MMP-9 Antibody, clone GE-213 | EMD Millipore MAB13415 product information

This webpage contains legacy information. The product is either no longer available from the supplier or has been delisted at Labome.

product summary

company name :

EMD Millipore

other brands :

Oncogene Research Products, Calbiochem, Novagen, Merck, Upstate Biotechnology, Chemicon, LINCO, Novabiochem, Guava

product type :

antibody

product name :

MMP-9 Antibody, clone GE-213

catalog :

MAB13415

quantity :

100 µg

clonality :

monoclonal

host :

mouse

conjugate :

nonconjugated

clone name :

GE-213

The same clone is also sold as:

Invitrogen: MA5-13595
LifeSpan Biosciences: LS-C88243, LS-C85299

reactivity :

human

application :

western blot, immunohistochemistry, immunoprecipitation

citations: 14

Published Application/Species/Sample/Dilution	Reference
western blot; human; 1:200; fig 2	Wei T, Zhang H, Cetin N, Miller E, Moak T, Suen J, et al. Elevated Expression of Matrix Metalloproteinase-9 not Matrix Metalloproteinase-2 Contributes to Progression of Extracranial Arteriovenous Malformation. Sci Rep. 2016;6:24378 pubmed publisher
	Cardeal L, Boccardo E, Termini L, Rabachini T, Andreoli M, Di Loreto C, et al. HPV16 oncoproteins induce MMPs/RECK-TIMP-2 imbalance in primary keratinocytes: possible implications in cervical carcinogenesis. PLoS ONE. 2012;7:e33585 pubmed publisher
	Wang R, Zhang J, Chen S, Lu M, Luo X, Yao S, et al. Tumor-associated macrophages provide a suitable microenvironment for non-small lung cancer invasion and progression. Lung Cancer. 2011;74:188-96 pubmed publisher
	Lagarrigue F, Dupuis Coronas S, Ramel D, Delsol G, Tronchère H, Payrastre B, et al. Matrix metalloproteinase-9 is upregulated in nucleophosmin-anaplastic lymphoma kinase-positive anaplastic lymphomas and activated at the cell surface by the chaperone heat shock protein 90 to promote cell invasion. Cancer Res. 2010;70:6978-87 pubmed publisher
	Fedorcsak P, Polec A, Raki M, Holm R, Jebsen P, Abyholm T. Differential release of matrix metalloproteinases and tissue inhibitors of metalloproteinases by human granulosa-lutein cells and ovarian leukocytes. Endocrinology. 2010;151:1290-8 pubmed publisher
	Saalbach A, Klein C, Schirmer C, Briest W, Anderegg U, Simon J. Dermal fibroblasts promote the migration of dendritic cells. J Invest Dermatol. 2010;130:444-54 pubmed publisher
	Kyriakides T, Wulsin D, Skokos E, Fleckman P, Pirrone A, Shipley J, et al. Mice that lack matrix metalloproteinase-9 display delayed wound healing associated with delayed reepithelization and disordered collagen fibrillogenesis. Matrix Biol. 2009;28:65-73 pubmed publisher
	MacLauchlan S, Skokos E, Meznarich N, Zhu D, Raoof S, Shipley J, et al. Macrophage fusion, giant cell formation, and the foreign body response require matrix metalloproteinase 9. J Leukoc Biol. 2009;85:617-26 pubmed publisher
	Roy R, Louis G, Loughlin K, Wiederschain D, Kilroy S, Lamb C, et al. Tumor-specific urinary matrix metalloproteinase fingerprinting: identification of high molecular weight urinary matrix metalloproteinase species. Clin Cancer Res. 2008;14:6610-7 pubmed publisher
	Saalbach A, Arnhold J, Lessig J, Simon J, Anderegg U. Human Thy-1 induces secretion of matrix metalloproteinase-9 and CXCL8 from human neutrophils. Eur J Immunol. 2008;38:1391-403 pubmed publisher
	Krupinski J, Turu M, Font M, Ahmed N, Sullivan M, Rubio F, et al. Increased tissue factor, MMP-8, and D-dimer expression in diabetic patients with unstable advanced carotid atherosclerosis. Vasc Health Risk Manag. 2007;3:405-12 pubmed
	Ries C, Pitsch T, Mentele R, Zahler S, Egea V, Nagase H, et al. Identification of a novel 82 kDa proMMP-9 species associated with the surface of leukaemic cells: (auto-)catalytic activation and resistance to inhibition by TIMP-1. Biochem J. 2007;405:547-58 pubmed
	Turu M, Krupinski J, Catena E, Rosell A, Montaner J, Rubio F, et al. Intraplaque MMP-8 levels are increased in asymptomatic patients with carotid plaque progression on ultrasound. Atherosclerosis. 2006;187:161-9 pubmed
	Yucel T, Mutnal A, Fay K, Fligiel S, Wang T, Johnson T, et al. Matrix metalloproteinase expression in basal cell carcinoma: relationship between enzyme profile and collagen fragmentation pattern. Exp Mol Pathol. 2005;79:151-60 pubmed

product information

Catalog Number :

MAB13415

Subcategory :

Cell Structure

Product Name :

Anti-MMP-9 Antibody, clone GE-213

Product Type :

Antibodies

Clonality :

Monoclonal Antibody

Gene ID :

P14780

Host Name :

Mouse

Antigen :

MMP-9

Clone :

GE-213

Conjugate :

Purified

Isotype :

IgG1

Product Description :

Anti-MMP-9 Antibody, clone GE-213

Cross Reactivity :

Human

ALT Names :

Gelatinase B; 92 kDa Type IV Collagenase

Immunogen :

Purified human gelatinase B.

Specificity :

Under non-reducing conditions, it recognizes proteins of 92 kDa and 86 kDa which are identified as pro (latent) and active forms of matrix metalloproteinase-9 (MMP-9; also known as 92 kDa and collagenase IV or gelatinase B) of human MMP-9. MAB13415 reacts with the complex (~200 kDa) of MMP-9 and tissue inhibitor of metalloproteinases-1 (TIMP-1; Nikkari et al., 1996). It shows no cross-reaction with pro and active forms of MMP-2 (Nikkari et al., 1996). Clone GE-213 also shows very low reactivity to mouse MMP-9 proteins by western blot, but at high enough antibody and antigen concentrations some detection is possible. Mouse immunhistochemistry is untested. Cellular Localization: Peripheral cytoplasmic.

Package Size :

100 µg

Uses :

Immunoprecipitation;Western Blotting;Immunohistochemistry;Affects Function

Storage :

Maintain at 2-8°C in undiluted aliquots for up to 12 months from date of receipt. During shipment, small volumes of product will occasionally become entrapped in the seal of the product vial. For products with volumes of 200μL or less, we recommend gently tapping the vial on a hard surface or briefly centrifuging the vial in a tabletop centrifuge to dislodge any liquid in the container's cap.