains controversial. Here, we demonstrate that A Disintegrin and Metalloproteinase 10, Scube2, and Disp act synergistically to remove Shh from the PM and transfer it to LPP acceptors. We also demonstrate physical Scube2 interactions with LPPs and that these interactions increase Shh release. Finally, we demonstrate that Scube2 strongly binds to heparan sulfate (HS) on cell surfaces. These findings reveal Scube2's previously unknown role in binding low-abundance, soluble LPP carriers for Shh and recruiting these carriers to HS-rich Shh release sites at the PM to enhance morphogen release. - Source: PubMed
Publication date: 2026/01/08
Puschmann JSteffes GFroese JManikowski DEhring KWittke JGarbers CWegner S VGrobe K