Saltar al contenido
Merck

F0162

Sigma-Aldrich

Fibronectina

lyophilized powder, 45 kDa

Sinónimos:

Fibronectin

Iniciar sesiónpara Ver la Fijación de precios por contrato y de la organización


About This Item

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

biological source

human plasma

Quality Level

assay

≥90% (SDS-PAGE)

form

lyophilized powder

mol wt

45 kDa

packaging

pkg of 0.5 mg

technique(s)

cell culture | mammalian: suitable

impurities

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

solubility

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

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... FN1(2335)

¿Está buscando productos similares? Visita Guía de comparación de productos

General description

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.

Biochem/physiol Actions

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.

Caution

The product should be stored at -20°C.

Preparation Note

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.

Optional

Referencia del producto
Descripción
Precios

pictograms

Exclamation mark

signalword

Warning

Hazard Classifications

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

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

¿Ya tiene este producto?

Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.

Visite la Librería de documentos

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)
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.
Plasma Fibronectin: Structure and Functions (1985)
Fibronectin in Health and Disease (2018)
E Nègre et al.
The Journal of biological chemistry, 269(35), 22039-22045 (1994-09-02)
A 30-kDa proteolytic fragment from the gelatin/collagen-binding domain of fibronectin is a potent inhibitor of fibronectin binding to Candida albicans, with a molar inhibition constant equal to that of intact fibronectin. Recombinant and proteolytic fragments from the cell-, the fibrin

Protocolos

Dilute fibronectin for cell attachment, varying per cell type. Coating protocol, products, and FAQs provided.

Dilute fibronectin for cell attachment, varying per cell type. Coating protocol, products, and FAQs provided.

Dilute fibronectin for cell attachment, varying per cell type. Coating protocol, products, and FAQs provided.

Dilute fibronectin for cell attachment, varying per cell type. Coating protocol, products, and FAQs provided.

Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.

Póngase en contacto con el Servicio técnico