SAB4500974
Anti-Fibronectin 1 antibody produced in rabbit
affinity isolated antibody
Synonyme(s) :
CIG, FINC, cold-insoluble globulin, fibronectin, fibronectin 1
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About This Item
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41
Produits recommandés
Source biologique
rabbit
Conjugué
unconjugated
Forme d'anticorps
affinity isolated antibody
Type de produit anticorps
primary antibodies
Clone
polyclonal
Forme
buffered aqueous solution
Poids mol.
antigen 262 kDa
Espèces réactives
rat, mouse, human
Concentration
~1 mg/mL
Technique(s)
ELISA: 1:1000
immunohistochemistry: 1:50-1:100
western blot: 1:500-1:1000
Numéro d'accès NCBI
Numéro d'accès UniProt
Conditions d'expédition
wet ice
Température de stockage
−20°C
Modification post-traductionnelle de la cible
unmodified
Informations sur le gène
human ... FN1(2335)
Description générale
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.
Immunogène
The antiserum was produced against synthesized peptide derived from human Fibronectin 1.
Immunogen Range: 2337-2386
Immunogen Range: 2337-2386
Application
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)
Western Blotting (1 paper)
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.
Caractéristiques et avantages
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.
Forme physique
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Clause de non-responsabilité
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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Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
nwg
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Les clients ont également consulté
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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
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)
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Terashima M, et al.
Biochemical and Biophysical Research Communications, 490(4), 1407-1413 (2017)
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The Journal of biological chemistry, 293(47), 18016-18030 (2018-09-29)
Long noncoding RNAs (lncRNAs) are important regulatory molecules in various biological and pathological processes, including cancer development. We have previously shown that the MEG3 lncRNA plays an essential role in transforming growth factor-β (TGF-β)-induced epithelial-mesenchymal transition (EMT) of human lung
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
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