MMP2 Monoclonal Antibody (2C1-1D12) | Invitrogen 35-1300Z 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 :

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 :

MMP2 Monoclonal Antibody (2C1-1D12)

catalog :

35-1300Z

quantity :

100 µg

price :

US 430

clonality :

monoclonal

host :

mouse

conjugate :

nonconjugated

clone name :

2C1-1D12

reactivity :

human

application :

western blot, ELISA, immunohistochemistry, immunocytochemistry, immunoprecipitation, immunohistochemistry - paraffin section, immunohistochemistry - frozen section

citations: 8

Published Application/Species/Sample/Dilution	Reference
immunocytochemistry; human; loading ...; fig 6b western blot; human; 1:1000; loading ...; fig 6a	Torres Martínez A, Gallardo Vera J, Lara Holguin A, Montano L, Rendón Huerta E. Claudin-6 enhances cell invasiveness through claudin-1 in AGS human adenocarcinoma gastric cancer cells. Exp Cell Res. 2017;350:226-235 pubmed publisher
western blot; human; 1:1000; fig 2	Shih M, Pan K, Cherng J. Possible Mechanisms of Di(2-ethylhexyl) Phthalate-Induced MMP-2 and MMP-9 Expression in A7r5 Rat Vascular Smooth Muscle Cells. Int J Mol Sci. 2015;16:28800-11 pubmed publisher
western blot; human; fig s4	Al Alwan M, Olabi S, Ghebeh H, Barhoush E, Tulbah A, Al Tweigeri T, et al. Fascin is a key regulator of breast cancer invasion that acts via the modification of metastasis-associated molecules. PLoS ONE. 2011;6:e27339 pubmed publisher
immunohistochemistry; human; fig 3	Fang J, Zhou H, Zeng C, Yang J, Liu Y, Huang X, et al. MicroRNA-29b suppresses tumor angiogenesis, invasion, and metastasis by regulating matrix metalloproteinase 2 expression. Hepatology. 2011;54:1729-40 pubmed publisher
western blot; human; 1:300; fig 2	Liu H, Chen A, Guo F, Yuan L. A short-hairpin RNA targeting osteopontin downregulates MMP-2 and MMP-9 expressions in prostate cancer PC-3 cells. Cancer Lett. 2010;295:27-37 pubmed publisher
western blot; human; fig 7	Liu H, Chen A, Guo F, Yuan L. Influence of osteopontin short hairpin RNA on the proliferation and invasion of human renal cancer cells. J Huazhong Univ Sci Technolog Med Sci. 2010;30:61-8 pubmed publisher
	Chen T, Chen Z, Lian X, Wu W, Chu L, Zhang S, et al. MUC 15 Promotes Osteosarcoma Cell Proliferation, Migration and Invasion through Livin, MMP-2/MMP-9 and Wnt/β-Catenin Signal Pathway. J Cancer. 2021;12:467-473 pubmed publisher
	Anjanappa M, Cardoso A, Cheng L, Mohamad S, Gunawan A, Rice S, et al. Individualized Breast Cancer Characterization through Single-Cell Analysis of Tumor and Adjacent Normal Cells. Cancer Res. 2017;77:2759-2769 pubmed publisher

product information

Product Type :

Antibody

Product Name :

MMP2 Monoclonal Antibody (2C1-1D12)

Catalog # :

35-1300Z

Quantity :

100 µg

Price :

US 430

Clonality :

Monoclonal

Purity :

protein A

Host :

Mouse

Reactivity :

Human

Applications :

ELISA: 0.1 µg/mL, Immunohistochemistry (Frozen): 5 µg/mL, Immunohistochemistry (Paraffin): 1:10 - 1:100, Immunoprecipitation: Assay-dependent, Western Blot: 1:500

Species :

Human

Clone :

2C1-1D12

Isotype :

IgG1, kappa

Storage :

-20°C

Description :

MMP (matrix metalloproteinase) are proteolytic enzymes capable of degrading connective tissue components. MMP have a common mode of activation, a conserved amino acid sequence in the putative metal binding-active site region, and are inhibited by specific tissue inhibitors of metalloproteinases (TIMPs). MMPa and TIMPs play a significant role in regulating angiogenesis. MMP2 is synthesized as a 631 amino acid proenzyme which is activated by cleavage of the first 80 amino acids, and contains the basic structure of propeptide, catalytic, and hemopexin domains. The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane-bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non-fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc-binding site characterizes the structure of the MMPs. Functionally, MMP2 is involved in tissue remodeling. Mutations in MMP-2 gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Two transcript variants encoding different isoforms of MMP-2 have been found.

Immunogen :

Activated recombinant human MMP-2 protein.

Format :

Liquid

Applications w/Dilutions :

ELISA: 0.1 µg/mL, Immunohistochemistry (Frozen): 5 µg/mL, Immunohistochemistry (Paraffin): 1:10 - 1:100, Immunoprecipitation: Assay-dependent, Western Blot: 1:500

Aliases :

72 kDa gelatinase; 72 kDa type IV collagenase; 72 kDa type IV collagenase isoform a preproprotein; 72kD gelatinase; 72kD type IV collagenase; 72kDa gelatinase; 72kDa type IV collagenase; CLG 4A; CLG4; CLG4A; Collagenase; collagenase type IV-A; endopeptidase; GelA; gelatinase A; Gelatinase alpha; Mat; matrix metallo protease; matrix metallopeptidase 2; matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase); matrix metalloprotease 2; matrix metalloproteinase; matrix metalloproteinase 2; matrix metalloproteinase 2 (72 KDa type IV collagenase); matrix metalloproteinase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase); matrix metalloproteinase-2; matrix metalloproteinase-II; MMP; MMP2; MMP-2; MMP-2 protein; MMP-II; MMPs; MONA; neutrophil gelatinase; PEX; prepro-72kDa matrix metalloproteinase; Progelatinase A; TBE1; TBE-1; wu:fa99h12; wu:fk89d01