MAB1935
Anti-Fibronectin Antibody, CT, clone 868A11
clone 868A11, Chemicon®, from mouse
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Product Name
Anti-Fibronectin Antibody, CT, clone 868A11, clone 868A11, Chemicon®, from mouse
technique(s)
ELISA: suitable
western blot: suitable
biological source
mouse
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®
isotype
IgG1
UniProt accession no.
shipped in
ambient
storage temp.
2-8°C
Gene Information
human ... FN1(2335)
Related Categories
Analysis Note
Tested
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.
Biochem/physiol Actions
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.
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.
Immunogen
Epitope: C-terminus
Human plasma fibronectin.
Other Notes
Please refer to lot specific datasheet.
Physical form
Format: Purified
In 0.02MPB with 0.25M NaCl, pH=7.6 with 0.1% Sodium azide.
Preparation Note
Maintain refrigerated at 2-8°C.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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Storage Class
10 - Combustible liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
新产品
This item has
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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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
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
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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