Matrix Metalloproteinase 9 Pro Monomer (MMP-9, Collagenase 4, Gelatinase B)
Catalog No : USB-M2425-40
713.81€
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| Product name | Matrix Metalloproteinase 9 Pro Monomer (MMP-9, Collagenase 4, Gelatinase B) | ||
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| Catalog No | USB-M2425-40 | ||
| Supplier’s Catalog No | M2425-40 | ||
| Supplier | US Biologicals | ||
| Source antigen | Isolated from human blood, the preparation is free from MMP-9 dimer and from complexes of MMP-9 with TIMP-1 or lipocalin. Upon activation with trypsin, enzymatically active MMP-9 of Mr 86kD is formed. | ||
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| Storage | -70°C | ||
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| Grade | Highly Purified | ||
| Purity | >95% of total protein. MMP-9 monomer appears as a major band at 92kD in non-reducing SDS-PAGE. | ||
| Form | Supplied as a liquid in 50mM Tris-HCl, pH 7.0, 200mM sodium chloride, 5mM CaCl2, 1mM ZnCl2, 0.05% Brij-35, 0.05% sodium azide. | ||
| Reactivity life | 12 months | ||
| Note | For reserch purpose only | ||
| Purity | >95% of total protein. MMP-9 monomer appears as a major band at 92kD in non-reducing SDS-PAGE. | ||
| Description | Human MMP-9 consists of 668aa with a calculated Mrof 76,240D. Due to N- and O-linked glycosylated the Mr in SDS-PAGE is about 92kD. Within the protein sequence, the following structural domains can be distinguished: An N-terminal propeptide, which confers latency to the proenzyme, a Ca2+ and Zn2+ ion-binding catalytic domain containing an insertion of three repeats homologous to type II repeats in the gelatin-binding region of fibronectin, and a C-terminal hemopexin-like domain. Catalytic and hemopexin domains are connected by a proline-rich sequence with homology to sequences in collagens. The gelatin-binding region and the hemopexin domain confer specific macromolecular substrate binding to MMP-9. The hemopexin domain of the latent enzyme binds TIMP-1. Activation of latent MMP-9 can be mediated by proteases like stromelysin, cathepsin G, kallikrein and trypsin or by incubation with APMA. In the presence of APMA, the propeptide is not removed completely, however, and there occurs considerable C-terminal self-processing. The enzyme is inhibited by TIMP-1 and TIMP-2. MMP-9 is secreted from macrophages, polymorphonuclear leukocytes, keratinocytes and many tumor cells. It is detected in human plasma and saliva. MMP-9 is involved in physiological processes such as angiogenesis, wound healing, bone remodeling, migration of macrophages and leukocytes. Hydrolysis of type IV collagen and other matrix proteins in basement membranes by MMP-9 contributes to tumor cell invasion and aortic aneurysm formation. Inhibitors: MMP-9 is inhibited by TIMPs and by chelators of divalent cations, such as EDTA or o-phenanthroline. Specific Activity: The specific activity of activated MMP-9 after trypsin activation is ≥ 450mU/mg, where 1U is the activity that hydrolyzes 1umol peptide (7-methoxycoumarin-4-yl) acetyl-Pro-Leu-Gly-Leu-(3-[2, 4- dinitrophenyl]-L-2, 3-diamino-propionyl)- Ala-Arg-NH3 (Mca-Pro-Leu-Gly-Leu-Dpa- Ala-Arg) within 1 minute under the assay conditions described by Knight, et al. Activation: An aliquot of 10ul MMP-9 monomer is mixed with 20ul trypsin solution (see below) and activation buffer in a total volume of 100ul. The mixture is incubated for 20 min at 37°C. Thereafter trypsin is inhibited by addition of 10ul aprotinin solution. Trypsin Solution: 0.50mg TPCK-trypsin/ml activation buffer. The solution is stored in aliquots at -20°C. Activation Buffer: 50mM Tris-HCl, pH 7.5, 150mM NaCl, 5mM CaCl2. Aprotinin Solution: 1mg aprotinin/ml activation buffer. The solution is stored at -20°C. Storage and Stability: Aliquot to avoid repeated freezing and thawing and store at -70°C. Aliquots are stable for 6 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. | ||
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