Use your antibodies-online credentials, if available.
Il n’y a pas de produits dans votre liste de comparaison.
Votre panier est vide.
Afficher toutes les espèces
Afficher tous les synonymes
Sélectionnez vos espèces et l'application
anti-Mouse (Murine) COL4a3 Anticorps:
anti-Rat (Rattus) COL4a3 Anticorps:
anti-Human COL4a3 Anticorps:
Vous arrivez à notre recherche pré-filtrée.
Human Polyclonal COL4a3 Primary Antibody pour IHC, ELISA - ABIN347487
Thevenard, Ramont, Mir, Dupont-Deshorgue, Maquart, Monboisse, Brassart-Pasco: A new anti-tumor strategy based on in vivo tumstatin overexpression after plasmid electrotransfer in muscle. dans Biochemical and biophysical research communications 2013
Show all 2 Pubmed References
Human Polyclonal COL4a3 Primary Antibody pour IF (p), IHC (p) - ABIN678128
Yasuda, Fukui, Okada, Yamawaki: T3 peptide, a fragment of tumstatin, stimulates proliferation and migration of cardiac fibroblasts through activation of Akt signaling pathway. dans Naunyn-Schmiedeberg's archives of pharmacology 2017
Human Polyclonal COL4a3 Primary Antibody pour IF, IHC - ABIN1534339
Faiz, Tjin, Harkness, Weckmann, Bao, Black, Oliver, Burgess: The expression and activity of cathepsins D, H and K in asthmatic airways. dans PLoS ONE 2013
Show all 2 Pubmed References
Human Polyclonal COL4a3 Primary Antibody pour ICC, IF - ABIN4363552
Jeruschke, Jeruschke, DiStasio, Karaterzi, Büscher, Nalbant, Klein-Hitpass, Hoyer, Weiss, Stottmann, Weber: Everolimus Stabilizes Podocyte Microtubules via Enhancing TUBB2B and DCDC2 Expression. dans PLoS ONE 2015
The quality and quantity of alpha3IV-NC1-specific Ab and T cell responses are critical for the phenotype of the glomerulonephritis.
Report novel mouse model of Alport syndrome with accumulation abnormal collagen alpha3alpha4alpha5(IV) trimers in the glomerular basement membrane.
Report monoclonal antibody against the collagen type IV alpha3NC1 domain as a marker for glomerular disease.
Data show that deletion of tumstatin and TSP1 in p53-/- mice leads to increased tumor burden and reduced survival.
the pathogenetic role of USAG-1 in Col4a3-/- mice might involve crosstalk between kidney tubules and the glomerulus and that inhibition of USAG-1 may be a promising therapeutic approach for the treatment of Alport syndrome.
Collagen alpha3(IV) nor alpha4(IV) were detected in the lens capsule 2 weeks postnatal.
Matrix metalloproteinase-9 generated fragments of procollagen, type IV, alpha 3 has endogenous function as integrin-mediated suppressors of pathologic angiogenesis and tumor growth.
Alpha3(IV), alpha4(IV), and alpha5(IV) chains form a complex, which is a heterotrimer, and a defect in complex formation might be one of the molecular mechanisms underlying the pathogenesis of Alport syndrome.
CCR1-mediated recruitment and local activation of macrophages contribute to disease progression in COL4A3-deficient mice. CCR1 is potential therapeutic target for Alport disease or other progressive nephropathies with interstitial macrophage infiltrates.
Upregulation of Lama5 transcription and concentration of laminin alpha1 and alpha5 within (Alport)collagen alpha3(IV) knockout glomerular basement membrane thickenings contribute to abnormal permeabilities.
Collagen alpha 3 alpha 4 alpha 5(IV) originates solely from podocytes; therefore, glomerular Alport disease is a genetic defect that manifests specifically within this cell type.
A single immunization of highly denatured recombinant mouse collagen IV alpha 3 chain noncollagen domain induces severe glomerulonephritis in 100% of Wistar Kyoto rats.
COL4A3/A4/A5 mutations were found in aconsiderable fraction of patients with hereditary nephritis that is difficult to diagnose clinicopathologically.
Our study suggested that polymorphisms in the PIK3CD and COL4A3 were correlated with susceptibility to HAPC in the Tibetan population.
Goodpasture antigen peptide alpha3127-148 was identified as a mutual T and B cell epitope in patients with anti-glomerular basement membrane disease.
