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MMP-9 (hinge region) polyclonal antibody

 
BML-SA680-0100 100 µg 258.00 USD
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Product Specification

Alternative Name:Matrix metalloproteinase 9, Gelatinase B, 92kDa Type IV collagenase
 
Host:Rabbit
 
Immunogen:Synthetic peptide corresponding to the hinge region of human MMP-9.
 
UniProt ID:P14780
 
Species reactivity:Human, Mouse, Rat
Bovine, Monkey
 
Specificity:Recognizes latent (92 and 88kDa) and active (68kDa and smaller) forms of MMP-9.
 
Crossreactivity:Does not cross-react with MMP-2 (Gelatinase A) or other MMPs.
 
Applications:ELISA, WB
 
Recommended Dilutions/Conditions:Western Blot (1:1,000 using colorimetric substrates, 1:5,000 using chemiluminescent substrates. Suggested incubation time is overnight at +4°C)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
 
Purity Detail:Affinity purified.
 
Formulation:Liquid. In PBS containing 50% glycerol.
 
Use/Stability:Stable for at least 6 months after receipt when stored undiluted at -20°C.
 
Handling:Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -20°C.
 
Shipping:Shipped on Blue Ice
 
Long Term Storage:-20°C
 
Technical Info/Product Notes:Replacement for ADI-905-486
 
bml-sa680
Figure: Western blot analysis using PAb to MMP-9 (Hinge Region) (Prod. No. BML-SA680). Lane 1: 50ng purified MMP-1, 2: 50ng purified MMP-2, 3: 50ng purified MMP-3, 4: 50ng purified MMP-8, 5: 50ng purified MMP-9, 6: 50ng purified MMP-12, 7: 50ng full-length recombinant MMP-13, 8: rat brain, 9: mouse thymus, 10: Jurkat cell extract (human), 11: rat liver, 12: PC12 cell extract (rat).
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bml-sa680

General Literature References

Mechanism of activation of human neutrophil gelatinase B. Discriminating between the role of Ca2+ in activation and catalysis: C.H. Bu & T. Pourmotabbed; J. Biol. Chem 270, 18563 (1995), Abstract; Full Text
Interaction of 92-kDa type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerization, complex formation with interstitial collagenase, and activation of the proenzyme with stromelysin: G.I. Goldberg, et al.; J. Biol. Chem. 267, 4583 (1992), Abstract; Full Text

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