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444231 MMP-9, Monomer, Human Neutrophil

444231
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Overview

Replacement Information

Products

Catalogue NumberPackaging Qty/Pack
444231-5UG Plastová ampulka 5 μg
Description
OverviewMonomeric, native MMP-9 from stimulated human neutrophils. Requires activation prior to use.
Note: 1 mU = 1 milliunit.
Catalogue Number444231
Brand Family Calbiochem®
SynonymsMatrix Metalloproteinase 9, Gelatinase B, 92 kDa Type IV Collagenase
References
ReferencesReynolds, M. A., et al. 2003. Clin. Chem. 49, 1733.
Kolkenbrock, H., et al. 1996. Biol. Chem. 377, 529.
Marcy, A.I., et al. 1991. Biochemistry 30, 6476.
Stricklin, et al. 1983. Biochemistry 22, 61.
Product Information
Unit of DefinitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol 2,4-DNP-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH per min at 37°C, pH 7.0.
EC number3.4.24.35
FormLiquid
FormulationIn 200 mM NaCl, 50 mM Tris-HCl, 5 mM CaCl₂, 1 µM ZnCl₂, 0.05% BRIJ® 35 Detergent, 0.05% NaN₃, pH 7.0.
Quality LevelMQ100
Applications
Biological Information
Purity≥90% by SDS-PAGE
SourcePrepared from stimulated neutrophils that have been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.
Specific Activity≥1000 mU/mg protein
Concentration Label Please refer to vial label for lot-specific concentration
Physicochemical Information
Contaminantsno other MMP activity detectable
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Dry Ice Only
Toxicity Standard Handling
Storage ≤ -70°C
Avoid freeze/thaw Avoid freeze/thaw
Do not freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalogue Number GTIN
444231-5UG 04055977186383

Documentation

MMP-9, Monomer, Human Neutrophil MSDS

Title

Safety Data Sheet (SDS) 

MMP-9, Monomer, Human Neutrophil Certificates of Analysis

TitleLot Number
444231

References

Reference overview
Reynolds, M. A., et al. 2003. Clin. Chem. 49, 1733.
Kolkenbrock, H., et al. 1996. Biol. Chem. 377, 529.
Marcy, A.I., et al. 1991. Biochemistry 30, 6476.
Stricklin, et al. 1983. Biochemistry 22, 61.
Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision18-July-2007 RFH
SynonymsMatrix Metalloproteinase 9, Gelatinase B, 92 kDa Type IV Collagenase
DescriptionMonomeric, native MMP-9 from stimulated human neutrophils. Matrix metalloproteinases (MMP) are members of a family of at least 20 zinc-dependent endoproteinases that function extracellularly at neutral pH. The enzymes are synthesized as latent or inactive zymogens that contain a regulatory propeptide. This propeptide confers latency by binding to the Zn2+ molecule present in the active site. MMP activation can be achieved through autoactivation, via cleavage by other MMPs or proteases, such as furin, urokinase, plasmin, and trypsin, or by treatment with organomercurial comounds. This preparation is highly purified native MMP-9 from stimulated human neutrophils. Requires activation prior to use.
FormLiquid
FormulationIn 200 mM NaCl, 50 mM Tris-HCl, 5 mM CaCl₂, 1 µM ZnCl₂, 0.05% BRIJ® 35 Detergent, 0.05% NaN₃, pH 7.0.
Concentration Label Please refer to vial label for lot-specific concentration
Recommended reaction conditions

Organomercurial Activation Protocol This protocol is provided only as a general guide. Researchers should standardize this assay for their own specific needs and should consult published literature. The following protocol is from Stricklin, et al., which describes the use of p-aminophenylmercuric acetate (APMA) to activate pro-MMP. This protocol is also adaptable to other types of organomercurals, such as p-(hydroxymercuric) benzoate (PHMB), phenylmercuric chloride (PMC), or mersalyl. 1. Prepare a 10-50 mM stock solution of APMA (or other organomercurial compound) in 0.1 M NaOH just prior to use. Although not absolutely necessary, the stock solution may be adjusted to pH 11 with 5 N HCl (see Marcy, A.I., et al.). 2. To initiate the activation mix the proenzyme solution with the APMA solution at a 10:1 volume ratio (MMP:APMA). If a higher concentration of APMA is desired, increase the concentration of the stock solution. Do not exceed the 10:1 ratio, as this could result in significant changes in pH. 3. Incubate the mixture at 37°C for 2-3 h. It is recommended that an analytical run be conducted first to determine the optimal incubation time. For example, a small-scale experiment with a fixed concentration of pro-MMP and organomercurial would be incubated as described above. Remove aliquots of the sample at various time points during the incubation. Stop the reaction by the addition of SDS-PAGE sample buffer (e.g., 10 µl 2X sample buffer to 10 µl aliquot) and heat the samples to 95°C. The progress of activation can be monitored qualitatively by analyzing the aliquots on a 12% SDS-PAGE gel. 4. The activated MMP can be used without removing the APMA from the mixture. Please refer to Marcy, A.I., et al. for removal of organomercurials by gel filtration.
SourcePrepared from stimulated neutrophils that have been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.
EC number3.4.24.35
Purity≥90% by SDS-PAGE
Contaminantsno other MMP activity detectable
Specific activity≥1000 mU/mg protein
Unit definitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol 2,4-DNP-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH per min at 37°C, pH 7.0.
Storage Avoid freeze/thaw
≤ -70°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Toxicity Standard Handling
ReferencesReynolds, M. A., et al. 2003. Clin. Chem. 49, 1733.
Kolkenbrock, H., et al. 1996. Biol. Chem. 377, 529.
Marcy, A.I., et al. 1991. Biochemistry 30, 6476.
Stricklin, et al. 1983. Biochemistry 22, 61.

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Categories

Life Science Research > Proteins and Enzymes > Other Enzymes