Datasheet

Biological Description

Specificity	Fibronectin/FN1 Rabbit mAb recognizes endogenous levels of total Fibronectin/FN1 protein.
Background	Fibronectin (Fn) is a multidomain glycoprotein widely distributed in extracellular fluids and matrices across virtually all vertebrate tissues and organs. It serves as a crucial mediator connecting cells to the extracellular matrix (ECM) and plays essential roles in numerous physiological processes, including cell adhesion, differentiation, growth, and migration. Fn also contributes significantly to embryonic development, wound healing, and blood coagulation. Disruptions in fibronectin expression, degradation, or structural organization are associated with various pathological conditions, such as cancer progression and fibrotic diseases. Despite being encoded by a single gene, alternative splicing of its pre-mRNA generates at least 20 different isoforms in humans. Fibronectin exists in two main forms: a soluble form found in body fluids and an insoluble form incorporated into extracellular matrices and basement membranes. In its soluble state, fibronectin adopts a compact structure due to intramolecular interactions. However, when incorporated into the ECM through a process known as fibronectin assembly, the protein unfolds into an extended conformation. Soluble fibronectin is primarily synthesized by hepatocytes and released into the bloodstream, while fibroblasts and endothelial cells are responsible for producing the insoluble, matrix-associated form.

Specificity

Fibronectin/FN1 Rabbit mAb recognizes endogenous levels of total Fibronectin/FN1 protein.

Background

Fibronectin (Fn) is a multidomain glycoprotein widely distributed in extracellular fluids and matrices across virtually all vertebrate tissues and organs. It serves as a crucial mediator connecting cells to the extracellular matrix (ECM) and plays essential roles in numerous physiological processes, including cell adhesion, differentiation, growth, and migration. Fn also contributes significantly to embryonic development, wound healing, and blood coagulation. Disruptions in fibronectin expression, degradation, or structural organization are associated with various pathological conditions, such as cancer progression and fibrotic diseases. Despite being encoded by a single gene, alternative splicing of its pre-mRNA generates at least 20 different isoforms in humans. Fibronectin exists in two main forms: a soluble form found in body fluids and an insoluble form incorporated into extracellular matrices and basement membranes. In its soluble state, fibronectin adopts a compact structure due to intramolecular interactions. However, when incorporated into the ECM through a process known as fibronectin assembly, the protein unfolds into an extended conformation. Soluble fibronectin is primarily synthesized by hepatocytes and released into the bloodstream, while fibroblasts and endothelial cells are responsible for producing the insoluble, matrix-associated form.

Usage Information

Application

WB, IP, IHC, IF

Dilution

WB	IP	IHC	IF
1:1000	1:100	1:100 - 1:400	1:200 - 1:800

Reactivity

Human

Source

Rabbit

MW

300 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/31779172/

Fibronectin/FN1 Rabbit mAb

Biological Description

Usage Information

References

Application Data