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The protein encoded by FBN2 is a component of connective tissue microfibrils and may be involved in elastic fiber assembly. Additionally we are shipping Fibrillin 2 Antibodies (72) and Fibrillin 2 Proteins (4) and many more products for this protein.
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The coordinate upregulation of fibrillin-1 (show FBN1 ELISA Kits) and fibrillin-2 expression with the onset of tropoelastin (show ELN ELISA Kits) production is consistent with a role in elastic fiber assembly.
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.
The presence of the splice site mutation in FBN2 gene has been confirmed in a Japanese family with congenital contractural arachnodactyly complicated with aortic dilatation and dissection.
DNA sequence variation within the FBN2 gene is associated with both Achilles tendon (AT) and anterior cruciate ligament (ACL (show ACLY ELISA Kits)) rupture.
Rare and common variants in extracellular matrix gene Fibrillin 2 (FBN2) are associated with macular degeneration.
we demonstrate an important role for FBN1 (show FBN1 ELISA Kits) and FBN2 in AIS (show AR ELISA Kits) pathogenesis. We show that rare variants are enriched in severely affected AIS (show AR ELISA Kits) patients and are significantly associated with curve severity.
There was no association of overall methylation of FBN2 in the serum DNA with age, maximal tumor size, extent of tumor, tumor site, histology, presence of lymph node metastasis, distant metastasis, or Dukes' stage.
These results suggest that both fibrillin-1 (show FBN1 ELISA Kits) and fibrillin-2 are essential for the formation of thick oxytalan fibers in the ciliary zonule.
Data demonstrated that N-terminal fibrillin-2 epitopes are masked in postnatal microfibrils.
Data show that in wound healing and sclerotic skin diseases, a marked increase of fibrillin-2 expression was found by immunohistology.
Ten novel mutations have been identified in the critical region of FBN2, indicating a mutation detection rate of 75% in this limited region; none of the mutations altered amino acids in the calcium binding consensus sequence of EGF (show EGF ELISA Kits)-like domains.
fibrillins can directly interact in an N- to C-terminal fashion to form homotypic fibrillin-1 (show FBN1 ELISA Kits) or heterotypic fibrillin-1 (show FBN1 ELISA Kits)/fibrillin-2 microfibrils
Fibrillin-2 and periostin (show POSTN ELISA Kits) are target genes in Osterix (show SP7 ELISA Kits)-mediated osteoblast differentiation.
These results suggest that both fibrillin-1 (show FBN1 ELISA Kits) and fibrillin-2 expression is required to form thick oxytalan fibers in periodontal ligament.
Fibrillin-2 plays a role in forelimb muscle differentiation and infiltration of fat into the limb connective tissue space.
the bronchial epithelial dysplasia accompanying microfibril dysregulation in Adamtsl2 (show ADAMTSL2 ELISA Kits)(-/-) mice cannot be reversed by TGFbeta (show TGFB1 ELISA Kits) neutralization, and thus might be mediated by other mechanisms.
We propose that the Mp "worse-than-null" eye phenotype plausibly results from a failure in normal trafficking of proteins that are co-expressed with Fbn2 within the ciliary margin
Fbn2 has an indispensable role in ocular morphogenesis in mice. The high incidence of iris coloboma in Fbn2-null animals implies a previously unsuspected role in optic fissure closure.
fibrillin-2 exerts a greater positive influence on the mechanical properties of bone than fibrillin-1 (show FBN1 ELISA Kits) assemblies
Fibrillin-1 and -2, the structural components of extracellular microfibrils, differentially regulate TGF-beta and bone morphogenetic protein (BMP) bioavailability in bone.
Findings indicate that Fbn2 is involved in integrity of structures required for strength in limb movement.
interaction with microfibril-associated glycoprotein-2 (show MFAP5 ELISA Kits)
The protein encoded by this gene is a component of connective tissue microfibrils and may be involved in elastic fiber assembly. Mutations in this gene cause congenital contractural arachnodactyly.
, fibrillin 5
, fibrillin 2 (congenital contractural arachnodactyly)
, syndatyly ems