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MAB13414

Sigma-Aldrich

Anti-MMP-7 Antibody, clone ID-2

clone ID-2, Chemicon®, from mouse

Synonym(s):

Matrilysin, PUMP-1

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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

ID-2, monoclonal

species reactivity

human

manufacturer/tradename

Chemicon®

technique(s)

immunofluorescence: suitable
immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable

isotype

IgG2bκ

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... MMP7(4316)

General description

Matrix metalloproteinases (MMPs) are a family of enzymes that are responsible for the degradation of extracellular matrix components such as collagen, laminin and proteoglycans. In addition to sequence homology, all MMPs share the following characteristics: the catalytic mechanism is dependent upon a zinc ion at the active center, they cleave one or more extracellular matrix components, they are secreted as zymogens which are activated by removal of an approximately 10 kDa segment from the N-terminus and they are inhibited by tissue inhibitor of metalloproteinases (TIMP). These enzymes are involved in normal physiological processes such as embryogenesis and tissue remodeling and may play an important role in angiogenesis, arthritis, periodontitis, and metastasis. Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28 kDa proenzyme and can be activated in vitro by organomercurials (e.g., 4-aminophenylmercuric acetate, APMA) and trypsin and in vivo by MMP-3 to a 18 kDa active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, pancreatic carcinomas and approximately 50% of gliomas.

Specificity

Antibody recognizes proteins of ~28 kDa and ~18 kDa which are identified as pro (latent) and active forms of matrix metalloproteinase-7. The antibody shows no cross-reaction with the pro and active forms of other MMPs.

Cellular Localization: Cytoplasmic (Visscher et al., 1994).

Immunogen

Recombinant human matrilysin.

Application

Immunofluorescence

Immunohistochemistry on frozen and formalin-fixed paraffin embedded tissue sections: 1:100-1:200 for 60 minutes at room temperature*.

*No pretreatment /antigen retrieval required for staining routine formalin-fixed, paraffin embedded sections.

Optimal working dilutions must be determined by end user.
Research Category
Cell Structure
Research Sub Category
MMPs & TIMPs
This Anti-MMP-7 Antibody, clone ID-2 is validated for use in IF, IH, IH(P) for the detection of MMP-7.

Physical form

Format: Purified
Purified from ascites fluid by Protein A chromatography. Liquid in 10 mM PBS, pH 7.4, with 0.2% BSA and 15 mM sodium azide.

Storage and Stability

Maintain at 2-8°C in undiluted aliquots for up to 12 months from date of receipt.

Analysis Note

Control
POSITIVE CONTROL: 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 Code

12 - Non Combustible Liquids

WGK

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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Seong Woo Hong et al.
Journal of the Korean Society of Coloproctology, 27(3), 133-139 (2011-08-11)
Matrix metalloproteinase-2 (MMP-2) and MMP-7 have been implicated in tumor growth and metastasis. This study aimed to investigate the expressions of MMP-2 and -7 in colorectal cancer and to evaluate their values as prognostic markers. Immunohistochemical staining for MMP-2 and
Barbara Grzechocinska et al.
Folia histochemica et cytobiologica, 56(3), 133-140 (2018-09-07)
Endometrium undergoes regular, cyclic tissue remodeling mostly associated to the endocrine system status. It is well-known fact that steroid hormones are strongly responsible for changes in endometrium. The precise mechanism of their action is still under investigation. The aim of
The loss of tuberin promotes cell invasion through the ?-catenin pathway.
Barnes, EA; Kenerson, HL; Mak, BC; Yeung, RS
American Journal of Respiratory Cell and Molecular Biology null
Wee J Chng et al.
Blood, 113(3), 635-645 (2008-11-01)
We conducted comprehensive gene expression profiling (GEP) of primary pulmonary mucosa-associated lymphoid tissue (MALT) lymphoma (n = 33) and compared the results to GEP of other B- and T-cell lymphomas and normal lymphocytes to identify novel markers and deregulated pathways.
Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase.
Fu, X; Kassim, SY; Parks, WC; Heinecke, JW
The Journal of Biological Chemistry null

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