Fibulin-2 Antibodies

Fibulin-2 (FBLN2)

Its binding to fibronectin and some other ligands is calcium dependent. May act as an adapter which mediates the interaction between FBN1 and ELN (PubMed:17255108).

.

Gene Information

Human
Gene Name:	FBLN2
Uniprot:	P98095
Entrez:	2199

Family

Belongs to:
fibulin family

Alternative Names

FBLN2; FIBL-2; Fibulin 2; Fibulin-2

Molecular Weight

Mass (kDA):
126.573 kDA

Genomic Context

Human
Location:	3p25.1
Sequence:	3; NC_000003.12 (13549125..13638408)

Tissue Specificity

Component of both basement membranes and other connective tissues. Expressed in heart, placenta and ovary.

Subcellular Localizations

Secreted, extracellular space, extracellular matrix.

Diseases

• Malignant Neoplasms
• Neoplasms
• Carcinoma
• Neoplasm Metastasis
• Cell Invasion
• Neoplasm Invasiveness
• Marfan Syndrome
• Colorectal Neoplasms
• Malignant Squamous Cell Neoplasm
• Tissue Adhesions
• Cholangiocarcinoma
• Malignant Neoplasm Of Breast

• Down Syndrome
• Aneuploidy
• Dissection Of Aorta
• Tumor Angiogenesis
• Pituitary Diseases
• Mammary Neoplasms
• L1 Acute Lymphoblastic Leukemia

Pathways

• Methylation
• Sertoli Cell Differentiation
• Cell Proliferation
• Elastic Fiber Assembly
• Dna Methylation
• Sex Determination
• Localization
• Cartilage Development
• Cell Differentiation
• Cell Growth

• Angiogenesis
• Gonad Development
• Pathogenesis
• Heart Development

PTMs

• Methylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/FBLN2

Best Uses Of The FBLN2 Marker

What is Fibulin-2? What can it do for your research? This article will discuss the science behind protein and its best uses. It is a member the fibulin family. It is the most common gene in the body. Therefore, its presence in blood may help with certain diseases. It is used by scientists who are interested in research, application development, and many other purposes.

Fibulin-2 is a member of the fibulin family

Although there is no direct link between fibulin-2-related cancer and the protein, multiple studies have confirmed that it plays a crucial role during cancer development. These results point to a potential therapeutic target for cancer treatment. Fibulin-2 is found within the same tissues as its counterpart in ADAMTS. It regulates organogenesis, tissue homeostasis, inflammation, and other processes.

This extracellular matrix proteins binds calcium and other extracellular molecules. It may play a part in the development and differentiation of neuronal, cardiac, and skeletal structures. Fibulins can be found in many metazoans as well as nematodes. Some species have two fibulins. Elastogenic fibulins are those with a shorter length.

Atherosclerosis of the aorta induces smooth muscle cells to secrete fibulin-2. Fibulin-2 might be involved with ECM organisation and regulate SMC movement and adhesion during vessel wall repairs. Fibulin-2 may be important for the development of atherosclerosis and restenosis. It is also linked with improved smooth muscle cell proliferation and vascular integrity.

Atherosclerotic lesions are associated with the production of fibulin-2 using synthetic SMCs. The protein is a dimer and crosslinks lectican-hyaluronan. Fibulin-2 may also play a role in the differentiation of mesenchymal cells. Its expression was seen in atherosclerotic plaques suggesting that the proteins might interact during atherogenesis.

There are many genetic variants linked to the loss fibulin-2 in ectoderms. One such gene is ADAMTS-1. ADAMTS-1 interacts with fibulin-1 to modulate its activity. ADAMTS-1 also interacts and causes the loss or the disappearance of the pro domain. ADAMTS-1 can also regulate versican activity.

While all members the fibulin family interacts with tropoelastin (as do all other members), the interaction between the proteins is quite different. While fibulin-1 is very similar in structure to fibulin-2, their protein levels vary in different organs. Fibulin-2 is a more restricted member of the fibulin family and is only present in the lung blood vessel. The airways and parenchyma are the other members of this fibulin family.

Although most members of the fibulin family share a conserved C-terminal domain, fibulin-2 is unique in the N-terminal domain. Its cysteine enriched and cysteine void domains set it apart from other fibulins. Fibulin-7 contains a sushi domain. Hemicentin-1 (fibulin-2), has an immunoglobulin C-2 domain, and a von Willebrand domain. These proteins can be found in human beings in varying levels.

Fibulin-2 is lost in mice and there is no compensatory increase in other fibulin members. This was confirmed by a Northern blot analysis involving total RNA from newborn mice. Fibulin-1 and -3 mRNA expression levels were similar in Fbln2-/ mouse to their counterparts. This suggests that matrix construction is not compromised in mice without fibulin-2.

