MAB13406
Anti-MMP-2 Antibody, pro and active form, clone VB3
clone VB3, 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
VB3, monoclonal
species reactivity
human
manufacturer/tradename
Chemicon®
technique(s)
ELISA: suitable
immunofluorescence: suitable
western blot: suitable
isotype
IgG1
suitability
not suitable for immunohistochemistry
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... MMP2(4313)
Specificity
The antibody recognizes proteins of 72kDa and 66kDa which are identified as pro (latent) and active forms of matrix metalloproteinase-2 (MMP-2; also known as 72 kDa collagenase IV or gelatinase A). Shows no cross-reactivity with pro and active forms of other MMPs. MMPs are proteolytic enzymes capable of degrading connective tissue components. Degradation of the extracellular matrix (ECM) is an essential step in tumor invasion and metastasis. MMPs each have different substrate specificities within the ECM and are important in its degradation. MMP-2 mainly degrades type IV collagen and denatured collagens. MMP activity is modulated by tissue inhibitors of metalloproteinases (TIMP). Imbalanced secretion of certain MMP or disturbances in the differential control of MMP by TIMP have been implicated in the invasive potential of malignant tumors.Cellular Localization: cytoplasmic
Immunogen
Epitope: pro and active form
Human native 72 kDa Gelatinase A.
Application
Research Category
Cell Structure
Cell Structure
Research Sub Category
MMPs & TIMPs
MMPs & TIMPs
This Anti-MMP-2 Antibody, pro & active form, clone VB3 is validated for use in ELISA, IF, WB for the detection of MMP-2.
Western blot: 1:200-1:400 for 2 hours at room temperature
ELISA
Immunofluorescence
Does not work for immunohistochemistry Optimal working dilutions must be determined by end user.
ELISA
Immunofluorescence
Does not work for immunohistochemistry Optimal working dilutions must be determined by end user.
Linkage
Replaces: 04-1048
Physical form
200 μg/mL. of antibody purified from ascites fluid by Protein G chromatography. Liquid in 10 mM PBS, pH 7.4, with 0.2% BSA and 0.09% sodium azide.
Format: Purified
Storage and Stability
Maintain refrigerated at 2-8°C in undiluted aliquots for up to 12 months.
Analysis Note
Control
POSITIVE CONTROL: Conditioned, serum-free medium from (dexametha-sone-treated) human fibrosarcoma HT-1080 or endothelial HUVEC cells. Placenta. Bladder, breast and ovarian carcinomas.
POSITIVE CONTROL: Conditioned, serum-free medium from (dexametha-sone-treated) human fibrosarcoma HT-1080 or endothelial HUVEC cells. Placenta. Bladder, breast and ovarian carcinomas.
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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wgk_germany
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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In situ detection of matrix metalloproteinase-2 (MMP2) and the metalloproteinase inhibitor TIMP2 transcripts in human primary hepatocellular carcinoma and in liver metastasis.
Musso, O, et al.
Journal of Hepatology, 26, 593-605 (1997)
J E Nutt et al.
British journal of cancer, 78(2), 215-220 (1998-07-31)
The matrix metalloproteinases are a family of enzymes that degrade the extracellular matrix and are considered to be important in tumour invasion and metastasis. The effect of epidermal growth factor (EGF) on matrix metalloproteinase-1 (MMP1) production in two human bladder
N Théret et al.
International journal of cancer, 74(4), 426-432 (1997-08-22)
Degradation of basement membranes is a key step in tumoral invasion, mainly mediated by matrix metalloproteinases (MMPs) and their inhibitors (TIMPs). Since the liver is a main target for metastases from gastrointestinal adenocarcinoma, we have investigated MMP2 and TIMP2 expression
Cigarette smoke exposure inhibits extracellular MMP-2 (gelatinase A) activity in human lung fibroblasts.
La Rocca, G; Anzalone, R; Magno, F; Farina, F; Cappello, F; Zummo, G
Respiratory Research null
Active-MMP2 in cancer cell nests of oral cancer patients: correlation with lymph node metastasis.
Kawamata, H, et al.
International journal of oncology, 13, 699-704 (1998)
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