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MAB13414

Sigma-Aldrich

Anti-MMP-7 Antibody, clone ID-2

clone ID-2, Chemicon®, from mouse

Sinonimo/i:

Matrilysin, PUMP-1

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About This Item

Codice UNSPSC:
12352203
eCl@ss:
32160702
NACRES:
NA.41

Origine biologica

mouse

Livello qualitativo

Forma dell’anticorpo

purified antibody

Tipo di anticorpo

primary antibodies

Clone

ID-2, monoclonal

Reattività contro le specie

human

Produttore/marchio commerciale

Chemicon®

tecniche

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

Isotipo

IgG2bκ

N° accesso NCBI

N° accesso UniProt

Condizioni di spedizione

wet ice

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... MMP7(4316)

Descrizione generale

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.

Specificità

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).

Immunogeno

Recombinant human matrilysin.

Applicazioni

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.

Stato fisico

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.

Stoccaggio e stabilità

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

Risultati analitici

Control
POSITIVE CONTROL: Bladder, breast, and ovarian carcinomas.

Altre note

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Note legali

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

Esclusione di responsabilità

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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Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 2

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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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
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
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
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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