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 :
Invitrogen
other brands :
NeoMarkers, Lab Vision, Endogen, Pierce, BioSource International, Zymed Laboratories, Caltag, Molecular Probes, Research Genetics, Life Technologies, Applied Biosystems, GIBCO BRL, ABgene, Dynal, Affinity BioReagents, Nunc, Invitrogen, NatuTec, Oxoid, Richard-Allan Scientific, Arcturus, Perseptive Biosystems, Proxeon, eBioscience
product type :
antibody
product name :
MMP9 Monoclonal Antibody (GE-213)
catalog :
MA5-13595
quantity :
500 uL
price :
US 480.00
clonality :
monoclonal
host :
mouse
conjugate :
nonconjugated
clone name :
GE-213
reactivity :
human
application :
immunohistochemistry, immunoprecipitation, immunohistochemistry - frozen section
citations: 50
Reference |
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Fanelli M, Chinen L, Begnami M, Costa W, Fregnami J, Soares F, et al. The influence of transforming growth factor-?, cyclooxygenase-2, matrix metalloproteinase (MMP)-7, MMP-9 and CXCR4 proteins involved in epithelial-mesenchymal transition on overall survival of patients with gastric cancer. Histopathology. 2012;61:153-61 pubmed publisher
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Tao Y, Chai D, Ma L, Zhang T, Feng Z, Cheng Z, et al. Identification of distinct gene expression profiles between esophageal squamous cell carcinoma and adjacent normal epithelial tissues. Tohoku J Exp Med. 2012;226:301-11 pubmed
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Lin C, Jin J, Yu C, Tsai W. Expression of LGR8 and related biomarkers in hepatocellular carcinoma: correlation with clinicopathological parameters. Chin J Physiol. 2011;54:161-8 pubmed
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Gonzalez L, Gonzalez Reyes S, Junquera S, Marin L, Gonzalez L, del Casar J, et al. Expression of metalloproteases and their inhibitors by tumor and stromal cells in ductal carcinoma in situ of the breast and their relationship with microinvasive events. J Cancer Res Clin Oncol. 2010;136:1313-21 pubmed publisher
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del Casar J, Gonzalez L, Alvarez E, Junquera S, Marin L, Gonzalez L, et al. Comparative analysis and clinical value of the expression of metalloproteases and their inhibitors by intratumor stromal fibroblasts and those at the invasive front of breast carcinomas. Breast Cancer Res Treat. 2009;116:39-52 pubmed publisher
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Ullmann U, Gilles C, De Rycke M, Van de Velde H, Sermon K, Liebaers I. GSK-3-specific inhibitor-supplemented hESC medium prevents the epithelial-mesenchymal transition process and the up-regulation of matrix metalloproteinases in hESCs cultured in feeder-free conditions. Mol Hum Reprod. 2008;14:169-79 pubmed publisher
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Boyd S, Tolvanen K, Virolainen S, Kuivanen T, Kyllönen L, Saarialho Kere U. Differential expression of stromal MMP-1, MMP-9 and TIMP-1 in basal cell carcinomas of immunosuppressed patients and controls. Virchows Arch. 2008;452:83-90 pubmed
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Zhang Y, Du J, Tian X, Zhong Y, Fang W. Expression of E-cadherin, beta-catenin, cathepsin D, gelatinases and their inhibitors in invasive ductal breast carcinomas. Chin Med J (Engl). 2007;120:1597-605 pubmed
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Gonzalez L, Pidal I, Junquera S, Corte M, Vazquez J, Rodriguez J, et al. Overexpression of matrix metalloproteinases and their inhibitors in mononuclear inflammatory cells in breast cancer correlates with metastasis-relapse. Br J Cancer. 2007;97:957-63 pubmed
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Cho Y, Lee W, Song S, Shin H, Yun S, Chun H. Matrix metalloproteinase-9 activity is associated with poor prognosis in T3-T4 node-negative colorectal cancer. Hum Pathol. 2007;38:1603-10 pubmed
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Kubben F, Sier C, Hawinkels L, Tschesche H, van Duijn W, Zuidwijk K, et al. Clinical evidence for a protective role of lipocalin-2 against MMP-9 autodegradation and the impact for gastric cancer. Eur J Cancer. 2007;43:1869-76 pubmed
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Vizoso F, Gonzalez L, Corte M, Rodriguez J, Vazquez J, Lamelas M, et al. Study of matrix metalloproteinases and their inhibitors in breast cancer. Br J Cancer. 2007;96:903-11 pubmed
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Hao L, Zhang C, Qiu Y, Wang L, Luo Y, Jin M, et al. Recombination of CXCR4, VEGF, and MMP-9 predicting lymph node metastasis in human breast cancer. Cancer Lett. 2007;253:34-42 pubmed
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Seo Y, Park J, Kim J, Kim J, Yeon J, Kim J, et al. Usefulness of MMP-9/TIMP-1 in predicting tumor recurrence in patients undergoing curative surgical resection for gastric carcinoma. Dig Dis Sci. 2007;52:753-9 pubmed
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Rönkkö S, Rekonen P, Kaarniranta K, Puustjarvi T, Teräsvirta M, Uusitalo H. Matrix metalloproteinases and their inhibitors in the chamber angle of normal eyes and patients with primary open-angle glaucoma and exfoliation glaucoma. Graefes Arch Clin Exp Ophthalmol. 2007;245:697-704 pubmed
