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444248 MMP-13, Proenzyme, His•Tag®, Human, Recombinant, S. frugiperda

MMP-13, Proenzyme, His•Tag®, Human, Recombinant, S. frugiperda: MSDS (material safety data sheet) o SDS, certificato d’analisi (CoA) e certificato di qualità (CoQ), dossier, brochure e altri documenti disponibili.

Sinonimi: Collagenase-3

444248
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Panoramica

Replacement Information

Products

Numero di catalogoConfezionamento Qtà/conf
444248-10UG Fiala di plastica 10 μg
Description
OverviewFull-length recombinant, human MMP-13 fused to a His•Tag® sequence and expressed in S. frugiperda insect cells. This 452 amino acid proenzyme contains the N-terminal propeptide, the Ca2+- and Zn2+-binding catalytic domain, the hinge region, and the C-terminal hemopexin domain. Hydrolyzes collagen type II 5 to 6 times faster than collagens Type I and III. Exhibits high activity towards gelatin and degrades α1-antichymotrypsin and plasminogen activator inhibitor-2 (PAI-2).
Note: 1 mU = 1 milliunit.
Catalogue Number444248
Brand Family Calbiochem®
SynonymsCollagenase-3
References
ReferencesHerget, J., et al. 2003. Am. J. Physiol. 285, 4199.
Nagase, H. 1997. Biol. Chem. 378, 151.
Knäuper, V., et al. 1996. J. Biol. Chem. 271, 1544.
Knauper, V., et al. 1996. J. Biol. Chem. 271, 17124.
Pei, D., and Weiss, S.J. 1996. J. Biol. Chem. 271, 9135.
Knight, C.G., et al. 1992. FEBS Lett. 296, 263.
Product Information
Unit of DefinitionOne unit is defined as the amount of APMA-activated enzyme that will hydrolyze 1.0 µmol MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH₂ (<a href = "/Products/ProductDisplay.asp→catNO=03-32-5032">Cat. No. 03-32-5032</a>) per min at 37°C, pH 7.5.
FormLiquid
FormulationIn 150 mM NaCl, 50 mM Tris-HCl, 5 mM CaCl₂, pH 7.5.
Quality LevelMQ100
Applications
Biological Information
Purity≥90% by SDS-PAGE
Specific Activity≥50 mU/mg protein
Physicochemical Information
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
Numero di catalogo GTIN
444248-10UG 04055977186482

Documentation

MMP-13, Proenzyme, His•Tag®, Human, Recombinant, S. frugiperda MSDS

Titolo

Scheda di sicurezza (MSDS) 

MMP-13, Proenzyme, His•Tag®, Human, Recombinant, S. frugiperda Certificati d'Analisi

TitoloNumero di lotto
444248

Riferimenti bibliografici

Panoramica delle referenze
Herget, J., et al. 2003. Am. J. Physiol. 285, 4199.
Nagase, H. 1997. Biol. Chem. 378, 151.
Knäuper, V., et al. 1996. J. Biol. Chem. 271, 1544.
Knauper, V., et al. 1996. J. Biol. Chem. 271, 17124.
Pei, D., and Weiss, S.J. 1996. J. Biol. Chem. 271, 9135.
Knight, C.G., et al. 1992. FEBS Lett. 296, 263.
Scheda tecnica

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
SynonymsCollagenase-3
DescriptionFull-length recombinant, human MMP-13 fused to a His•Tag® sequence and expressed in S. frugiperda insect cells. This 452 amino acid proenzyme contains an N-terminal propeptide which confers latency to the proenzyme, a Ca2+- and Zn2+- binding catalytic domain, a hinge region, and a C-terminal hemopexin domain. Hydrolyzes collagen type II 5-6 times faster than collagens type I and III. Exhibits high activity towards gelatin and degrades α1-antichymotrypsin and plasminogen activator inhibitor-2.
FormLiquid
FormulationIn 150 mM NaCl, 50 mM Tris-HCl, 5 mM CaCl₂, pH 7.5.
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.
Purity≥90% by SDS-PAGE
Specific activity≥50 mU/mg protein
Unit definitionOne unit is defined as the amount of APMA-activated enzyme that will hydrolyze 1.0 µmol MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH₂ (Cat. No. 03-32-5032) per min at 37°C, pH 7.5.
Storage Avoid freeze/thaw
≤ -70°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Toxicity Standard Handling
ReferencesHerget, J., et al. 2003. Am. J. Physiol. 285, 4199.
Nagase, H. 1997. Biol. Chem. 378, 151.
Knäuper, V., et al. 1996. J. Biol. Chem. 271, 1544.
Knauper, V., et al. 1996. J. Biol. Chem. 271, 17124.
Pei, D., and Weiss, S.J. 1996. J. Biol. Chem. 271, 9135.
Knight, C.G., et al. 1992. FEBS Lett. 296, 263.