MAB1935
Anti-Fibronectin Antibody, CT, clone 868A11
clone 868A11, Chemicon®, from mouse
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About This Item
UNSPSC-Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Empfohlene Produkte
Biologische Quelle
mouse
Qualitätsniveau
100
300
Antikörperform
purified antibody
Antikörper-Produkttyp
primary antibodies
Klon
868A11, monoclonal
Speziesreaktivität
human
Verpackung
antibody small pack of 25 μg
Hersteller/Markenname
Chemicon®
Methode(n)
ELISA: suitable
western blot: suitable
Isotyp
IgG1
NCBI-Hinterlegungsnummer
UniProt-Hinterlegungsnummer
Versandbedingung
ambient
Lagertemp.
2-8°C
Angaben zum Gen
human ... FN1(2335)
Spezifität
The C-terminal domain which contains the second fibrin binding site and it distinguishes between two major proteolytic fragments (140kd and 160dk), but not between the A and B chains. Epitope = C-terminal heparin binding fragment.
Immunogen
Epitope: C-terminus
Human plasma fibronectin.
Anwendung
Research Category
Zellstruktur
Zellstruktur
Research Sub Category
ECM-Proteine
ECM-Proteine
ELISA
Immunohistochemistry, formalin fixed, 10-25 μg/ml
Western blotting at 1-5 μg/ml
Final working dilutions must be determined by end user.
Immunohistochemistry, formalin fixed, 10-25 μg/ml
Western blotting at 1-5 μg/ml
Final working dilutions must be determined by end user.
This Anti-Fibronectin Antibody, C-terminus, clone 868A11 is validated for use in ELISA, WB for the detection of Fibronectin.
Qualität
Tested
Physikalische Form
Format: Purified
In 0.02MPB with 0.25M NaCl, pH=7.6 with 0.1% Sodium azide.
Lagerung und Haltbarkeit
Maintain refrigerated at 2-8°C.
Sonstige Hinweise
Please refer to lot specific datasheet.
Rechtliche Hinweise
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
Haftungsausschluss
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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Lagerklassenschlüssel
10 - Combustible liquids
WGK
WGK 2
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Analysenzertifikate (COA)
Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.
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Brant Hubbard et al.
Matrix biology : journal of the International Society for Matrix Biology, 34, 124-131 (2013-10-24)
Extracellular matrix (ECM) conformation is regulated by a variety of stimuli in vivo, including mechanical forces and allosteric binding partners, and these conformational changes contribute to the regulation of cell behavior. Heparin and heparan sulfate, for example, have been shown
Janette K Burgess et al.
The Journal of allergy and clinical immunology, 118(3), 649-657 (2006-09-05)
Airway smooth muscle (ASM) cells may contribute to airway remodeling through the release of growth factors, cytokines, and extracellular matrix (ECM) proteins. The effect of current asthma therapies on this release is not known. We examined the effect of corticosteroids
Binding and orientation of fibronectin on surfaces with collagen-related peptides. Student Research Award in the Masters Science Degree Candidate category, 27th annual meeting of the Society for Biomaterials, St. Paul, MN, April 24-29, 2001.
U Klueh, S Goralnick, J D Bryers, D L Kreutzer
Journal of Biomedical Materials Research null
André N Tiaden et al.
The Journal of biological chemistry, 287(25), 21335-21345 (2012-05-05)
Human HTRA1 is a highly conserved secreted serine protease that degrades numerous extracellular matrix proteins. We have previously identified HTRA1 as being up-regulated in osteoarthritic patients and as having the potential to regulate matrix metalloproteinase (MMP) expression in synovial fibroblasts
Definition of the native and denatured type II collagen binding site for fibronectin using a recombinant collagen system.
An, B; Abbonante, V; Yigit, S; Balduini, A; Kaplan, DL; Brodsky, B
The Journal of Biological Chemistry null
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