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TIMP-1 (human neutrophils)

 
ALX-200-426-C005 5 µg 372.00 USD
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Specific inhibitor of matrix metalloproteinases (MMPs). It has no activity on mammalian membrane metalloproteinases, procollagen peptidase or on bacterial metalloproteinases such as thermolysin.

Product Details

Alternative Name:Tissue inhibitor of metalloproteinase 1
 
MW:~28kDa.
 
Source:Isolated from stimulated human neutrophils. The secreted protein consists of 184 amino acids, six disulfide bonds and two glycosylation sites containing N-linked oligosaccharides.
 
UniProt ID:P01033
 
Formulation:Liquid. In 50mM TRIS-HCl, pH 7.0, containing 200mM sodium chloride, 5mM CaCl2, 1µM ZnCl2, 0.05% BRIJ-35 and 0.05% sodium azide.
 
Purity:≥92% (SDS-PAGE, Western blot)
 
Shipping:Dry Ice
 
Short Term Storage:-20°C
 
Long Term Storage:-80°C
 
Use/Stability:TIMP-1 is very stable if stored at -80°C. It can be kept at -20°C for several months or +4°C for weeks without significant loss of activity.
 
Handling:Avoid freeze/thaw cycles.
 
Technical Info/Product Notes:Note: It is recommended to perform a preincubation of ~20 min. at 37°C to allow formation of the enzyme-inhibitor complex.
 
Regulatory Status:RUO - Research Use Only
 

Product Literature References

Shedding of the Transferrin Receptor Is Mediated Constitutively by an Integral Membrane Metalloprotease Sensitive to Tumor Necrosis Factor alpha Protease Inhibitor-2: M. Kaup, et al.; J. Biol. Chem. 277, 38494 (2002), Abstract; Full Text
Progelatinase B forms from human neutrophils. complex formation of monomer/lipocalin with TIMP-1: H. Kolkenbrock, et al.; Biol. Chem. 377, 529 (1996), Abstract;
Generation and activity of the ternary gelatinase B/TIMP-1/LMW-stromelysin-1 complex: H. Kolkenbrock, et al.; Biol. Chem. 376, 495 (1995), Abstract;
Tissue inhibitor of metalloproteinase (TIMP-2). A new member of the metalloproteinase inhibitor family: W.G. Stettler-Stevenson, et al.; J. Biol. Chem. 264, 17374 (1989), Abstract; Full Text
Stromelysin is an activator of procollagenase. A study with natural and recombinant enzymes: G. Murphy, et al.; Biochem. J. 248, 265 (1987), Abstract;
The interaction of purified rabbit bone collagenase with purified rabbit bone metalloproteinase inhibitor: T.E. Cawston, et al.; Biochem. J. 211, 313 (1983), Abstract;

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