MAB3308
Anti-MMP-2 Antibody, a.a. 468-483 hMMP2, clone 42-5D11
clone 42-5D11, Chemicon®, from mouse
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
Recommended Products
biological source
mouse
Quality Level
antibody form
purified antibody
antibody product type
primary antibodies
clone
42-5D11, monoclonal
species reactivity
rat, bovine, human, rabbit, horse, mouse, pig
manufacturer/tradename
Chemicon®
technique(s)
ELISA: suitable
immunohistochemistry: suitable (paraffin)
western blot: suitable
isotype
IgG1κ
NCBI accession no.
UniProt accession no.
shipped in
dry ice
target post-translational modification
unmodified
Gene Information
human ... MMP2(4313)
General description
The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane-bound zinc endopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non-fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer′s, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.
MMP2, also known as Gelatinase A, is a type IV collagenase that specifically cleaves type IV collagen, the major structural component of basement membranes. The metastatic potential of tumor cells has been found to correlate with the activity of this enzyme.
MMP2, also known as Gelatinase A, is a type IV collagenase that specifically cleaves type IV collagen, the major structural component of basement membranes. The metastatic potential of tumor cells has been found to correlate with the activity of this enzyme.
Specificity
Specifically reacts with precursor and active forms of human MMP-2. Does not cross react with human MMP-1, -3, -9, or -13. Also reacts with rat, mouse, and bovine MMP2, other species not tested.
Immunogen
Epitope: a.a. 468-483 hMMP2
Synthetic oligopeptide corresponding to amino acid residue 468-483 (VTPRDKPMGPLLVATF) of human matrix metalloproteinase 2 (human MMP-2, gelatinase A).
Application
Immunoblotting 1-5 μg/mL
Immunohistochemistry on frozen and paraffin-embedded tissues using PLP fixation: 1-5 μg/mL (has not been tested in traditional formalin fixed tissues)
ElA
Immunohistochemistry on frozen and paraffin-embedded tissues using PLP fixation: 1-5 μg/mL (has not been tested in traditional formalin fixed tissues)
ElA
Research Category
Cell Structure
Cell Structure
Research Sub Category
MMPs & TIMPs
MMPs & TIMPs
This Anti-MMP-2 Antibody, a.a. 468-483 hMMP2, clone 42-5D11 is validated for use in ELISA, IH(P), WB for the detection of MMP-2.
Target description
72 kDa
Physical form
Format: Purified
Liquid in 0.1 M sodium phosphate buffer, pH 7.0 containing 2% protease free bovine Serum albumin.
Protein A purified
Storage and Stability
Maintain for 1 year at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Analysis Note
Control
Lung, nerve, and various soft tissue tumors
Lung, nerve, and various soft tissue tumors
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
Manufactured by Daiichi Fine Chemical Co., Ltd
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.
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
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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A one-step sandwich enzyme immunoassay for human matrix metalloproteinase 2 (72-kDa gelatinase/type IV collagenase) using monoclonal antibodies
Fujimoto, N. et al.
Clinica Chimica Acta; International Journal of Clinical Chemistry, 221, 91-103 (1993)
Alteration of matrix metalloproteinases in selective left ventricular adriamycin-induced cardiomyopathy in the pig.
Goetzenich A, Hatam N, Zernecke A, Weber C, Czarnotta T, Autschbach R, Christiansen S
The Journal of Heart and Lung Transplantation : the Official Publication of the International Society For Heart Transplantation null
Expression of MMP-2 and MMP-9 in the rat trigeminal ganglion during the development of temporomandibular joint inflammation.
Nascimento, GC; Rizzi, E; Gerlach, RF; Leite-Panissi, CR
Brazilian journal of medical and biological research null
Glycogen synthase kinase-3beta is activated by matrix metalloproteinase-2 mediated proteolysis in cardiomyoblasts.
Kandasamy, Arulmozhi D and Schulz, Richard
Cardiovascular Research, 83, 698-706 (2009)
C S Ceron et al.
British journal of pharmacology, 160(1), 77-87 (2010-03-25)
Increased oxidative stress and up-regulation of matrix metalloproteinases (MMPs) may cause structural and functional vascular changes in renovascular hypertension. We examined whether treatment with spironolactone (SPRL), hydrochlorothiazide (HCTZ) or both drugs together modified hypertension-induced changes in arterial blood pressure, aortic
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