GW20021F
Anti-Fibronectin Antibody
chicken polyclonal
Synonym(s):
Anti-Cold-insoluble globulin, Anti-FN
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About This Item
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Product Name
Anti-Fibronectin antibody produced in chicken, affinity isolated antibody, buffered aqueous solution
biological source
chicken
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
species reactivity
human, mouse, rat
manufacturer/tradename
Genway 15-288-20021F
concentration
1.0-1.2 mg/mL
technique(s)
indirect ELISA: suitable
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... FN1(2335)
General description
The gene FN1 (Fibronectin) is mapped to human chromosome 2q34. It is present as a soluble dimeric form in plasma. At the cell surface and in the extracellular matrix, it is present as a dimeric or multimeric form.
Application
Anti-Fibronectin antibody produced in chicken is suitable for western blotting at a working dilution of 1:500 and for cell staining at a working dilution of 1:200. It is also suitable for indirect ELISA.
Biochem/physiol Actions
Fibronectin (FN1) is a glycoprotein that is involved in cell adhesion and migration processes, such as embryogenesis, wound healing, blood coagulation, host defense, and metastasis. It binds to cell surfaces and compounds, such as collagen, fibrin, heparin, fibulin, integrins, cell adhesive mac-2 binding protein (M2BP), cartilage oligomeric matrix protein (COMP), DNA, and actin. Fibronectin interaction with FLRG (Follistatin-related gene protein) and follistatin is important for human hematopoietic cell adhesiveness. It is associated with glomerulopathy with fibronectin deposits, an autosomal dominant disease. Polymorphism in gene is linked with increased risk of knee osteoarthritis. Human pathogens, Staphylococcus aureus and Streptococcus pyogenes, target fibronectin for adhesion to and invasion of host cells. Pigment epithelium-derived factor (PEDF) down-regulates fibronectin to suppress breast cancer metastasis.
Physical form
Solution in phosphate buffered saline containing 0.02% sodium azide.
Disclaimer
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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Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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R Carlsson et al.
Proceedings of the National Academy of Sciences of the United States of America, 78(4), 2403-2406 (1981-04-01)
Laminin, a basement membrane glycoprotein isolated from cultures of mouse endodermal cells and rat yolk sac carcinoma cells, promoted the attachment of liver cells obtained from regenerating mouse liver. Cells from normal mouse liver attached readily to dishes coated with
Myelin-reactive B cells exacerbate CD4+ T cell-driven CNS autoimmunity in an IL-23-dependent manner.
Mohamed Reda Fazazi et al.
Nature communications, 15(1), 5404-5404 (2024-06-27)
B cells and T cells collaborate in multiple sclerosis (MS) pathogenesis. IgH[MOG] mice possess a B cell repertoire skewed to recognize myelin oligodendrocyte glycoprotein (MOG). Here, we show that upon immunization with the T cell-obligate autoantigen, MOG[35-55], IgH[MOG] mice develop
Natalia B Pikor et al.
Immunity, 43(6), 1160-1173 (2015-12-20)
Tertiary lymphoid tissues (TLTs) have been observed in the meninges of multiple sclerosis (MS) patients, but the stromal cells and molecular signals that support TLTs remain unclear. Here, we show that T helper 17 (Th17) cells induced robust TLTs within
E Engvall et al.
International journal of cancer, 20(1), 1-5 (1977-07-15)
Fibronectin, a plasma protein immunologically identical with a major surface protein of normal fibroblasts, was found to bind to collagen and gelatin. A solid phase enzyme immunoassay was used for the binding tests. Collagen, gelatin or various control proteins were
C Ffrench-Constant et al.
The Journal of cell biology, 109(2), 903-914 (1989-08-01)
The adhesive extracellular matrix glycoprotein fibronectin (FN) is thought to play an important role in the cell migration associated with wound healing. Immunolocalization studies show abundant FN in healing wounds; however, these studies cannot define the cellular site(s) of FN
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