Mouse Anti-FBN1 (AA 2772-2872) Recombinant Antibody (CBXF-0367) (CBMAB-F0280-CQ)

Mouse

Human

CBXF-0367

IgG2a

ELISA, IHC, WB

Human

IgG2a

Monoclonal

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Liquid

PBS, pH 7.2

0.09% sodium azide

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

AA 2772-2872

fibrillin 1

This gene encodes a member of the fibrillin family of proteins. The encoded preproprotein is proteolytically processed to generate two proteins including the extracellular matrix component fibrillin-1 and the protein hormone asprosin. Fibrillin-1 is an extracellular matrix glycoprotein that serves as a structural component of calcium-binding microfibrils. These microfibrils provide force-bearing structural support in elastic and nonelastic connective tissue throughout the body. Asprosin, secreted by white adipose tissue, has been shown to regulate glucose homeostasis. Mutations in this gene are associated with Marfan syndrome and the related MASS phenotype, as well as ectopia lentis syndrome, Weill-Marchesani syndrome, Shprintzen-Goldberg syndrome and neonatal progeroid syndrome.

Fibrillin 1; Asprosin; FBN; Fibrillin 1 (Marfan Syndrome); Fibrillin-1 Preproprotein; Marfan Syndrome; Fibrillin 15; Fibrillin-1; GPHYSD2; ACMICD;

Fibrillin-1:
Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues (PubMed:1860873, PubMed:15062093).

Fibrillin-1-containing microfibrils provide long-term force bearing structural support (PubMed:27026396).

In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin (PubMed:27026396).

In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus where they provide tensile strength and have anchoring roles (PubMed:27026396).

Fibrillin-1 also plays a key role in tissue homeostasis through specific interactions with growth factors, such as the bone morphogenetic proteins (BMPs), growth and differentiation factors (GDFs) and latent transforming growth factor-beta-binding proteins (LTBPs), cell-surface integrins and other extracellular matrix protein and proteoglycan components (PubMed:27026396).

Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively (By similarity).

Negatively regulates osteoclastogenesis by binding and sequestering an osteoclast differentiation and activation factor TNFSF11 (PubMed:24039232).

This leads to disruption of TNFSF11-induced Ca2+ signaling and impairment of TNFSF11-mediated nuclear translocation and activation of transcription factor NFATC1 which regulates genes important for osteoclast differentiation and function (PubMed:24039232).

Mediates cell adhesion via its binding to cell surface receptors integrins ITGAV:ITGB3 and ITGA5:ITGB1 (PubMed:12807887, PubMed:17158881).

Binds heparin and this interaction has an important role in the assembly of microfibrils (PubMed:11461921).

Asprosin:
Adipokine secreted by white adipose tissue that plays an important regulatory role in the glucose metabolism of liver, muscle and pancreas (PubMed:27087445, PubMed:30853600).

Hormone that targets the liver in response to fasting to increase plasma glucose levels (PubMed:27087445).

Binds the olfactory receptor OR4M1 at the surface of hepatocytes and promotes hepatocyte glucose release by activating the protein kinase A activity in the liver, resulting in rapid glucose release into the circulation (PubMed:27087445, PubMed:31230984).

May act as a regulator of adaptive thermogenesis by inhibiting browning and energy consumption, while increasing lipid deposition in white adipose tissue (By similarity).

Also acts as an orexigenic hormone that increases appetite: crosses the blood brain barrier and exerts effects on the hypothalamus (By similarity).

In the arcuate nucleus of the hypothalamus, asprosin directly activates orexigenic AgRP neurons and indirectly inhibits anorexigenic POMC neurons, resulting in appetite stimulation (By similarity).

Activates orexigenic AgRP neurons via binding to the olfactory receptor OR4M1 (By similarity).

May also play a role in sperm motility in testis via interaction with OR4M1 receptor (By similarity).

Activation of protein kinase A activity Source: UniProtKB
Anatomical structure morphogenesis Source: GO_Central
Camera-type eye development Source: UniProtKB
Cell adhesion mediated by integrin Source: UniProtKB
Cellular response to insulin-like growth factor stimulus Source: Ensembl
Cellular response to transforming growth factor beta stimulus Source: Ensembl
Embryonic eye morphogenesis Source: UniProtKB
Glucose homeostasis Source: UniProtKB
Glucose metabolic process Source: UniProtKB
Heart development Source: UniProtKB
Metanephros development Source: Ensembl
Negative regulation of osteoclast development Source: UniProtKB
Negative regulation of osteoclast differentiation Source: UniProtKB
Post-embryonic eye morphogenesis Source: UniProtKB
Protein kinase A signaling Source: UniProtKB
Sequestering of BMP in extracellular matrix Source: BHF-UCL
Sequestering of TGFbeta in extracellular matrix Source: BHF-UCL
Skeletal system development Source: UniProtKB

Secreted. Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin (PubMed:24982166).
Fibrillin-1: Extracellular matrix
Asprosin: Secreted. Secreted by white adipose tissue and circulates in the plasma.

