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Human Monoclonal HPSE Primary Antibody für ICC, FACS - ABIN438793
Dorrell, Abraham, Lanxon-Cookson, Canaday, Streeter, Grompe: Isolation of major pancreatic cell types and long-term culture-initiating cells using novel human surface markers. in Stem cell research 2009
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Human Polyclonal HPSE Primary Antibody für WB - ABIN3042457
Tang, Zhang, Zhao, Wang, Lu, Song, Zhao, Kang, Wang, Xu, Tian: The expression and clinical significance of microRNA-1258 and heparanase in human breast cancer. in Clinical biochemistry 2013
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Human Polyclonal HPSE Primary Antibody für WB - ABIN3043707
Tang, Piao, Zhao, Mu, Li, Ma, Song, Wang, Zhao, Zhang: Expression and correlation of matrix metalloproteinase-9 and heparanase in patients with breast cancer. in Medical oncology (Northwood, London, England) 2014
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Data demonstrate that the mesenchymal features induced by HPSE in MM cells contribute to enhanced tumor cell motility and bone-dissemination.
c-Myc (zeige MYC Antikörper) and heparanase expression was positively correlated with hTERT levels, and was also an independent predictor of metastasis and survival.
miR (zeige MLXIP Antikörper)-558 facilitates the progression of gastric cancer through directly targeting the HPSE promoter to attenuate Smad4 (zeige SMAD4 Antikörper)-mediated repression of HPSE expression.
High HPSE expression is associated with breast carcinoma.
data suggest that heparanase plays a critical role in NK cell invasion into tumors and thereby tumor progression and metastases.
The heparanase/syndecan1 (zeige SDC1 Antikörper) axis in gallbladder carcinoma cells plays an important role in the invasion and metastasis, thus providing a new therapeutic target.
Results show that HPSE is upregulated in human glioma and seems to confer a growth advantage on glioma cells.
under physiological pH and low levels of tissue factor (zeige F3 Antikörper), heparanase may exert a non-enzymatic function interacting and activating the inhibitory function of antithrombin (zeige SERPINC1 Antikörper).
Heparanase has emerged as a major regulator of cancer by degrading heparan sulfate thereby influencing multiple signaling pathways that control gene expression, syndecan (zeige SDC1 Antikörper) shedding and cell behavior. (Review)
The most common HPA genotypes among Saudis were HPA-1 a + b- (75%), HPA-2 (zeige HPSE2 Antikörper) a + b- (62%), HPA-3 a + b- (51.5%), HPA-4 a + b- (99%), HPA-5 (zeige ITGA2 Antikörper) a + b- (76.5%), HPA-6 a + b- (100%) and HPA-15 a + b + (50%). The prevalent allele among the HPA systems was (a), except in the HPA-15 system where the (b) allele was found in 52% of the subjects.
eNOS (zeige NOS3 Antikörper) prevents heparanase induction and the development of proteinuria
Data show that heparanase-1 (HPA-1) induced shedding of heparan sulfate chain from syndecan-1 (SDC-1 (zeige SDC1 Antikörper)) facilitated the release of vascular endothelial growth factor C (VEGF-C (zeige VEGFC Antikörper)) from SDC-1 (zeige SDC1 Antikörper)/VEGF-C (zeige VEGFC Antikörper) complex into the medium of hepatocarcinoma cell.
the activation of intestinal heparanase contributes to intestinal injury during early sepsis by facilitating the destruction of mucosal epithelial glycocalyx and promoting inflammatory responses.
Heparanase increases the inflammation in AGEs-stimulated macrophages through activating the RAGE (zeige AGER Antikörper)-NF-kappaB (zeige NFKB1 Antikörper) pathway. Heparanase driven inflammation from AGEs-stimulated macrophages increases the adherence of glomerular endothelial cells (GEnCs) and augments the permeability of GEnCs.
heparanase contributes to allergen-induced eosinophil recruitment to the lung.
Unfractionated heparin inhibits heparanase, and reverses the activation of NF-kappaB (zeige NFKB1 Antikörper) and MAPK P38 (zeige MAPK1 Antikörper) signaling pathways to attenuate inflammatory responses induced by sepsis. These results suggest that UFH
Results show a critical role for heparanase in regulating the branching and invasive behavior of normal mammary epithelia which could be the result of its mutually reciprocal feedback with MMP-14 (zeige MMP14 Antikörper).
Data suggest a potential mechanism of diabetic enteropathy, which is depending remarkably on syndecan-1 (Sdc1 (zeige SDC1 Antikörper)) and -beta-D-glucuronidase (zeige GUSB Antikörper) heparanase (HPSE).
Findings identify a dual function for HPSE in malignant melanoma with a protumorigenic extracellular activity and a tumor-suppressive nuclear action.
Studies in heparanase-deficient mice established its contributions to autophagy.
These data suggest that porcine reproductive and respiratory syndrome virus activates NF-kappaB (zeige NFKB1 Antikörper) and cathepsin L to upregulate and process heparanase, and then the active heparanase cleaves heparan sulfate, resulting in viral release.
during late gestation, the mRNA and HPSE levels were higher in Meishan placentae than Yorkshire pigs
study of tissue expression profiles, polymorphisms of HPSE and HPSE2 (zeige HPSE2 Antikörper) genes and changes of their mRNA levels in porcine alveolar macrophages (PAMs) induced by PRRSV; upon stimulation in healthy piglets with PRRSV, HPSE mRNA was obviously upregulated, while HPSE2 (zeige HPSE2 Antikörper) mRNA did not induce a prominent change in PAMs
our results support a critical role for heparanase in the development of vulnerable atherosclerotic plaques
report molecular cloning and characterisation of heparanase mRNA in the porcine placenta throughout gestation.
Suggest that high glucose is a potent stimulator of endothelial heparanase secretion.
Lutropin (zeige LHB Antikörper) induces a transient increase in HPSE mRNA at specific times after its addition.
Heparan sulfate proteoglycans are major components of the basement membrane and extracellular matrix. The protein encoded by this gene is an enzyme that cleaves heparan sulfate proteoglycans to permit cell movement through remodeling of the extracellular matrix. In addition, this cleavage can release bioactive molecules from the extracellular matrix. Several transcript variants encoding different isoforms have been found for this gene.
, endoglycosidase heparanase