MMP2 Polyclonal Antibody | Invitrogen PA5-85197 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 Polyclonal Antibody

catalog :

PA5-85197

quantity :

100 uL

price :

US 454.00

clonality :

polyclonal

host :

domestic rabbit

conjugate :

nonconjugated

reactivity :

human

application :

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

citations: 7

Reference
Zhao Y, Chen J, Xu S, Chen Y. CircMETTL15 induces TMTC3 production by absorbing miR-944 to promote hepatocellular carcinoma cell malignancy. J Biochem Mol Toxicol. 2024;38:e23567 pubmed publisher
Xu Y, Yang Q, Fang Z, Tan X, Zhang M, Chen W. TRIM66 Promotes Malignant Progression of Non-Small-Cell Lung Cancer Cells via Targeting MMP9. Comput Math Methods Med. 2022;2022:6058720 pubmed publisher
Wang H, Luo Y, Chu Z, Ni T, Ou S, Dai X, et al. Poria Acid, Triterpenoids Extracted from Poria cocos, Inhibits the Invasion and Metastasis of Gastric Cancer Cells. Molecules. 2022;27: pubmed publisher
Chu Z, Luo Y, Ni T, Zhu M, Feng X, Liu Y, et al. Betulonic Acid, as One of the Active Components of the Celastrus orbiculatus Extract, Inhibits the Invasion and Metastasis of Gastric Cancer Cells by Mediating Cytoskeleton Rearrangement In Vitro. Molecules. 2022;27: pubmed publisher
Alzahrani A, Rajendran P, Veeraraghavan V, Hanieh H. Cardiac Protective Effect of Kirenol against Doxorubicin-Induced Cardiac Hypertrophy in H9c2 Cells through Nrf2 Signaling via PI3K/AKT Pathways. Int J Mol Sci. 2021;22: pubmed publisher
Li Y, Gong H, Feng L, Mao D, Xiao Y, Wang Y, et al. Chondroitin polymerizing factor promotes breast carcinoma cell proliferation, invasion and migration and affects expression of epithelial-mesenchymal transition-related markers. FEBS Open Bio. 2021;11:423-434 pubmed publisher
Tagliatela A, Hempstead S, Hibshman P, Hockenberry M, Brighton H, Pecot C, et al. Coronin 1C inhibits melanoma metastasis through regulation of MT1-MMP-containing extracellular vesicle secretion. Sci Rep. 2020;10:11958 pubmed publisher

product information

Product Type :

Antibody

Product Name :

MMP2 Polyclonal Antibody

Catalog # :

PA5-85197

Quantity :

100 uL

Price :

US 454.00

Clonality :

Polyclonal

Purity :

Antigen affinity chromatography

Host :

Rabbit

Reactivity :

Human

Applications :

Immunocytochemistry: 1:100-1:1,000, Immunohistochemistry (Paraffin): 1:100-1:1,000, Immunoprecipitation: 1:100-1:500, Western Blot: 1:500-1:3,000

Species :

Human

Isotype :

IgG

Storage :

Store at 4 C short term. For long term storage, store at -20 C, avoiding freeze/thaw cycles.

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 :

Recombinant protein encompassing a sequence within the center region of human MMP2.

Format :

Liquid

Applications w/Dilutions :

Immunocytochemistry: 1:100-1:1,000, Immunohistochemistry (Paraffin): 1:100-1:1,000, Immunoprecipitation: 1:100-1:500, Western Blot: 1:500-1:3,000

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