IM33

Anti-MMP-2 (Ab-3) Mouse mAb (42-5D11)

Name: Anti-MMP-2 (Ab-3) Mouse mAb (42-5D11)
Brand: MM

liquid, clone 42-5D11, Calbiochem^®

Synonym(s):

Anti-72 kDa Gelatinase, Anti-Gelatinase A, Anti-Matrix Metalloproteinase 2

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About This Item

NACRES:

NA.41

UNSPSC Code:

12352203

Product Name

Anti-MMP-2 (Ab-3) Mouse mAb (42-5D11), liquid, clone 42-5D11, Calbiochem^®

biological source

mouse

antibody form

purified antibody

antibody product type

primary antibodies

clone

42-5D11, monoclonal

form

liquid

contains

≤0.1% sodium azide as preservative

species reactivity

bovine, rat, mouse, human

manufacturer/tradename

Calbiochem^®

storage condition

OK to freeze
avoid repeated freeze/thaw cycles

dilution

(Frozen Sections
Immunoblotting (1 µg/mL)
Paraffin Sections )

isotype

IgG1

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

100

Gene Information

human ... MMP2(4313)

Packaging

Please refer to vial label for lot-specific concentration.

Physical form

In 100 mM sodium phosphate buffer, 0.1% BSA, pH 7.0

Preparation Note

Following initial thaw, aliquot and freeze (-20°C).

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Manufactured by Daiichi Fine Chemical Co., Ltd. Not available for sale in Japan.

Analysis Note

Negative Control
MMP-9 protein (Cat. Nos. PF024 or PF038)

Positive Control
MMP-2 protein (Cat. Nos. PF023 or PF037)

Application

Frozen Sections (see application references)
Immunoblotting (1 g/ml)
Paraffin Sections (see application references)

Disclaimer

Toxicity: Standard Handling (A)

General description

Purified mouse monoclonal antibody (see application references). Recognizes the ~72 kDa latent and the ~66 kDa active forms of MMP-2.

Recognizes the ~72 kDa latent and the ~66 kDa active forms of the MMP-2.

This Anti-MMP-2 (Ab-3) Mouse mAb (42-5D11) is validated for use in Frozen Sections, Immunoblotting, Paraffin Sections for the detection of MMP-2 (Ab-3).

Immunogen

Epitope: within amino acids 468-483 of human MMP-2 (numbered from the propeptide)

Human

a synthetic peptide (VTPRDKPMGPLLVATF) corresponding to amino acids 468-483 of human MMP-2

Other Notes

Cottam, D. W. and Rees, R. C. 1993. Intl J. Oncol.2, 861.
Fujimoto, N., et al. 1993. Clinica Chimica Acta.221, 91.
Stetler-Stevenson, W. G., et al. 1993. FASEB J.7, 1434.
Woessner, J. F. 1991. FASEB J.5, 2145.
Liotta, L. A. and Stetler-Stevenson, W. G. 1990. in Seminars in Cancer Biology, ed. M. M. Gottesman. Vol. 1(2), 99.

This antibody will not cross-react with human MMP-1, MMP-3, MMP-9, or MMP-13. Antibody should be titrated for optimal results in individual systems.

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Storage Class

10 - Combustible liquids

wgk

WGK 1

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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Alterations in membrane type-1 matrix metalloproteinase abundance after the induction of thoracic aortic aneurysm in a murine model.

Jeffrey A Jones et al.

American journal of physiology. Heart and circulatory physiology, 299(1), H114-H124 (2010-04-27)

Thoracic aortic aneurysms (TAAs) develop as a result of dysregulated extracellular matrix remodeling mediated by several matrix metalloproteinases (MMPs). Membrane type-1 MMP (MT1-MMP) is the prototypical member of a unique family of membrane-bound MMPs, possessing multiple substrates and functions. The

Otago Glaucoma Surgery Outcome Study: the pattern of expression of MMPs and TIMPs in bleb capsules surrounding Molteno implants.

Peter McCluskey et al.

Investigative ophthalmology & visual science, 50(5), 2161-2164 (2009-01-02)

To determine whether MMPs and TIMPs are present in the bleb wall of Molteno implants. An observational case series consisting of ocular specimens from 10 human eyes obtained postmortem from patients who had undergone placement of Molteno implants for glaucoma.

Membrane-type-1 matrix metalloproteinase transcription and translation in myocardial fibroblasts from patients with normal left ventricular function and from patients with cardiomyopathy.

Laura S Spruill et al.

American journal of physiology. Cell physiology, 293(4), C1362-C1373 (2007-08-03)

Past studies have identified that a unique type of matrix metalloproteinase, the membrane-type-1 MMP (MT1-MMP), is increased within the left ventricle (LV) of patients with dilated cardiomyopathy (DCM). However, the cellular and molecular basis for this induction of MT1-MMP with

In situ analysis of gelatinolytic activity in human dentin.

Thiago Henrique Scarabello Stape et al.

Acta histochemica, 120(2), 136-141 (2018-01-27)

Matrix metalloproteinases (MMPs) such as gelatinases are differentially expressed in human tissues. These enzymes cleave specific substrates involved in cell signaling, tissue development and remodeling and tissue breakdown. Recent evidences show that gelatinases are crucial for normal dentin development and

Matrix metalloproteinase activity creates pro-angiogenic environment in primary human retinal pigment epithelial cells exposed to complement.

Mausumi Bandyopadhyay et al.

Investigative ophthalmology & visual science, 53(4), 1953-1961 (2012-03-13)

Mechanistic studies have shown that inflammation, complement activation, extracellular matrix (ECM) turnover, growth factor imbalance, and oxidative stress are fundamental components of age-related macular degeneration (AMD). Matrix metalloproteinases (MMPs) mediate ECM turnover but also process various bioactive molecules. Here, we

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