SUMF1
- Known as:
- SUMF1
- Catalog number:
- Y214327
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- SUMF1
Related genes to: SUMF1
- Gene:
- SUMF1 NIH gene
- Name:
- sulfatase modifying factor 1
- Previous symbol:
- -
- Synonyms:
- FGE, UNQ3037
- Chromosome:
- 3p26.1
- Locus Type:
- gene with protein product
- Date approved:
- 2004-04-30
- Date modifiied:
- 2014-11-18
Related products to: SUMF1
Antibodies: SUMF1 HOST: Goat Clonality: pAbAntigens SUMF1, 91-374aa, Human, His tag, E.coli, RecombinantBos taurus,Bovine,C-alpha-formylglycine-generating enzyme 1,Sulfatase-modifying factor 1,SUMF1Bovine sulfatase modifying factor 1 (SUMF1) ELISA kit, Species Bovine, Sample Type serum, plasmaBovine Sulfatase-modifying factor 1(SUMF1) ELISA kitBovine Sulfatase-modifying factor 1(SUMF1) ELISA kit SpeciesBovineC-alpha-formylglycine-generating enzyme 1,FGE,Homo sapiens,Human,PSEC0152,Sulfatase-modifying factor 1,SUMF1,UNQ3037_PRO9852C-alpha-formylglycine-generating enzyme 1,Fge,Mouse,Mus musculus,Sulfatase-modifying factor 1,Sumf1Cytoskeleton: SUMF1, 91-374aa, Human, His tag, E.coliCytoskeleton: SUMF1, 91-374aa, Human, His tag, E.coliELISA Kit for Sulfatase Modifying Factor 1 (SUMF1)ELISA Kit for Sulfatase Modifying Factor 1 (SUMF1)ELISA Kit for Sulfatase Modifying Factor 1 (SUMF1) Homo sapiens (Human)ELISA Kit for Sulfatase Modifying Factor 1 (SUMF1) Organism Homo sapiens (Human)ELISA Kit for Sulfatase Modifying Factor 1 (SUMF1) Organism: Homo sapiens (Human) Related articles to: SUMF1
- Convergence and extension (C&E) cell movements that elongate the primary embryonic axis are precisely timed during vertebrate gastrulation, but mechanisms controlling their onset remain unknown. Using zebrafish embryonic explants that recapitulate C&E and its timing, we identified sulfatase modifying factor 2 (sumf2) as a candidate trigger gene for C&E onset. sumf2 and its paralog sumf1 encode negative and positive sulfatase regulators, respectively, whose expression levels invert and increase heparan sulfate sulfation during gastrulation. Overexpressing sumf1 or sumf2 causes delayed or precocious C&E, respectively, whereas their loss shifts C&E timing in the opposite direction. We identified Sulf1, a modifier of heparan sulfate proteoglycans (HSPGs), as their key downstream effector and found that altering heparan sulfate sulfation levels shifts C&E onset and suppresses sumf1 and sumf2 mutant phenotypes. This work supports a model in which sumf2 expression reduces sulfatase activity, rewriting HSPG sulfation patterns to promote the onset of C&E morphogenesis. - Source: PubMed
Publication date: 2026/03/31
Cervino Ailen SoledadBasu AmritaWeiss Ryan JKaur Bajwa GursimranMarín-Juez RubénGrimm Sandra LCoarfa CristianWilliams Margot Kossmann - The complex metabolic and immune characteristics of ovarian cancer and their interconnections can promote tumor immune evasion, ultimately leading to immunotherapy failure. A comprehensive understanding of these relationships can inform the development of diagnostic markers and more effective therapeutics. - Source: PubMed
Publication date: 2025/12/24
Yu HongkaiYou ChangXu TingZhao ZiyanWang DanyangHu LuDai LiangzheZheng WanlinWang LuyaoJi MinghuiZhuang TianchiYang Yingqi - To shape the emerging body plan, morphogenetic cell movements must be coordinated not only in space, but also in time. Convergence and Extension (C&E) movements that elongate the anteroposterior axis initiate with precise timing during vertebrate gastrulation, but the mechanisms controlling their onset remain unknown. We examined this question using zebrafish embryonic explants that faithfully recapitulate C&E cell movements and their precise timing in culture, in isolation from other gastrulation movements. We determined that new transcription is required at gastrulation onset for C&E in explants and identified () as a candidate 'trigger' gene expressed at this time. and its paralog encode negative and positive regulators, respectively, of all sulfatase enzymes, which remove sulfate groups from their substrates, altering their biological activity. In zebrafish embryos and explants, expression levels invert at gastrulation onset, predicting a reduction in sulfatase activity and consequent increase