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IM09L Anti-MMP-9 (Ab-1) Mouse mAb (6-6B)

This Anti-MMP-9 (Ab-1) Mouse mAb (6-6B) is validated for use in Immunoblotting, Immunoprecipitation, Neutralization Studies, Paraffin Sections for the detection of MMP-9 (Ab-1).

Anti-MMP-9 (Ab-1) Mouse mAb (6-6B) MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: Anti-92 kDa Gelatinase, Anti-Matrix Metalloproteinase 9, Anti-Type IV Collagenase, Anti-Gelatinase B

IM09L
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Overview

Replacement Information

Key Spec Table

Species ReactivityHostAntibody Type
HMMonoclonal Antibody

Products

Catalogue NumberPackaging Qty/Pack
IM09L-100UG Plastová ampulka 100 μg
IM09L-1MG Plastová ampulka 1 mg
Description
OverviewRecognizes the ~92 kDa latent and the ~83 kDa active forms of MMP-9 under non-reducing conditions, but only the latent form under reducing conditions. Inhibits the enzymatic activity of MMP-9. For paraffin sections, use Cat. No. IM37L.
Catalogue NumberIM09L
Brand Family Calbiochem®
SynonymsAnti-92 kDa Gelatinase, Anti-Matrix Metalloproteinase 9, Anti-Type IV Collagenase, Anti-Gelatinase B
References
ReferencesCottam, D.W. and Rees, R.C. 1993. Intl. J. of Oncol. 2, 861.
Nakajima, M., et al. 1993. Cancer Res. 53, 5802.
Ramos-DeSimone, et al. 1993. Hybridoma. 12, 349.
Stetler-Stevenson, W.G., et al. 1993. FASEB. 7, 1434.
Zucker, S., et al. 1993. Cancer Res. 53, 140.
Woessner, J.F. 1991. FASEB. 5, 2145.
Liotta, L.A. and Stetler-Stevenson, W.G. 1990. in Seminars in Cancer Biology, ed. M.M. Gottesman. Vol. 1; 99-106.
Product Information
DeclarationNot available for sale in Japan.
FormLyophilized
FormulationLyophilized from a volatile buffer, 100 µg BSA.
Positive controlMMP-9 protein (Cat. Nos. PF024 or PF038)
PreservativeNone
Quality LevelMQ100
Applications
Application ReferencesImmunoprecipitation Ramos-DeSimone, N. and French, D. L. 1994. Ann. NY Acad. Sci. 732, 469. Immunoblotting, Neutralization Studies Ramos-DeSimone, N., et al. 1993. Hybridoma. 12, 349.
Key Applications Immunoblotting (Western Blotting)
Immunoprecipitation
Not Paraffin Sections
Neutralization Studies
Application NotesImmunoblotting (2 µg/ml)
Immunoprecipitation (see appplication references)
Neutralization Studies (see comments and application references)
Paraffin Sections (not recommended)
Application CommentsInhibits MMP-9 enzymatic activity. For staining paraffin sections, use Anti-MMP-9 (626-644) (Ab-3) Mouse mAb (56-2A4) (Cat. No. IM37L). Antibody should be titrated for optimal results in individual systems.
Biological Information
ImmunogenMMP-9 from conditioned medium of PMA-stimulated HT-1080 human fibrosarcoma cells
ImmunogenHuman
Clone6-6B
HostMouse
IsotypeIgG₁
Species Reactivity
  • Human
Antibody TypeMonoclonal Antibody
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Ambient Temperature Only
Toxicity Standard Handling
Storage +2°C to +8°C
Do not freeze Ok to freeze
Special InstructionsStore at 4°C until reconstituted, then store in aliquots at -20°C or at 4°C with 0.1% azide. Resuspend the antibody with sterile PBS, pH 7.4, or sterile 20 mM Tris-saline, pH 7.4, to yield a final concentration of 100 µg/ml; product will be more stable if 0.1% sodium azide is included (do not add azide if antibody is to be used with viable cells). Lyophilized antibodies should be resuspended at 4°C with occasional gentle mixing for at least 2 h. Freezing of aliquots is best for long-term storage of reconstituted product; repetitive freezing and thawing should be avoided.
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalogue Number GTIN
IM09L-100UG 04055977228151
IM09L-1MG 04055977228144

Documentation

Anti-MMP-9 (Ab-1) Mouse mAb (6-6B) Certificates of Analysis

TitleLot Number
IM09L

References

Reference overview
Cottam, D.W. and Rees, R.C. 1993. Intl. J. of Oncol. 2, 861.
Nakajima, M., et al. 1993. Cancer Res. 53, 5802.
Ramos-DeSimone, et al. 1993. Hybridoma. 12, 349.
Stetler-Stevenson, W.G., et al. 1993. FASEB. 7, 1434.
Zucker, S., et al. 1993. Cancer Res. 53, 140.
Woessner, J.F. 1991. FASEB. 5, 2145.
Liotta, L.A. and Stetler-Stevenson, W.G. 1990. in Seminars in Cancer Biology, ed. M.M. Gottesman. Vol. 1; 99-106.
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.

