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MAB3308

Sigma-Aldrich

Anti-MMP-2 Antibody, a.a. 468-483 hMMP2, clone 42-5D11

clone 42-5D11, Chemicon®, from mouse

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Synonym(s):
Gelatinase A, 72 kDa Type IV Collagenase
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

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.

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
Research Category
Cell Structure
Research Sub Category
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

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.

WGK

WGK 2


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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Xiaohu Fan et al.
American journal of physiology. Heart and circulatory physiology, 311(1), H183-H189 (2016-05-21)
Cardiomyocyte dedifferentiation may be an important source of proliferating cardiomyocytes facilitating cardiac repair. Cardiomyocyte dedifferentiation and proliferation induced by oncostatin-M (OSM) is characterized by sarcomere degeneration. However, the mechanism underlying sarcomere degeneration remains unclear. We hypothesized that this process may
Hien Thi Vu et al.
BioMed research international, 2018, 5971080-5971080 (2018-09-19)
All-trans retinoic acid (ATRA) is an effective drug for the induction therapy of acute promyelocytic leukemia. However, the treatment is associated with adverse events such as retinoic acid syndrome (RAS) in some patients, whose histologic characteristics included organ infiltration by
S B A Cau et al.
British journal of pharmacology, 164(2), 372-381 (2011-03-26)
Mounting evidence implicates matrix metalloproteinase (MMP) in the vascular dysfunction and remodelling associated with hypertension. We tested the hypothesis that treatment with pyrrolidine dithiocarbamate (PDTC), which interferes with NF-κB-induced MMPs gene transcription, could exert antihypertensive effects, prevent MMP-2 and MMP-9
Hazem Akkad et al.
PloS one, 9(4), e92622-e92622 (2014-04-08)
Critical illness myopathy (CIM) is a debilitating common consequence of modern intensive care, characterized by severe muscle wasting, weakness and a decreased myosin/actin (M/A) ratio. Limb/trunk muscles are primarily affected by this myopathy while cranial nerve innervated muscles are spared
Stefany B A Cau et al.
Basic & clinical pharmacology & toxicology, 117(4), 234-241 (2015-03-31)
Imbalanced matrix metalloproteinase (MMP) activity is involved in hypertensive cardiac hypertrophy. Pharmacological inhibition of nuclear factor kappaB (NF-кB) with pyrrolidine dithiocarbamate (PDTC) can prevent MMP up-regulation. We suggested that treatment with PDTC could prevent 2-kidney, 1-clip (2K1C) hypertension-induced left ventricular

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