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IM33

Sigma-Aldrich

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

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

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

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

isotype

IgG1

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... MMP2(4313)

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

Application


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

Packaging

Please refer to vial label for lot-specific concentration.

Warning

Toxicity: Standard Handling (A)

Physical form

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

Reconstitution

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

Analysis Note

Negative Control
MMP-9 protein (Cat. Nos. PF024 or PF038)
Positive Control
MMP-2 protein (Cat. Nos. PF023 or PF037)

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.

Legal Information

Manufactured by Daiichi Fine Chemical Co., Ltd. Not available for sale in Japan.
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

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Storage Class Code

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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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
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.
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
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
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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