Marfan syndrome (MFS):
The disease is caused by variants affecting the gene represented in this entry. The majority of the more than a thousand mutations in FBN1 currently known are point mutations, the rest are frameshifts and splice site mutations. Marfan syndrome has been suggested in at least 2 historical figures, Abraham Lincoln and Paganini. A hereditary disorder of connective tissue that affects the skeletal, ocular, and cardiovascular systems. A wide variety of skeletal abnormalities occurs with Marfan syndrome, including scoliosis, chest wall deformity, tall stature, abnormal joint mobility. Ectopia lentis occurs in most of the patients and is almost always bilateral. The leading cause of premature death is progressive dilation of the aortic root and ascending aorta, causing aortic incompetence and dissection. Neonatal Marfan syndrome is the most severe form resulting in death from cardiorespiratory failure in the first few years of life.
Ectopia lentis 1, isolated, autosomal dominant (ECTOL1):
An ocular abnormality characterized by partial or complete displacement of the lens from its space resulting from defective zonule formation.
Weill-Marchesani syndrome 2 (WMS2):
A rare connective tissue disorder characterized by short stature, brachydactyly, joint stiffness, and eye abnormalities including microspherophakia, ectopia lentis, severe myopia and glaucoma.
Overlap connective tissue disease (OCTD):
Heritable disorder of connective tissue characterized by involvement of the mitral valve, aorta, skeleton, and skin. MASS syndrome is closely resembling both the Marfan syndrome and the Barlow syndrome. However, no dislocation of the lenses or aneurysmal changes occur in the aorta, and the mitral valve prolapse is by no means invariable.
Stiff skin syndrome (SSKS):
A syndrome characterized by hard, thick skin, usually over the entire body, which limits joint mobility and causes flexion contractures. Other occasional findings include lipodystrophy and muscle weakness.
Geleophysic dysplasia 2 (GPHYSD2):
An autosomal dominant disorder characterized by severe short stature, short hands and feet, joint limitations, and skin thickening. Radiologic features include delayed bone age, cone-shaped epiphyses, shortened long tubular bones, and ovoid vertebral bodies. Affected individuals have characteristic facial features including a 'happy' face with full cheeks, shortened nose, hypertelorism, long and flat philtrum, and thin upper lip. Other distinctive features include progressive cardiac valvular thickening often leading to an early death, toe walking, tracheal stenosis, respiratory insufficiency, and lysosomal-like storage vacuoles in various tissues.
Acromicric dysplasia (ACMICD):
An autosomal dominant disorder characterized by severe short stature, short hands and feet, joint limitations, and skin thickening. Radiologic features include delayed bone age, cone-shaped epiphyses, shortened long tubular bones, and ovoid vertebral bodies. Affected individuals have distinct facial features, including round face, well-defined eyebrows, long eyelashes, bulbous nose with anteverted nostrils, long and prominent philtrum, and thick lips with a small mouth. Other characteristic features include hoarse voice and pseudomuscular build, and there are distinct skeletal features as well, including an internal notch of the femoral head, internal notch of the second metacarpal, and external notch of the fifth metacarpal.
Marfanoid-progeroid-lipodystrophy syndrome (MFLS):
Asprosin: An autosomal dominant syndrome characterized by congenital lipodystrophy, a progeroid facial appearance due to lack of subcutaneous fat, and variable signs of Marfan syndrome. Clinical features include premature birth with an accelerated linear growth disproportionate to the weight gain, ectopia lentis, aortic dilatation, dural ectasia, and arachnodactyly. Mental and motor development are within normal limits.

Cleavage of N- and C-terminus by furin is required for incorporation into the extracellular matrix and assembly into microfibrils (PubMed:27026396). The C-terminus, which corresponds to the Asprosin chain, was initially thought to constitute a propeptide (PubMed:24982166). Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin, an essential step for incorporation of Fibrillin-1 into the nascent microfibrils (PubMed:24982166).
Fibrillin-1:
Forms intermolecular disulfide bonds either with other fibrillin-1 molecules or with other components of the microfibrils.