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Key Documents

SAB4500974

Sigma-Aldrich

Anti-Fibronectin 1 antibody produced in rabbit

affinity isolated antibody

Sinonimo/i:

CIG, FINC, cold-insoluble globulin, fibronectin, fibronectin 1

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About This Item

Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

rabbit

Livello qualitativo

Coniugato

unconjugated

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Forma fisica

buffered aqueous solution

PM

antigen 262 kDa

Reattività contro le specie

rat, mouse, human

Concentrazione

~1 mg/mL

tecniche

ELISA: 1:1000
immunohistochemistry: 1:50-1:100
western blot: 1:500-1:1000

N° accesso NCBI

N° accesso UniProt

Condizioni di spedizione

wet ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... FN1(2335)

Descrizione generale

Anti-Fibronectin 1 antibody detects endogenous levels of total Fibronectin 1 protein.
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. It is mapped to human chromosome 2q35.

Immunogeno

The antiserum was produced against synthesized peptide derived from human Fibronectin 1.

Immunogen Range: 2337-2386

Applicazioni

Anti-Fibronectin 1, C-Terminal antibody has been used in western blotting, cell staining and immunofluorescence.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)

Azioni biochim/fisiol

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.

Caratteristiche e vantaggi

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Stato fisico

Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

Esclusione di responsabilità

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.

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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

nwg

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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Ziying Jian et al.
Cellular and molecular gastroenterology and hepatology, 6(4), 429-449 (2018-09-28)
Although nearly half of pancreatic ductal adenocarcinoma (PDAC) patients have diabetes mellitus with episodes of hyperglycemia, its tumor microenvironment is hypoglycemic. Thus, it is crucial for PDAC cells to develop adaptive mechanisms dealing with oscillating glucose levels. So far, the
Colorectal Cancer Aggressiveness is Related to Fibronectin Over Expression, Driving the Activation of SDF-1:CXC
Fernandes SG, et al.
International Journal of Cancer and Clinical Research, 3(8), 72-81 (2016)
Kusuma Suphakhong et al.
The Journal of biological chemistry, 298(11), 102554-102554 (2022-10-03)
N6-methyladenosine (m6A) is the most common internal chemical modification of mRNAs involved in many pathological processes including various cancers. In this study, we investigated the m6A-dependent regulation of JUN and JUNB transcription factors (TFs) during transforming growth factor-beta-induced epithelial-mesenchymal transition
International Journal of Cancer and Clinical Research null
Epigenetic regulation of epithelial-mesenchymal transition by KDM6A histone demethylase in lung cancer cells
Terashima M, et al.
Biochemical and Biophysical Research Communications, 490(4), 1407-1413 (2017)

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