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FBN1 encodes a member of the fibrillin family. Additionally we are shipping Fibrillin 1 Kits (36) and Fibrillin 1 Proteins (20) and many more products for this protein.
Showing 10 out of 149 products:
Cow (Bovine) Monoclonal Fibrillin 1 Primary Antibody for IHC (fro), IF - ABIN356182
Sakai, Keene, Engvall: Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils. in The Journal of cell biology 1987
Show all 3 references for ABIN356182
Human Polyclonal Fibrillin 1 Primary Antibody for IHC, IHC (p) - ABIN4311653
Zhang, Ota, Shridhar, Chien, Wu, Kuang: Network-based survival analysis reveals subnetwork signatures for predicting outcomes of ovarian cancer treatment. in PLoS computational biology 2013
Show all 3 references for ABIN4311653
Cow (Bovine) Monoclonal Fibrillin 1 Primary Antibody for IEM, IHC (fro) - ABIN356181
Wright, McDaniels, Swasdison, Accavitti, Mayne, Mayne: Immunization with undenatured bovine zonular fibrils results in monoclonal antibodies to fibrillin. in Matrix biology : journal of the International Society for Matrix Biology 1994
Show all 3 references for ABIN356181
Cow (Bovine) Monoclonal Fibrillin 1 Primary Antibody for ICC, IF - ABIN259623
Shin, Lee, Kim, Kum, Jung, Park: Anti-glycation activities of phenolic constituents from Silybum marianum (Milk Thistle) flower in vitro and on human explants. in Molecules (Basel, Switzerland) 2015
Show all 2 references for ABIN259623
Cow (Bovine) Polyclonal Fibrillin 1 Primary Antibody for WB - ABIN2780329
Uyeda, Takahashi, Eto, Sato, Xu, Kanezaki, Toki, Yonesaka, Ito: Three novel mutations of the fibrillin-1 gene and ten single nucleotide polymorphisms of the fibrillin-3 gene in Marfan syndrome patients. in Journal of human genetics 2004
Data suggest that genetic fibrillin-1 deficiency could alter normal endothelial signaling.
In cases of vascular calcification, the decreased expression of FBN1 may be partially responsible for decreased vascular elasticity and also for the decreased formation of new elastic fibers.
The coordinate upregulation of fibrillin-1 and fibrillin-2 (show FBN2 Antibodies) expression with the onset of tropoelastin (show ELN Antibodies) production is consistent with a role in elastic fiber assembly.
a calcium-binding epidermal growth factor (show EGF Antibodies)-like domain of fibrillin-1 c.3598G > A, p.E1200K mutation is responsible for a bovine model of Marfan syndrome
This is the first study to investigate the expression and localization of fibrillin proteins and latent TGF-beta (show TGFB1 Antibodies) binding proteins affecting TGFbeta (show TGFB1 Antibodies) bioavailability in the ovary.
FBN1 gene mutation is associated with Marfan syndrome.
Results showed two novel mutations in exon 12 and 50 of FBN1 identified in two Chinese family members with Marfan syndrome (MFS) which may be responsible for cardiovascular manifestations.
The results expand the FBN1 mutation spectrum and enrich our knowledge of genotype-phenotype correlations. Genetic testing for MFS and its related aortic diseases is increasingly important for early intervention and treatment.
miR (show MLXIP Antibodies)-486-5p induces papillary thyroid carcinoma cell growth inhibition and apoptosis by targeting and suppressing FBN1.
information of genotype-phenotype correlation owing to FBN1 mutations; the same FBN1 mutation, c. 1633C>T (Arg545Cys), was detected simultaneously in three different cardinal (show CARD8 Antibodies) phenotypes (ectopia lentis, aortic dissection and unaffected) within one family.
Data show that interaction of fibrillin-1 with the bone morphogenetic protein 7 (BMP-7 (show BMP7 Antibodies)) complex results in a conformational change.
Authors discovered a protein hormone that regulates glucose homeostasis. It is the C-terminal cleavage product of profibrillin (encoded by FBN1). Its absence in humans results in a unique pattern of metabolic dysregulation that includes partial lipodystrophy, accompanied by reduced plasma insulin (show INS Antibodies), while maintaining euglycemia.
A marked decrease in heart rate variability, documented in the study, may be an important clinical feature in MS patients with confirmed FBN1 mutations.
The R2726W FBN1 variant is associated with skeletal features of Marfan syndrome.
New insights into the structure, assembly and biological roles of 10-12 nm connective tissue microfibrils from fibrillin-1 studies.
These results suggest that both fibrillin-1 and fibrillin-2 (show FBN2 Antibodies) expression is required to form thick oxytalan fibers in periodontal ligament.
findings show that fibrillin-1 regulates MSC (show MSC Antibodies) activity by modulating TGFbeta (show TGFB1 Antibodies) bioavailability within the microenvironment of marrow niches.
Fibrillin-1 mgDelta(lpn) Marfan syndrome mutation associates with preserved proteostasis and bypass of a protein disulfide isomerase (show P4HB Antibodies)-dependent quality checkpoint
fibrillin-1 deficiency is associated with relevant dysfunction of the endothelial barrier that enables adenovirus to induce vessel-harming inflammation.
the Fbn1(C1039G/+) mouse model demonstrates mild intrinsic left ventricular dysfunction
This study demonstrated that dysfunctional fibrillin-1 impairs blood-brain barrier permeability /BCSFB integrity, facilitating peripheral leukocyte infiltration, which further degrades the BBB (show ALMS1 Antibodies)/BCSFB.
The review discuss FBN1 point mutations on the structure and function of the protein associated with Marfan syndrome in affected patients impairing protein folding and traficking, secretion, proteolysis or heparin binding.
The concomitant induction of both fibrillin-1 and alpha8 integrin in a self-limited model of glomerular injury points to a protective role of the interaction of fibrillin-1 with alpha8 integrin in the glomerulus.
Data show that fibrillin-1 (FBN1) modulates bone marrow mesenchymal stem cells (BMMSCs) lineage differentiation via IL4 receptor alpha (show IL4R Antibodies)/mTOR (show FRAP1 Antibodies) protein signaling.
latent transforming growth factor-beta-1 (show TGFB1 Antibodies) binding protein-2 was prominently associated with annular fibrils containing fibrillin-1
This gene encodes a member of the fibrillin family. The encoded protein is a large, extracellular matrix glycoprotein that serve as a structural component of 10-12 nm calcium-binding microfibrils. These microfibrils provide force bearing structural support in elastic and nonelastic connective tissue throughout the body. Mutations in this gene are associated with Marfan syndrome, isolated ectopia lentis, autosomal dominant Weill-Marchesani syndrome, MASS syndrome, and Shprintzen-Goldberg craniosynostosis syndrome.
, fibrillin 15
, fibrillin 1 (Marfan syndrome)
, tight skin