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FC010

Sigma-Aldrich

Human Fibronectin

from human plasma, liquid, 1 mg/mL, purified protein, suitable for cell culture

Synonym(s):

Fibronectin protein

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About This Item

UNSPSC Code:
12352202
eCl@ss:
32160405
NACRES:
NA.75

product name

Human Plasma Fibronectin Purified Protein, from human plasma, liquid, 1 mg/mL (100 MG pack size is lyophilized), purified protein, suitable for cell culture

biological source

human

Quality Level

Assay

~95% (SDS-PAGE)

form

(liquid: 1MG, 5MG, 10MG pack size
lyophilized: 100 MG pack size)

mol wt

220 kDa

manufacturer/tradename

Chemicon®

concentration

1 mg/mL

technique(s)

cell culture | mammalian: suitable

surface coverage

2—10 μg/cm2

input

sample type mesenchymal stem cell(s)
sample type neural stem cell(s)
sample type: human embryonic stem cell(s)
sample type epithelial cells
sample type hematopoietic stem cell(s)
sample type induced pluripotent stem cell(s)
sample type pancreatic stem cell(s)

UniProt accession no.

Binding Specificity

Peptide Source: Collagen

Peptide Source: Laminin

shipped in

wet ice

storage temp.

2-8°C

Gene Information

human ... FN1(2335)

General description

Fibronectins (FNs) are high-molecular-mass adhesive glycoproteins of the extracellular matrix (ECM) and body fluids. It is a dimer composed of two subunits linked by two disulfide bonds. Each monomer of FN consists of three types of repeating units: 12 FN repeats of type I (approximately 40 amino acids each), two type II repeats (around 60 amino acids), and 15-17 type III repeats (approximately 90 amino acids). These repeating units contribute to the structural and functional diversity of fibronectin molecules.

Application

Human fibronectin (HFN) is suitable for use as an attachment factor in the propagation of cells in vitro when used to coat cell culture surfaces, including plastic ware, glassware, and microcarrier beads.

Biochem/physiol Actions

Fibronectin plays a crucial role in mediating diverse cellular interactions and is involved in various processes, including cell adhesion, the establishment and maintenance of cell morphology, cell migration, growth, and differentiation. It interacts with several extracellular matrix (ECM) and cell surface proteins, such as collagen, heparin, fibrin, and specific cell membrane receptors. Fibronectin can also serve as a ligand for multiple integrins, including the well-known fibronectin receptor alpha5-beta1, which binds to the arginylglycylaspartic acid (RGD) sequence in the repeat III-10 region of fibronectin. This extensive network of interactions highlights fibronectin′s significance in regulating cellular behavior and mediating tissue function.

Physical form

Liquid in 50 mM tris-buffered saline (TBS), pH 7.5,containing no preservatives.Lyophilized from 50 mM tris-buffered saline (TBS), pH 7.5,containing no preservatives (100 MG pack size). Reconstitute the entire vial ofhFN to 1 mg/mL using a sterile balanced salt solution at 37°C.

Storage and Stability

Maintain at 2-8°C for up to 6 months from date of receipt. Do not freeze.

Analysis Note

A double band of 220 kDa is present under reduced conditions.hFN is purified by affinity chromatography on gelatin agarose, followed by chromatography on heparin-agarose.Plasma from donors has been screened, and shown to be negative for HIV, HTLV, Hepatitis B and C.

Other Notes

Suggested Procedure for Coating Cell Cultureware

1.Determine the amount of HFN needed to coat culture vessels by multiplying the total surface area (cm2) by the desired concentration (μg/mL) of HFN. Recommended amount is 2-10 μg/cm2.

2.Wet the surface of each culture vessel to be coated with a minimum amount of sterile balanced salt solution (serum and protein free) required to cover the entire area.

3.Introduce the proper CO2 atmosphere, if required.

4.Add the calculated amount of HFN to each culture vessel.

5.Allow HFN to adsorb to the surface of the vessel for 5-20 minutes.

6.Remove residual balanced salt solution before proceeding with standard cell culture procedures


Product is filtered using a 0.1 micron filter during production. It is recommended to filter product again before use/after reconstitution.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Intestinal epithelial wound healing assay in an epithelial-mesenchymal co-culture system.
Seltana, Amira, et al.
Wound Repair and Regeneration, 18, 114-122 null
Johannes Rheinlaender et al.
Nature materials, 19(9), 1019-1025 (2020-05-27)
Cortical stiffness is an important cellular property that changes during migration, adhesion and growth. Previous atomic force microscopy (AFM) indentation measurements of cells cultured on deformable substrates have suggested that cells adapt their stiffness to that of their surroundings. Here
Aleksander A Rebane et al.
FEBS letters, 594(7), 1132-1144 (2019-12-14)
Golgins are an abundant class of peripheral membrane proteins of the Golgi. These very long (50-400 nm) rod-like proteins initially capture cognate transport vesicles, thus enabling subsequent SNARE-mediated membrane fusion. Here, we explore the hypothesis that in addition to serving as
Mattia Usuelli et al.
The Journal of biological chemistry, 296, 100584-100584 (2021-03-28)
Physical interactions between vascular endothelial growth factor (VEGF), a central player in blood endothelial cell biology, and fibronectin, a major fibrillar protein of the extracellular matrix, are important determinants of angiogenic activity in health and disease. Conditions signaling the need
E Ruoslahti et al.
The Biochemical journal, 193(1), 295-299 (1981-01-01)
Human fibronectin was isolated from second-trimester amniotic fluid, from amniotic fluid obtained at term and from adult plasma. The amniotic-fluid fibronectins had a slightly higher apparent molecular weight on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis than the plasma fibronectin. Early- and late-amniotic-fluid

Articles

Attachment Factors for 3-Dimensional Cell Culture

The extracellular matrix (ECM) is secreted by cells and surrounds them in tissues.

Development of a novel serum-free and xeno-free human mesenchymal stem cell (MSC) osteocyte differentiation media.

Extracellular matrix proteins such as laminin, collagen, and fibronectin can be used as cell attachment substrates in cell culture.

Protocols

Dilute fibronectin to the desired concentration. Optimum conditions for attachment are dependent on cell type and application. The typical coating concentration is 1 – 5 ug/cm2.Fibronectin coating protocol, products, and FAQs.

This page covers the indirect co-culture of embryonic stem cells with embryonic fibroblasts.

Information about mesenchyme, specifically mesenchymal stem cell procotols. Step-by-step cell culture protocols for mesenchymal stem cell (MSC) isolation, expansion and differentiation.

Related Content

This page covers the ECM coating protocols developed for four types of ECMs on Millicell®-CM inserts, Collagen Type 1, Fibronectin, Laminin, and Matrigel.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

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