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MAB13406

Sigma-Aldrich

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

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
Research Sub Category
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.

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.

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

12 - Non Combustible Liquids

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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