of substrate sulfation. We found that overexpressing and causes delayed or precocious C&E onset, respectively, whereas loss of and function shifts C&E timing in the opposite direction. We further identified Sulf1, an extracellular sulfatase that modifies heparan sulfate proteoglycans (HSPGs), as the key effector by which and control C&E timing. Accordingly, reduced or increased levels of sulfated heparan sulfate similarly shift C&E onset and suppress and mutant phenotypes. Together, our work supports a model in which expression at zebrafish gastrulation onset reduces sulfatase activity, rewriting HSPG sulfation patterns to promote and/or permit C&E morphogenesis. - Source: PubMed
Publication date: 2025/10/24
Cervino Ailen SoledadBasu AmritaWeiss Ryan JBajwa Gursimran KaurJuez Rubén MarínGrimm SandraCoarfa CristianWilliams Margot Kossmann - This study investigated whether specific () SNPs-previously linked to lung function-are associated with COPD progression and response to inhaled corticosteroid (ICS) treatment, specifically budesonide, given that expression is altered in COPD and its variants linked to increased disease risk. A subgroup of 165 COPD patients from the HISTORIC study were genotyped for two common SNPs, rs11915920 and rs793391. Patients first underwent a six-week run-in phase with open-label triple inhaled therapy (LAMA/LABA/ICS), then were randomized to receive either LAMA/LABA/placebo or LAMA/LABA/ICS for 12 months. Associations between SNPs, baseline characteristics, and response to ICS-based on FEV change over 12 months-were evaluated. Heterozygotes (TG) for the rs793391 polymorphism treated with LAMA/LABA/ICS showed a significant and clinically meaningful FEV improvement compared to the placebo group. This was supported by improved patient-reported outcomes, with lower SGRQ and CAT scores and a clinically relevant increase in General Health Questionnaire scores. These findings suggest that rs793391 may be linked to both COPD progression and ICS response and could contribute to more personalized treatment strategies in COPD. - Source: PubMed
Publication date: 2025/10/21
Ntenti CharikleiaPapakonstantinou EleniGrize LeticiaPascarella MariaFrye Björn CFähndrich SebastianIoannidou DespoinaSavic Prince SpasenijaGoulas AntonisStolz Daiana - SULF1, a human extracellular heparan 6-O-endosulfatase isoform 1, plays a critical role in embryonic development and cancer progression by modulating the 6-O-sulfation of heparan sulfate proteoglycans. However, limited recombinant protein production has hindered structural and functional characterization. To address this issue, we optimized SULF1 expression in HEK293F and HEK293T cells. We achieved yields of 2.2 mg/L of culture media after Ni2+-affinity purification of greater than 80% purity, representing a substantial improvement compared to the reported expression systems. We demonstrated that co-expression of sulfatase-modifying factor 1 in this expression system is essential for enhancing SULF1 enzymatic activity, which depends on conversion of active site cysteine to Cα-formylglycine and the presence of a Ca2+ ion. We further showed that a marine fucosylated chondroitin sulfate polymer isolated from the sea cucumber Holothuria floridana inhibits SULF1 enzymatic activity with IC50 of 0.05 ± 0.006 μg/mL and 0.07 ± 0.008 μg/mL for the GlcNS6S-GlcA-GlcNS6S-IdoA2S-GlcNS6S-IdoA2S-GlcNS6S-GlcA and 4-methylumbelliferyl sulfate substrates, respectively. Kinetic analysis revealed a mixed-mode inhibition, characterized by alterations in Vmax at all inhibitor concentrations and Km at high inhibitor concentrations. Efficient SULF1 production also enabled us to develop specific monoclonal antibodies, which confirmed SULF1 expression in the stroma of head and neck squamous cell cancer tissues. Collectively, this study provides an efficient workflow for the production of active human SULF1, investigates SULF1 inhibitors, and characterizes anti-SULF1 monoclonal antibodies, which will support further studies of this enzyme in various pathophysiological conditions. - Source: PubMed
Aljuhani ReemBenicky JuliusPanigrahi AswiniMukherjee PrithaSanda MiloslavZhu ShiyaNováková ZoraPomin Vitor HLiu JianDavidson BruceBařinka CyrilGoldman Radoslav