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Heparan sulfate proteoglycans (HSPGs) act as coreceptors for numerous heparin-binding growth factors and cytokines and are involved in cell signaling. Zusätzlich bieten wir Ihnen Sulfatase 2 Antikörper (92) und Sulfatase 2 Kits (23) und viele weitere Produktgruppen zu diesem Protein an.
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Sulf2 expression is almost entirely restricted to the CNS.
SULF2 promotes the growth and metastasis of CRC probably by activating Akt and Erk1/2 pathways.
Although no change in SULF2 was detected in squamous cell carcinoma of the head and neck (HNSCC) serum, its detection in saliva (zeige RAG1AP1 Proteine) makes it worthy of further investigation as a potential HNSCC biomarker.
results demonstrated that SULF2 can mediate the detrimental effects of ionizing radiation in vivo
The short variants of Sulf2 promoted FGF2 (zeige FGF2 Proteine)-induced MDA-MB231 and MCF7 in vitro growth while full-length Sulf1 (zeige SULF1 Proteine) inhibited growth supporting in vivo mammary tumour cell signalling patterns of growth.
Most pancreatic ductal adenocarcinomas had positive SULF2 staining in tumour cells and intratumoural or tumour-adjacent stroma. Elevated SULF2 in PDAC was associated with advanced tumour stage, vascular invasion, shorter interval to radiological progression and shorter overall survival.
The SULF1/SULF2 (zeige SULF1 Proteine) activation thus does not only promote regulated foetal growth and injury-induced liver regeneration but also dysregulated tumour growth.
Sulf2 facilitated lymphangiogenesis in breast cancer cells by regulating VEGF-D (zeige Figf Proteine) and that the AKT1related signaling pathway was involved.
renal cell carcinoma (zeige MOK Proteine) with lower SULF-2 expression might have a higher potential for cell invasion and proliferation, leading to a poorer prognosis via the activation of VEGF (zeige VEGFA Proteine) and/or FGF signaling
SULF2 is a multifaceted protein involved in triglyceride-rich lipoprotein homeostasis and angiogenesis. [review]
Our data confirmed that Sulf2 promoted breast cancer progression and regulated the expression of tumor-related genes in breast cancer.
Sulf1 (zeige SULF1 Proteine) and Sulf2 play indispensable roles to maintain glomerular integrity and protective roles in diabetic nephropathy, probably by growth factor modulation.
Expression of the heparan sulfate 6-O-endosulfatases, Sulf1 (zeige SULF1 Proteine) and Sulf2, in the avian and mammalian inner ear suggests a role for sulfation during inner ear development.
It is proposed that Sulf1 (zeige SULF1 Proteine), Sulf2 and ErbB1 (zeige EGFR Proteine) are involved in the inhibition of neurite outgrowth and may regulate structural plasticity and regeneration in the nervous system.
Sulf1 (zeige SULF1 Proteine)/, but not Sulf2/, mice, exhibited a marked delay in healing of corneal epithelial wounds.
SULF2 regulates tissue regeneration in part via the activation of a novel WNT (zeige WNT2 Proteine)-GLI1 (zeige GLI1 Proteine)-CYCLIN D1 (zeige CCND1 Proteine) pathway.
Sulf1 (zeige SULF1 Proteine) and Sulf2 differentially contribute to the generation of organ-specific sulfation patterns of heparan sulfate.
Heparan sulfate sulfatase (zeige SGSH Proteine) SULF2 regulates PDGFRalpha signaling and growth in human and mouse malignant glioma
Sulf-1 (zeige SULF1 Proteine) and Sulf-2 are essential regulators of GDNF signaling in the SSC (zeige CYP11A1 Proteine) niche and direct downstream targets of Sertoli cell-specific transcriptional factor Wilm's tumor 1.
SULF2 is an unexpected suppressor of atherogenic lipoprotein clearance by hepatocytes
These results reveal that Sulf1 (zeige SULF1 Proteine) and Sulf2 fulfil non-redundant functions in vivo in the development and maintenance of the murine nervous system.
Heparan sulfate proteoglycans (HSPGs) act as coreceptors for numerous heparin-binding growth factors and cytokines and are involved in cell signaling. Heparan sulfate 6-O-endosulfatases, such as SULF2, selectively remove 6-O-sulfate groups from heparan sulfate. This activity modulates the effects of heparan sulfate by altering binding sites for signaling molecules (Dai et al., 2005
, extracellular sulfatase Sulf-2-like
, extracellular sulfatase Sulf-2
, sulfatase FP2a
, sulfatase FP2b
, sulfatase FP2