Key features and details
- Expression system: Native
- Purity: > 95% SDS-PAGE
- Active: Yes
- Suitable for: SDS-PAGE, Functional Studies
Product nameNative human MMP9 /TIMP1 protein (Complex)
The specific activity of ab134451 after trypsin activation is >300 mU/mg. 1 U is the activity that hydrolyzes 1 µmol peptide (7-methoxycoumarin-4-yl) acetyl-Pro-Leu-Gly-Leu-(3-[2, 4-dinitrophenyl]-L- 2, 3-diamino-propionyl)-Ala-Arg-NH2 (Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg) within 1 min.
Purity> 95 % SDS-PAGE.
ab134451 is >95% homogenous by electrophoresis and Western Blotting analysis.
Protein lengthFull length protein
Our Abpromise guarantee covers the use of ab134451 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Gelatinase B is inhibited by tissue inhibitors of matrix metalloproteinases (TIMP) and by chelators of divalent cations as EDTA or o-phenanthroline.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Preservative: 0.05% Sodium azide
Constituents: 0.05% Brij, 0.05% Calcium chloride, 0.00001% Zinc chloride, 0.79% Tris HCl, 1.17% Sodium chloride
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- 92 kDa gelatinase
- 92 kDa type IV collagenase
RelevanceHuman progelatinase B consists of 668 amino acids with a calculated Mr of 76240 Da. Due to N- and O-linked glycosylation the Mr in SDS-PAGE is about 92 kDa. 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+ -ions 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 gelatinase B. The hemopexin domain of the latent enzyme binds TIMP-1. Gelatinase B from neutrophil granulocytes displays three bands on SDS-PAGE (reducing condition) at 92, 29 and 25 kDa. The 92 kDa form represents the monomer, the 29 kDa protein band represents TIMP 1 and the 25 kDa protein which belongs to the lipocalin family and displays homology with the a2- macroglobulin related protein from rats. These proteins are capable of forming complexes, including the binary MMP9/ TIMP1 complex, which behaves like the ternary MMP9/ Lipocalin/ TIMP1 complex that it is an inhibitor for active MMPs and, after activation, a gelatinase with a reduced activity.
SDS-PAGE analysis under reducing condition:
Lane 1; MMP9
Lane 2; MMP9/ Lipocalin/ TIMP1
Lane 3; MMP9/ TIMP1
Gelatinase B from neutrophil granulocytes displays three bands on SDS-PAGE (reducing condition) at 92, 29 and 25 kDa. The 92 kDa form represents the monomer, the 29 kDa protein band represents TIMP 1 and the 25 kDa protein belongs to the lipocalin family. These proteins are capable of forming complexes, including the binary MMP9/ TIMP1 complex.
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab134451 has not yet been referenced specifically in any publications.