Results showed that COL4A4 c.1471C>T and COL4A3 c.3418 + 1G>T variants in cis are pathogenic and co-segregate with the benign familial hematuria. This result suggests that COL4A3 and COL4A4 digenic mutations in cis mimicking an autosomal dominant inheritance should be considered as a novel inheritance pattern of benign familial hematuria.
In a large Spanish family with Alport sysndrome, carriers of certain mutations in the COL4A3 gene were more severely affected and had earlier onset of the disease compared to non-carriers of these mutations.
For mutation screening, all exons of COL4A3 and COL4A4 genes were polymerase chain reaction-amplified and direct sequenced from genomic DNA, and the mutations were analyzed by comparing with members in this family, 100 ethnicitymatched controls and the sequence of COL4A3 and COL4A4 genes from GenBank. A novel mutation determining a nucleotide change was found, i.e. c.4195 A>T (p.Met1399Leu) at 44th exon of COL4A4 gene.
Two families showed COL4A3/A4 mutations in cis, mimicking an autosomal dominant inheritance with a more severe phenotype and one showed COL4A3/A4 mutations in trans, mimicking an autosomal recessive inheritance with a less severe phenotype. In a fourth family, a de novo mutation (COL4A5) combined with an inherited mutation (COL4A3) triggered a more severe phenotype
Alport syndrome is the result of mutations in any of three type IV collagen genes, COL4A3, COL4A4, or COL4A5. Because the three collagen chains form heterotrimers, there is an absence of all three proteins in the basement membranes where they are expressed. (Review)
These findings indicate that the heterozygous mutations in COL4A3 or COL4A4 may cause ESRD on their own, although secondary factors, such as environmental factors or unknown genetic changes, might also contribute to the phenotype of kidney disease in patients with ADAS.
This study indicates that in our population, the COL4A3 rs55703767 polymorphism decreased the risk of KC. However, the TIMP-1 rs6609533 polymorphism was associated with an increased risk of KC.
mutations in COL4A3, COL4A4, and COL4A5 in Chinese patients with Alport Syndrome
COL4A3 gene expression is negatively regulated by ZEB1 binding to E2 box motifs in the COL4A3 promoter region.
COL4A3 expression is significantly downregulated in human masticatory mucosa during wound healing
New COL4A3 mutations among Portuguese patients with collagen IV-related nephropathies were identified in 18 unrelated families.
The results support the hypothesis that certain hypomorphic podocin variants may act as adverse genetic modifiers when co-inherited with COL4A3 mutations
Letter/Case Report: novel COL4A3 gene mutations in a consanguineous family with autosomal recessive Alport syndrome.
we identified seven families with associated mutations in COL4A3 and COL4A4 genes and four families with associated mutations in COL4A4 and COL4A5. We did not find kindreds with digenic inheritance attributable to mutations in COL4A3 and COL4A5
Functional studies in cultured podocytes transfected with wild type or mutant COL4A3 chains showed retention of mutant collagens and differential activation of the unfolded protein response cascade.
We found that 7 out of 70 families (10%) with familial focal segmental glomerulosclerosis in our cohort have rare variants in COL4A3 and COL4A4.
COL4A3 mutations cause focal segmental glomerulosclerosis.
Type IV collagen, the major structural component of basement membranes, is a multimeric protein composed of 3 alpha subunits. These subunits are encoded by 6 different genes, alpha 1 through alpha 6, each of which can form a triple helix structure with 2 other subunits to form type IV collagen. This gene encodes alpha 3. In the Goodpasture syndrome, autoantibodies bind to the collagen molecules in the basement membranes of alveoli and glomeruli. The epitopes that elicit these autoantibodies are localized largely to the non-collagenous C-terminal domain of the protein. A specific kinase phosphorylates amino acids in this same C-terminal region and the expression of this kinase is upregulated during pathogenesis. This gene is also linked to an autosomal recessive form of Alport syndrome. The mutations contributing to this syndrome are also located within the exons that encode this C-terminal region. Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another type IV collagen gene so that each gene pair shares a common promoter.
type IV collagen alpha 3 chain
, collagen alpha-3(IV) chain
, collagen type IV alpha3 chain
, procollagen, type IV, alpha 3
, collagen, type IV, alpha 3 (Goodpasture antigen)
, collagen IV, alpha-3 polypeptide