AB747
Anti-Collagen Type III Antibody
Chemicon®, from rabbit
Synonym(s):
Anti-EDS4A, Anti-EDSVASC, Anti-PMGEDSV
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
rabbit
Quality Level
antibody form
fractionated antiserum
antibody product type
primary antibodies
clone
polyclonal
species reactivity
human
manufacturer/tradename
Chemicon®
technique(s)
ELISA: suitable
immunofluorescence: suitable
suitability
not suitable for Western blot
not suitable for immunohistochemistry (Paraffin)
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... COL3A1(1281)
Specificity
The antibody reacts with native and heat denatured (non-reduced) human collagen type III. Cross reactions with other types of collagen under native conditions do occur. There is 10% cross reactivity with human collagen type I, 2% cross reactivity with human collagen type II, and 4% cross reactivity with human collagen type IV and V. There is no cross reactivity with other human plasma proteins under native ELISA conditions. Reactivity under denatured conditions has not been examined.
Cross Reactivity Percent
Human collagen type I 10%
Human collagen type II 2%
Human collagen type III 100%
Human collagen type IV and V 4%
Human plasma proteins do not interfere with binding to collagen.
Cross Reactivity Percent
Human collagen type I 10%
Human collagen type II 2%
Human collagen type III 100%
Human collagen type IV and V 4%
Human plasma proteins do not interfere with binding to collagen.
Immunogen
Human placental collagen type III
Application
ELISA 1:3,000
Indirect immunofluorescence on cryostat sections or cultured cells 1:20-1:40
Optimal working dilutions must be determined by the end user.
Indirect immunofluorescence on cryostat sections or cultured cells 1:20-1:40
Optimal working dilutions must be determined by the end user.
This Anti-Collagen Type III Antibody is validated for use in ELISA, IF for the detection of Collagen Type III.
Physical form
500ul containing of 0.15M NaCl, 10 mM sodium phosphate pH 7.5, with 0.1% mannitol and o.1% dextran as stabilizers contains no preservatives.
Immunoglobulin fraction was prepared by ammonium sulfate precipitation and chromatography on DEAE-cellulose, of antiserum cross-absorbed over immobilized human serum proteins, immunoglobulins, and collagen types I, II, IV and V.
Immunoglobulin fraction was prepared by ammonium sulfate precipitation and chromatography on DEAE-cellulose, of antiserum cross-absorbed over immobilized human serum proteins, immunoglobulins, and collagen types I, II, IV and V.
Format: Purified
Storage and Stability
Antibody is stable for 12 months from date of receipt when stored at 2-8ºC. Remove any nondispersed aggregates by microcentrifugation prior to use.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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recommended
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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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Shlomit Mendelboum Raviv et al.
Thrombosis research, 129(4), e29-e35 (2011-11-08)
Von Willebrand factor (VWF) and platelet binding needs a uniform collagen matrix therefore we aimed to find an optimal condition for the preparation of human type-I and type-III collagen matrices. The effects of pH, salt and ligand concentration and binding
The fetal fibroblast: the effector cell of scarless fetal skin repair.
H P Lorenz, R Y Lin, M T Longaker, D J Whitby, N S Adzick
Plastic and Reconstructive Surgery null
Chronic hibernating myocardium: interstitial changes.
J Ausma, J Cleutjens, F Thone, W Flameng, F Ramaekers, M Borgers
Molecular and Cellular Biochemistry null
Fibrillin microfibrils are reduced in skin exhibiting striae distensae.
R E Watson, E J Parry, J D Humphries, C J Jones, D W Polson, C M Kielty, C E Griffiths et al.
British Journal of Dermatology null
Emma J Watts et al.
Research in veterinary science, 92(2), 213-218 (2011-04-13)
Wounds on the limbs of horses are notoriously difficult to heal, with over production of TGFβ1 thought to be responsible for excessive scarring; in contrast, wounds in the oral cavity heal rapidly with minimal scarring. This experiment aimed to determine
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