Rabbit Anti-Fibrillin-1 Polyclonal Antibody #abs130335

abs130335-50ug

1-2 Weeks

201

abs130335-100ug

1-2 Weeks

301

Description

FBN1 Fibrillins, belonging to the fibrillin family, are crucial structural components found in 10-12 nm extracellular calcium-binding microfibrils. These microfibrils can be associated with elastin or exist as elastin-free bundles. The main function of fibrillin-1-containing microfibrils is to provide long-term support for bearing forces. Additionally, fibrillin-1 interacts with COL16A1. The information provided here is based on UniProtKB. Please note that the generated content has been rearranged to maintain its similarity to the original text while ensuring a different style of expression.

Other names

The extracellular microfibril comprises a glycoprotein component with a molecular weight of 350 kDa. It is known as Fibrillin-1 or FBN1. FBN1_HUMAN is the corresponding gene symbol for FBN1. This glycoprotein is also referred to as Fibrillin 15 or Fibrillin15 in some contexts. It plays a crucial role in various genetic disorders including Marfan syndrome, MASS, MFS1, Weill Marchesani syndrome (WMS), and SSSK. Additionally, it is associated with GPHYSD2, ACMICD, OCTD, SGS, and WMS2.

Source

Rabbit

Specificity

Detection of endogenous levels of Fibrillin-1 can be accomplished using Fibrillin-1 Antibody. The antibody provides reliable and accurate results by specifically targeting and detecting Fibrillin-1 protein in biological samples. This allows for the study and analysis of Fibrillin-1 expression and localization in various tissues and cells. The use of Fibrillin-1 Antibody is an efficient and effective tool in research and diagnostic applications related to Fibrillin-1 and associated disorders.

Species Reactivity

Human;Mouse;Rat

Application

IHC 1:50-1:200, ELISA(peptide) 1:20000-1:40000

Immunogen

Fibrillin-1, a human protein, serves as the basis for the creation of a synthesized peptide. The newly synthesized peptide is designed to possess a high degree of similarity to Fibrillin-1, using rearrangement techniques to maintain the original text information while presenting the content in a different format.

Properties

Concentration

1mg/ml

Purification

Immunogen affinity purified

Clonality

Polyclonal Antibody

Stability & Storage

It is recommended to store at a temperature of -20 °C for a duration of one year. It is important to avoid repeating the process of freezing and thawing as it may affect the quality of the product. Please ensure that the stored product is handled with care to maintain its effectiveness.

Storage buffer

The storage condition for Rabbit IgG is in phosphate buffered saline with a pH of 7.4, containing 150mM NaCl, 0.02% sodium azide, and 50% glycerol. It should be stored at -20 °C and has a shelf life of 12 months from the date of receipt. Please note that the following content is different from the original text and generated by a language model.

Target

Background

Fibrillin-1 is a crucial component of the extracellular matrix, specifically the microfibrils that have a diameter of 10-12 nm. These microfibrils provide both structural support and regulatory properties to connective tissues that bear loads. Their main role is to offer long-term force-bearing support to tissues such as the lung, blood vessels, and skin.
In certain tissues, like the ciliary zonule, tendon, cornea, and glomerulus, microfibrils form networks independently of elastin, serving as a source of tensile strength and acting as anchors. However, in tissues where elastin is present, microfibrils serve as a scaffold for its deposition. This is observed in the periphery of elastic fibers found in the lung, blood vessels, and skin.
Aside from its structural role, fibrillin-1 also actively participates in tissue homeostasis. It interacts with various growth factors, including bone morphogenetic proteins (BMPs), growth and differentiation factors (GDFs), and latent transforming growth factor-beta-binding proteins (LTBPs). Furthermore, fibrillin-1 engages with cell-surface integrins, other extracellular matrix proteins, and proteoglycans, further adding to its regulatory functions.
One of the specific roles of fibrillin-1 is its involvement in osteoblast maturation. It helps regulate the availability of transforming growth factor-beta (TGF-beta) and controls the levels of TGF-beta and BMP. These factors play crucial roles in osteoblast maturation. Additionally, fibrillin-1 acts as a negative regulator of osteoclastogenesis by binding to TNFSF11, a factor necessary for osteoclast differentiation and activation. This binding sequesters TNFSF11, disrupting its signaling pathway and impairing the activation of transcription factor NFATC1, which regulates genes important for osteoclast function.
Cell adhesion is another key function of fibrillin-1, achieved through its interactions with cell surface receptors integrins ITGAV:ITGB3 and ITGA5:ITGB1. These interactions enable cells to adhere to the extracellular matrix, contributing to tissue integrity.
Lastly, fibrillin-1 binds to heparin, an interaction that plays a crucial role in the assembly of microfibrils. This highlights the importance of heparin in the structural organization of the extracellular matrix.
In summary, fibrillin-1 is a versatile protein that acts as a structural component of microfibrils, providing load-bearing support and regulatory properties to connective tissues. It plays a key role in tissue homeostasis through interactions with growth factors, cell-surface receptors, and other extracellular matrix components. Fibrillin-1 is involved in osteoblast maturation, regulation of osteoclastogenesis, and cell adhesion, with heparin playing a significant role in microfibril assembly.

Posttranslational modification

Fibrillin-1: 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.

Celluar localization

Endoplasmic reticulum;Extracellular region or secreted;

UniPort

P35555