Fibulin is a widely expressed protein in the ECM with a wide binding repertoire. Fibulin-2 is expressed in skin, cornea, and skeletal muscle. It has been found to have important roles in tissue remodeling and cell migration. Fibulin-2 is also associated with a high level of collagen. These findings highlight the diverse role of fibulins in cancer treatment. There is no clear answer to the question "Why fibulins are important in cancer treatment?"

While fibulin-2 is found to bind fibrillin-1 in vitro, it is unknown if it is necessary for the formation of elastic fibers in mice. Fibulin-2-deficient mice in vivo fail to form elastic fibres. It was also found that embryonic fibrillar matrix could be formed in embryonic fibroblasts without fibulin-2. Fibulin-2 may have overlapped tissue distribution and expression patterns, which indicates functional redundancy between the two proteins.

The fibulins are a family of extracellular matrix glycoproteins that contain a unique three-modular structure. Fibulins have an I-domain, domain-II consists of tandem EGF-like modules, and domain-III is a fibulin-type module. This structure supports interacting with other proteins and regulating cell adhesion.

Fibulin-2 plays a crucial role in the development and maintenance of muscle. This protein is important, but it is rarely expressed in small vessels. Mice lacking fibulin-1 are therefore at risk of perinatal mortality. Fibulin-1 null mice suffer from bleeding due to a deficient endothelial basement. However, fibulin-2 does not exist in small blood vessels.

Fibulin-2, a protein that is part of the fibulin family, is Fibulin-2.

Fibulin-2 a disulfide -linked monomer is 200kDa in volume and contains 20 O -linked oligosaccharides. It is similar in structure to fibulin-1 but has a restricted distribution in tissues. It is only found within the blood vessels of a lung, while the four other fibulin proteins can be found in parenchyma as well as in the airways. The protein is relatively low in quantity in most organs, as measured by radioimmunoinhibition assays.

The Fibulin-2 gene can be found on the human chromosome, at p24-255, and in the mouse, at the D-E bands. The protein is composed of two distinct domains, which allow it to interact with multiple cell surfaces and ECM components. The protein plays multiple roles in development and has been implicated with heart valve diseases. Although its functions are not fully understood it plays an important function in the development of the heart valve and the formation of the aortic arch.

The fibulin family of glycoproteins consists of eight members, each with distinct roles in regulating extracellular matrix (ECM) aggregates. Fibulin-1 has tumor suppressive and is expressed in serum, matrix and basement membranes. Fibulin-2 partially interacts and co-localizes in serum with fibulin-1.

The protein fibulin-2 may be associated with ADAMTS-12 which is a cellular enzyme that inhibits fibulin-2 degradation. The interaction between fibulin-2, ADAMTS-12 could be a therapeutic target in breast cancer. However, it is not clear how these two proteins interact. These results suggest that both these families play an essential role in tissue health.

While the absence of fibulin-2 may affect elastin production, it does not affect the assembly and function of elastic fibers. However, the loss or upregulation of fibulin-2 is not a compensatory mechanism. The matrix formation by fibroblasts deficient in fibulin-2 is not affected by the loss of fibulin-2.

This protein is linked to integrins by a RGD motif. In addition, fibulin-2 may influence the development of various cancers, as it promotes tumor growth and invasion. Fibulin-3 can be linked to cervical cancer. It has also been linked to breast cancer by its overexpression. The protein is involved by several mechanisms in tumorigenesis.

Researchers have looked into the role played by fibulin-2 in female and male reproductive functions. Although it isn't known how fibulin-2 impacts reproduction, it may play some role in sequestration. In addition to sequestration, fibulins-2 and fibulin-1 may control the access of sex hormone-steroids to target cells. Moreover, both male and female mice lacking fibulin-2 are fertile.

Fibulin-2 is not affected by the formation elastic fibers in mice. However, elastogenesis is not affected if fibulin-2 is lost. Fibulin-2 plays an important role in the formation microfibrils and elastic fibres. Fibulin-2 is highly coordinated with elastin implantation. Because they are structurally related proteins, this is why they are highly coordinated.

Fibulins in humans are modules with similar biochemical structure and locations. They are however different in their functions and the binding partners they share. Fibulin-2, the most well-known of the four, is the best-known. Fibulin-2 (a beta subunit) is the only one that can splice variants. Its predicted molecular weight is about 600 kD.

Fibulins are proteins that make up the ECM in our body. The family includes the fibulins 1 and 2 as well as hemicentins, which are related proteins. Fibulin-1 is not only the best-known, but also has the most relevant partners. Fibulin-1-deficient mice don't survive beyond birth, but mice deficient fibulin-2 live and are not affected by phenotypic problems. This is likely because of the compensatory role of fibulin-2 within the body.