Human MMP-2 Recombinant Protein, PeproTech | Invitrogen 420-02-01M 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 :

protein

product name :

Human MMP-2 Recombinant Protein, PeproTech

catalog :

420-02-01M

quantity :

2 x 500 ug

price :

US 6010.00

citations: 7

Reference
Padma A, Carrière L, Krokström Karlsson F, Sehic E, Bandstein S, Tiemann T, et al. Towards a bioengineered uterus: bioactive sheep uterus scaffolds are effectively recellularized by enzymatic preconditioning. NPJ Regen Med. 2021;6:26 pubmed publisher
Hua D, Tang L, Wang W, Tang S, Yu L, Zhou X, et al. Improved Antiglioblastoma Activity and BBB Permeability by Conjugation of Paclitaxel to a Cell-Penetrative MMP-2-Cleavable Peptide. Adv Sci (Weinh). 2021;8:2001960 pubmed publisher
Li Y, Hu Q, Li C, Liang K, Xiang Y, Hsiao H, et al. PTEN-induced partial epithelial-mesenchymal transition drives diabetic kidney disease. J Clin Invest. 2019;129:1129-1151 pubmed publisher
Manders D, Kishore H, Gazdar A, Keller P, Tsunezumi J, Yanagisawa H, et al. Dysregulation of fibulin-5 and matrix metalloproteases in epithelial ovarian cancer. Oncotarget. 2018;9:14251-14267 pubmed publisher
Przybyla L, Theunissen T, Jaenisch R, Voldman J. Matrix remodeling maintains embryonic stem cell self-renewal by activating Stat3. Stem Cells. 2013;31:1097-106 pubmed publisher
Shi N, Gao W, Xiang B, Qi X. Enhancing cellular uptake of activable cell-penetrating peptide-doxorubicin conjugate by enzymatic cleavage. Int J Nanomedicine. 2012;7:1613-21 pubmed publisher
Wang Y, Tang Z, Xue R, Singh G, Lv Y, Shi K, et al. TGF-β1 promoted MMP-2 mediated wound healing of anterior cruciate ligament fibroblasts through NF-κB. Connect Tissue Res. 2011;52:218-25 pubmed publisher

product information

Product Type :

Protein

Product Name :

Human MMP-2 Recombinant Protein, PeproTech

Catalog # :

420-02-01M

Quantity :

2 x 500 ug

Price :

US 6010.00

Clonality :

Recombinant

Purity :

purified

Reactivity :

Human

Applications :

Functional Assay: Assay-dependent

Species :

Human

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.

Format :

Lyophilized

Applications w/Dilutions :

Functional Assay: Assay-dependent

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