Accéder au contenu
Merck
Toutes les photos(1)

Principaux documents

MAB13414

Sigma-Aldrich

Anti-MMP-7 Antibody, clone ID-2

clone ID-2, Chemicon®, from mouse

Synonyme(s) :

Matrilysin, PUMP-1

Se connecterpour consulter vos tarifs contractuels et ceux de votre entreprise/organisme


About This Item

Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

Forme d'anticorps

purified antibody

Type de produit anticorps

primary antibodies

Clone

ID-2, monoclonal

Espèces réactives

human

Fabricant/nom de marque

Chemicon®

Technique(s)

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

Isotype

IgG2bκ

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... MMP7(4316)

Description générale

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.

Spécificité

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).

Immunogène

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.

Forme physique

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.

Stockage et stabilité

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

Remarque sur l'analyse

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

Autres remarques

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

Informations légales

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

Clause de non-responsabilité

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.

Vous ne trouvez pas le bon produit ?  

Essayez notre Outil de sélection de produits.

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

Déjà en possession de ce produit ?

Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

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
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
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.

Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..

Contacter notre Service technique