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El Kenawy A, Lotfy M, El Kott A, El Shahat M. Significance of matrix metalloproteinase 9 and CD34 expressions in esophageal carcinoma: correlation with DNA content. J Clin Gastroenterol. 2005;39:791-4 pubmed
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Park K, Hwang S, Sheen S, Oh Y, Han J, Lee K. Expression of matrix metalloproteinase-9 in pleural effusions of tuberculosis and lung cancer. Respiration. 2005;72:166-75 pubmed
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Sun C, Cheng C, Chien C, Pang J, Ku W, Chen P, et al. Role of matrix metalloproteinase-9 in ex vivo expansion of human limbal epithelial cells cultured on human amniotic membrane. Invest Ophthalmol Vis Sci. 2005;46:808-15 pubmed
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Ciborowski P, Enose Y, Mack A, Fladseth M, Gendelman H. Diminished matrix metalloproteinase 9 secretion in human immunodeficiency virus-infected mononuclear phagocytes: modulation of innate immunity and implications for neurological disease. J Neuroimmunol. 2004;157:11-6 pubmed
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Stefanidakis M, Ruohtula T, Borregaard N, Gahmberg C, Koivunen E. Intracellular and cell surface localization of a complex between alphaMbeta2 integrin and promatrix metalloproteinase-9 progelatinase in neutrophils. J Immunol. 2004;172:7060-8 pubmed
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Alami J, Williams B, Yeger H. Derivation and characterization of a Wilms' tumour cell line, WiT 49. Int J Cancer. 2003;107:365-74 pubmed
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Zhang S, Li L, Lin J, Lin H. Imbalance between expression of matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 in invasiveness and metastasis of human gastric carcinoma. World J Gastroenterol. 2003;9:899-904 pubmed
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Ratzinger G, Stoitzner P, Ebner S, Lutz M, Layton G, Rainer C, et al. Matrix metalloproteinases 9 and 2 are necessary for the migration of Langerhans cells and dermal dendritic cells from human and murine skin. J Immunol. 2002;168:4361-71 pubmed
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Maguen E, Zorapapel N, Zieske J, Ninomiya Y, Sado Y, Kenney M, et al. Extracellular matrix and matrix metalloproteinase changes in human corneas after complicated laser-assisted in situ keratomileusis (LASIK). Cornea. 2002;21:95-100 pubmed
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product information
Product Type :
Antibody
Product Name :
MMP9 Monoclonal Antibody (GE-213)
Catalog # :
MA5-13595
Quantity :
500 uL
Price :
US 480.00
Clonality :
Monoclonal
Purity :
Protein G
Host :
Mouse
Reactivity :
Human
Applications :
Immunohistochemistry (Frozen): Assay-dependent, Immunoprecipitation: 2 ug/mL, Inhibition Assays: 2-4 ug/mL
Species :
Human
Clone :
GE-213
Isotype :
IgG1
Storage :
4 C
Description :
MMP9 (matrix metallopeptidase 9, GELB, CLG4B) is a matrix metalloproteinase, a family of zinc and calcium-dependent endopeptidases that degrade extracellular matrix proteins. MMP9 is secreted as a 92kDa zymogen and cleavage of pro-MMP9 results in the active enzyme with a molecular weight of 82kDa. MMP9 has a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. MMP9 is produced by monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts and endothelial cells, and is involved in inflammatory responses, tissue remodeling, wound healing, tumor growth and metastasis. MMP9 is supplied by bone marrow-derived cells and contributes to skin carcinogenesis. Further, MMP9 degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. Studies have shown that elevated MMP9 is associated with progression of idiopathic atrial fibrillation and aortic aneurysm.
Immunogen :
Purified human MMP-9
Format :
Liquid
Applications w/Dilutions :
Immunohistochemistry (Frozen): Assay-dependent, Immunoprecipitation: 2 ug/mL, Inhibition Assays: 2-4 ug/mL
Aliases :
67 kDa matrix metalloproteinase-9; 82 kDa matrix metalloproteinase-9; 92 kDa gelatinase; 92 kDa type IV collagenase; 92kD gelatinase; 92kD type IV collagenase; 92kDa gelatinase; 92kDa type IV collagenase; 92-kDa type IV collagenase; AW743869; B/MMP9; Clg4b; collagenase type IVB; fj05a08; Gel B; gelatinase B; Gelatinase-B; GELB; macrophage gelatinase; MANDP2; matrix metallo protease; matrix metallopeptidase 9; matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); matrix metalloproteinase 9; matrix metalloproteinase 9 (gelatinase B 92-kDa type IV collagenase); matrix metalloproteinase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); matrix metalloproteinase 9 (gelatinase B, 92kDa matrix metalloproteinase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); matrix metalloproteinase 9 (gelatinase B, 92-kDa type IV collagenase); Matrix metalloproteinase9; matrix metalloproteinase-9; MMP; Mmp9; MMP-9; mmp9 protein; MMP-9 protein; MMPs; Preproform of 92-kDa type IV collagenase (MMP-9): N-terminal; pro-MMP-9; type IV collagenase; type V collagenase; wu:fb02g06; wu:fb07b05; wu:fi98c09; wu:fj05a08; ZFMMP-9; zgc:64165
company information
Invitrogen
Thermo Fisher Scientific
81 Wyman Street
Waltham, MA USA 02451
https://www.thermofisher.com81 Wyman Street
Waltham, MA USA 02451
800-678-5599
headquarters: USA
questions and comments