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Key Documents

F0162

Sigma-Aldrich

Fibronectine

lyophilized powder, 45 kDa

Synonyme(s) :

Fibronectin

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About This Item

Numéro MDL:
Code UNSPSC :
12352202
eCl@ss :
42020141
Nomenclature NACRES :
NA.75

Source biologique

human plasma

Niveau de qualité

Pureté

≥90% (SDS-PAGE)

Forme

lyophilized powder

Poids mol.

45 kDa

Conditionnement

pkg of 0.5 mg

Technique(s)

cell culture | mammalian: suitable

Impuretés

HIV and HBsAg, source material tested negative
Small proteolytic fragments, may contain traces

Solubilité

water: soluble ≥0.500 mg/mL, clear to slightly hazy, colorless

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Température de stockage

−20°C

Informations sur le gène

human ... FN1(2335)

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Description générale

Fibronectin 1 is a glycoprotein of the extracellular matrix that is coded by FN1 gene. It is expressed in the plasma and at the cell surface.FN1 is mapped to human chromosome 2q35. Proteolytic fragments of fibronectin has a cell binding domain. Plasma fibronectin has two polypeptide chains connected by two disulphide bonds present near carboxy terminal. Each polypeptide chain is of 220-250 kDa.

Application

Fibronectin proteolytic fragment from human plasma has been used as fluorophore-conjugated proteins. It has also been used in solid phase binding assay.

Actions biochimiques/physiologiques

Fibronectin participates in cell adhesion, growth, migration, wound healing, blood coagulation and metastasis. Mutations in FN1 results in glomerulopathy. It plays an important role in cell attachment and spreading, control of cell cytoskeleton, morphology and differentiation. FN1 is also involved in extracellular matrix formation, hemostasis and thrombosis. Proteolytic fragments of fibronectin plays a vital role in mononuclear phagocyte function.
Fibronectins are high molecular weight glycoproteins with two subunits joined by a disulfide bond to form the dimer. The fragments are obtained using protelytic enzymes. This 45 kDa gelatin binding fragment is obtained through trypitc digestion of the N-terminal 70 kDa fragment, which is produced by Cathespin D digestion.

This fragment has an acidic pI (4.9-5.3) and does not bind to heparin. This domain is resistant to proteolysis due to intrachain disulfide bonding and the attached carbohydrate. The intrachain disulfide bonds are essential for binding to gelatin, while the complex, branched, asparagine-linked carbohydrate is not. This fragment binds to C1q, but not to fibrin.

Attention

The product should be stored at -20°C.

Notes préparatoires

This product is lyophilized from phosphate buffered saline with sucrose as a cryoprotectant. The source material has tested negative for antibody to HIV, HCN, and HBsAg. It is soluble in water at 0.5 mg/mL and yields a clear to slightly hazy solution.

En option

Pictogrammes

Exclamation mark

Mention d'avertissement

Warning

Mentions de danger

Classification des risques

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

Organes cibles

Respiratory system

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

A R Pickford et al.
Structure (London, England : 1993), 5(3), 359-370 (1997-03-15)
Fibronectin is an extracellular matrix glycoprotein involved in cell adhesion and migration events in a range of important physiological processes. Aberrant adhesion of cells to the matrix may contribute to the breakdown of normal tissue function associated with various diseases.
Fibronectin in Health and Disease (2018)
Plasma Fibronectin: Structure and Functions (1985)
Nanoparticle amplification via photothermal unveiling of cryptic collagen binding sites.
Lo J H, et al.
Journal of Material Chemistry B: Materials for Biology and Medicine, 1(39), 5235-5240 (2013)
Ming Liu et al.
Scientific reports, 5, 14449-14449 (2015-09-25)
Bacterial adhesins play a pivotal role in the tight bacteria-host cells attachment to initiate the downstream processes and bacterial infection of hosts. In this study, we identified a novel adhesin, VpadF in V. parahaemolyticus. Deletion of VpadF in V. parahaemolyticus

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