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FBN1 encodes a member of the fibrillin family. Additionally we are shipping Fibrillin 1 Antibodies (145) and Fibrillin 1 Proteins (20) and many more products for this protein.
Showing 10 out of 34 products:
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 ELISA Kits) expression with the onset of tropoelastin (show ELN ELISA Kits) production is consistent with a role in elastic fiber assembly.
a calcium-binding epidermal growth factor (show EGF ELISA Kits)-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 ELISA Kits) binding proteins affecting TGFbeta (show TGFB1 ELISA Kits) bioavailability in the ovary.
miR (show MLXIP ELISA Kits)-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 ELISA Kits) 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 ELISA Kits)) 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 ELISA Kits), 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.
Also, expansion of the mutation spectrum in FBN1 will be helpful in genetic counselling for Chinese patients with STAAD.
Data suggest that fibrillin-1 and ATP1B3 (show ATP1B3 ELISA Kits) are binding partners of BST-2 (show BST2 ELISA Kits); fibrillin-1 (unlike ATP1B3 (show ATP1B3 ELISA Kits)) restricts of HIV-1 replication in a mechanism independent of BST-2 (show BST2 ELISA Kits).
Data suggest that MFAP4 (microfibrillar-associated protein 4 (show MFAP4 ELISA Kits)) binds tropoelastin (show ELN ELISA Kits), fibrillin-1/-2, and elastin (show ELN ELISA Kits) cross-linking amino acid desmosine; MFAP4 (show MFAP4 ELISA Kits) co-localizes with fibrillin-1-positive fibers; MFAP4 (show MFAP4 ELISA Kits) promotes tropoelastin (show ELN ELISA Kits) self-assembly.
These results suggest that both fibrillin-1 and fibrillin-2 (show FBN2 ELISA Kits) expression is required to form thick oxytalan fibers in periodontal ligament.
findings show that fibrillin-1 regulates MSC (show MSC ELISA Kits) activity by modulating TGFbeta (show TGFB1 ELISA Kits) 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 ELISA Kits)-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 ELISA Kits)/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 ELISA Kits)/mTOR (show FRAP1 ELISA Kits) protein signaling.
latent transforming growth factor-beta-1 (show TGFB1 ELISA Kits) 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