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Human Monoclonal HPSE2 Primary Antibody pour ICC, FACS - ABIN438798
Bonner, Kerr-Conte, Gmyr, Queniat, Moerman, Thévenet, Beaucamps, Delalleau, Popescu, Malaisse, Sener, Deprez, Abderrahmani, Staels, Pattou: Inhibition of the glucose transporter SGLT2 with dapagliflozin in pancreatic alpha cells triggers glucagon secretion. dans Nature medicine 2015
Show all 4 Pubmed References
study of tissue expression profiles, polymorphisms of HPSE and HPSE2 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 mRNA did not induce a prominent change in PAMs
The results of this study the Heparanase 2 appeared overexpressed at different stages of Alzheimer disease.
our results suggest that heparanase 2 functions as a tumor suppressor in bladder cancer
we provide evidence that Hpa2 overexpression in head and neck cancer cells markedly reduces tumor growth
The most common HPA genotypes among Saudis were HPA-1 a + b- (75%), HPA-2 a + b- (62%), HPA-3 a + b- (51.5%), HPA-4 a + b- (99%), HPA-5 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.
Our findings identified these 2 genes as a novel breast cancer biomarker gene set, which may facilitate the diagnosis and treatment in breast cancer clinical therapies.
HPSE2 mutations were found in one Urofacial syndrome family but not detected in patients with non-neurogenic neurogenic bladder and severe lower urinary tract dysfunction
Heparanase 2 is more intensely expressed in the glandular tissue of cancer than in nonneoplastic endometrium; the HPSE2 expression in the stromal tissue is higher in the nonneoplastic controls compared with cancer mainly in the secretory endometrium.
autonomic neural protein implicated in bladder emptying
High expression of heparanase-2 is associated significantly with gastric tumor growth and differentiation
Data indicate that the overexpression of HPSE1 and HPSE2 in the intervertebral degenerated discs suggests a role for these factors in mediating extracellular matrix remodeling in degenerative discs during disease development.
HPSE2 c.631T>C (p.Y211H) is a novel benign SNP and c.1628A>T (p.N543I) is the disease-causing mutation in urofacial syndrome.
A large region of marker homozygosity was observed at 10q24, consistent with known autosomal recessive inheritance, family consanguinity and previous genetic mapping in other families with Ochoa syndrome.
Studies indicate that cathepsin L as the heparanase activating protease.
These results indicate a regulatory effect of heparanase on TFPI and TFPI-2 in trophoblasts, suggesting a potential involvement of heparanase in early miscarriages.
We now report evidence that Heparanse 2 (HPSE2) is the culprit gene for the syndrome. Mutations with a loss of function in the Heparanase 2 (HPSE2) gene
Homozygous exonic deletions, nonsense mutations, and frameshift mutations in five further unrelated families confirmed HPSE2 as the causative gene for UFS
Results demonstrated that the effectors from heparanase peptide-immunized mice could effectively lyse various tumor cells that were heparanase positive and HLA-A*0201 matched.
Heparanase 2 is involved in neoplastic proliferation, but it was not exclusively associated with the malignant process.
Heparanase may facilitate invasion and metastasis of gastric carcinoma cells.
Study demonstrating that increased heparanase expression in prostate cancer tissues is due to promoter hypomethylation and up-regulation of transcription factor EGR1.
Deletion of Hpse2 cause the urofacial syndrome-like phenotype in mice.
This gene encodes a heparanase enzyme. The encoded protein is a endoglycosidase that degrades heparin sulfate proteoglycans located on the extracellular matrix and cell surface. This protein may be involved in biological processes involving remodeling of the extracellular matrix including angiogenesis and tumor progression. Alternate splicing results in multiple transcript variants.
, heparanase 3
, heparanase-like protein
, inactive heparanase-2