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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Conjugate:
unconjugated
Clone:
polyclonal
Application:
IP, WB
Citations:
15
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
polyclonal
species reactivity
human, mouse, rat
manufacturer/tradename
Chemicon®
technique(s)
immunoprecipitation (IP): suitable, western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... MMP2(4313)
Immunogen
E. coli-expressed active rat 72 kDa type IV collagenase (catalytic domain)
Epitope: catalytic domain
Application
Detect MMP-2 using this Anti-MMP-2 Antibody, catalytic domain validated for use in IP & WB.
Research Category
Cell Structure
Cell Structure
Research Sub Category
MMPs & TIMPs
MMPs & TIMPs
Western blot: 1:2,000
Immunoprecipitation: 1:500
MMP-2 [Gelatinase-A] is constitutively produced in quiescent cells and tissues, and the enzyme has a high specific activity against denatured collagen. The low protein levels produced in cell culture (pg/mL) are often below the threshold of detection by standard Western Blotting. The enzyme can be concentrated from culture media by gelatin-agarose affinity chromatography (Goldberg, 1992) or immunoprecipitation. This can prevent appearance of a spurious band of antibody binding in the vicinity of 68 kDa displayed by some concentrated media.
Optimal working dilutions must be determined by end user.
Immunoprecipitation: 1:500
MMP-2 [Gelatinase-A] is constitutively produced in quiescent cells and tissues, and the enzyme has a high specific activity against denatured collagen. The low protein levels produced in cell culture (pg/mL) are often below the threshold of detection by standard Western Blotting. The enzyme can be concentrated from culture media by gelatin-agarose affinity chromatography (Goldberg, 1992) or immunoprecipitation. This can prevent appearance of a spurious band of antibody binding in the vicinity of 68 kDa displayed by some concentrated media.
Optimal working dilutions must be determined by end user.
Biochem/physiol Actions
Recognizes rat MMP-2. Exhibits no cross-reactivity with other MMP family members. The antibody was generated using E. coli-expressed active rat 72 kDa type IV collagenase (catalytic domain) as an immunogen.
Physical form
Purified immunoglobulin. Liquid in PBS, containing 0.05% sodium azide.
Format: Purified
Preparation Note
Maintain refrigerated at 2-8°C in undiluted aliquots for up to 12 months.
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Replaces: 04-1048
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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wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Storage Class
12 - Non Combustible Liquids
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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Vascular cell adhesion molecule 1 (VCAM-1) activation of endothelial cell matrix metalloproteinases: role of reactive oxygen species.
Deem, TL; Cook-Mills, JM
Blood null
John R Barbour et al.
The Journal of thoracic and cardiovascular surgery, 132(4), 788-795 (2006-09-27)
An important component of matrix remodeling during thoracic aortic aneurysm progression is the balance between matrix metalloproteinases and their endogenous inhibitors (tissue inhibitors of metalloproteinases). However, whether and to what degree matrix metalloproteinase/tissue inhibitor of metalloproteinases profiles change over time
Jennifer A Kwan et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 18(6), 690-692 (2004-02-10)
Matrix metalloproteinases (MMPs) are traditionally known for their role in extracellular matrix remodeling. Increasing evidence reveals several alternative substrates and novel biological roles for these proteases. Recent evidence showed the intracellular localization of MMP-2 within cardiac myocytes, colocalized with troponin
Global Trade Item Number
| SKU | GTIN |
|---|---|
| AB19015 | 04053252274336 |