AB19015
Anti-MMP-2 Antibody, catalytic domain
Chemicon®, from rabbit
Synonym(s):
Gelatinase A, 72 kDa Type IV Collagenase
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
biological source
rabbit
Quality Level
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)
Specificity
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.
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.
Linkage
Replaces: 04-1048
Physical form
Format: Purified
Purified immunoglobulin. Liquid in PBS, containing 0.05% sodium azide.
Storage and Stability
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.
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 Code
10 - 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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Find documentation for the products that you have recently purchased in the Document Library.
Merry L Lindsey et al.
Cardiovascular research, 66(2), 410-419 (2005-04-12)
To evaluate the effects of aging on left ventricular (LV) geometry, collagen levels, matrix metalloproteinase (MMP) and tissue inhibitor of metalloproteinase (TIMP) abundance, and myocardial fibroblast function. Young (3-month-old; n=28), middle-aged (MA; 15-month-old; n=17), and old (23-month-old; n=16) CB6F1 mice
Preconditioning decreases ischemia/reperfusion-induced release and activation of matrix metalloproteinase-2.
Manoj M Lalu,Csaba Csonka,Zoltan Giricz,Tamas Csont,Richard Schulz,Peter Ferdinandy
Biochemical and biophysical research communications null
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
Preconditioning with chronic cerebral hypoperfusion reduces a focal cerebral ischemic injury and increases apurinic/apyrimidinic endonuclease/redox factor-1 and matrix metalloproteinase-2 expression.
Sun-Ah Choi,Eun Hee Kim,Jong Yun Lee,Hyo Suck Nam,Seo Hyun Kim,Gyung Whan Kim et al.
Current neurovascular research null
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
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