Revision27-August-2007 RFH
SynonymsAnti-92 kDa Gelatinase, Anti-Matrix Metalloproteinase 9, Anti-Type IV Collagenase, Anti-Gelatinase B
ApplicationImmunoblotting (2 µg/ml)
Immunoprecipitation (see appplication references)
Neutralization Studies (see comments and application references)
Paraffin Sections (not recommended)
DescriptionPurified mouse monoclonal antibody. Recognizes the ~92 kDa latent and the ~83 kDa active forms of human MMP-9 under non-reducing conditions, but only the latent form under reducing conditions.
BackgroundMatrix metalloproteinases (MMP's) are a family of enzymes that are responsible for the degradation of extracellular matrix components such as collagen, laminin and proteoglycans. In addition to sequence homology, all MMP's share the following characteristics: the catalytic mechanism is dependent upon a zinc ion at the active center, they cleave one or more extracellular matrix components, they are secreted as zymogens which are activated by removal of an ~10 kDa segment from the N terminus and they are inhibited by tissue inhibitor of metalloproteinases (TIMP). These enzymes are involved in normal physiological processes such as embryogenesis and tissue remodeling and may play an important role in arthritis, periodontitis, and metastasis. MMP-9 (Gelatinase B, 92 kDa gelatinase/type IV collagenase) is secreted as a 92 kDa zymogen which is proteolytically processed to the 83 kDa active form; a 68 kDa has also been detected. MMP-9, along with its most closely related member of the MMP family, MMP-2, show substrate specificity toward type IV and V collagens, gelatin and elastin. Numerous studies have shown a correlation between collagenase expression and metastatic potential. Elevated levels of MMP-9 in plasma suggest that it may be a useful marker for the diagnosis or prognosis of cancer in general.
HostMouse
Immunogen speciesHuman
ImmunogenMMP-9 from conditioned medium of PMA-stimulated HT-1080 human fibrosarcoma cells
Clone6-6B
IsotypeIgG₁
Specieshuman
Positive controlMMP-9 protein (Cat. Nos. PF024 or PF038)
FormLyophilized
FormulationLyophilized from a volatile buffer, 100 µg BSA.
PreservativeNone
CommentsInhibits MMP-9 enzymatic activity. For staining paraffin sections, use Anti-MMP-9 (626-644) (Ab-3) Mouse mAb (56-2A4) (Cat. No. IM37L). Antibody should be titrated for optimal results in individual systems.
Storage +2°C to +8°C
Do Not Freeze Ok to freeze
Special InstructionsStore at 4°C until reconstituted, then store in aliquots at -20°C or at 4°C with 0.1% azide. Resuspend the antibody with sterile PBS, pH 7.4, or sterile 20 mM Tris-saline, pH 7.4, to yield a final concentration of 100 µg/ml; product will be more stable if 0.1% sodium azide is included (do not add azide if antibody is to be used with viable cells). Lyophilized antibodies should be resuspended at 4°C with occasional gentle mixing for at least 2 h. Freezing of aliquots is best for long-term storage of reconstituted product; repetitive freezing and thawing should be avoided.
Toxicity Standard Handling
ReferencesCottam, D.W. and Rees, R.C. 1993. Intl. J. of Oncol. 2, 861.
Nakajima, M., et al. 1993. Cancer Res. 53, 5802.
Ramos-DeSimone, et al. 1993. Hybridoma. 12, 349.
Stetler-Stevenson, W.G., et al. 1993. FASEB. 7, 1434.
Zucker, S., et al. 1993. Cancer Res. 53, 140.
Woessner, J.F. 1991. FASEB. 5, 2145.
Liotta, L.A. and Stetler-Stevenson, W.G. 1990. in Seminars in Cancer Biology, ed. M.M. Gottesman. Vol. 1; 99-106.
Application referencesImmunoprecipitation Ramos-DeSimone, N. and French, D. L. 1994. Ann. NY Acad. Sci. 732, 469. Immunoblotting, Neutralization Studies Ramos-DeSimone, N., et al. 1993. Hybridoma. 12, 349.