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
Productos recomendados
biological source
mouse
Quality Level
100
300
antibody form
purified antibody
antibody product type
primary antibodies
clone
868A11, monoclonal
species reactivity
human
packaging
antibody small pack of 25 μg
manufacturer/tradename
Chemicon®
technique(s)
ELISA: suitable
western blot: suitable
isotype
IgG1
UniProt accession no.
shipped in
ambient
storage temp.
2-8°C
Gene Information
human ... FN1(2335)
Specificity
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.
Application
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.
Research Category
Cell Structure
Cell Structure
Research Sub Category
ECM Proteins
ECM Proteins
This Anti-Fibronectin Antibody, C-terminus, clone 868A11 is validated for use in ELISA, WB for the detection of Fibronectin.
Quality
Tested
Physical form
Format: Purified
In 0.02MPB with 0.25M NaCl, pH=7.6 with 0.1% Sodium azide.
Storage and Stability
Maintain refrigerated at 2-8°C.
Other Notes
Please refer to lot specific datasheet.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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 2
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»
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Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
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
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
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
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.
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