Key features and details
- Expression system: Native
- Purity: > 95% SDS-PAGE
- Active: Yes
- Suitable for: Functional Studies, Inhibition Assay, SDS-PAGE
Product nameNative human MMP9/ TIMP1/Lipocalin protein (Complex)
Biological activityThe specific activity of ab134445 after trypsin activation is >600 mU/mg. 1 U is the activity that hydrolyzes 1 µmol peptide (7-methoxycoumarin-4-yl) acetyl-Pro-Leu-Gly-Leu-(3-[2, 4-initrophenyl]-L- 2, 3-diamino-propionyl)-Ala-Arg-NH2 (Mca-Pro-Leu-GlyLeu-Dpa-Ala-Arg) within 1 minute.
Purity> 95 % SDS-PAGE.
Protein lengthFull length protein
Predicted molecular weight130 kDa
Our Abpromise guarantee covers the use of ab134445 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.
Purified progelatinase B monomer can serve as antigen standard in immunochemical analyses. Active gelatinase B is used to study the degradation of extracellular matrix proteins, to screen inhibitors of matrix metalloproteinases and to characterize inhibitor actions.
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, 0.0001% 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
RelevanceMMP9 may play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide. TIMP1 complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Also mediates erythropoiesis in vitro; but, unlike IL3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. Known to act on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Lipocalin could play a role in taste reception. Could be necessary for the concentration and delivery of sapid molecules in the gustatory system. Can bind various ligands, with chemical structures ranging from lipids and retinoids to the macrocyclic antibiotic rifampicin and even to microbial siderophores. Exhibits an extremely wide ligand pocket.
SDS-PAGE (reducing) analysis of ab134445.
ab134445 consists of 668 amino acids with a calculated MWt of 76 kDa. Due to N- and O-linked glycosylation the MWt in SDS-PAGE is about 92 kDa. MMP9/TIMP1/Lipocalin from neutrophil granulocytes displays three bands on SDS-PAGE 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 Lipocalin.
Lane 1: MMP9
Lane 2: MMP9/TIMP1/Lipocalin
Lane 3: MMP9/TIMP1
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.
ab134445 has not yet been referenced specifically in any publications.