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IM68 Anti-MMP-2 (Ab-8) Mouse mAb (VB3)

IM68
  
Purchase on Sigma-Aldrich

Přehled

Replacement Information

Tabulka spec. kláve

Species ReactivityHostAntibody Type
HMMonoclonal Antibody
Description
OverviewRecognizes the ~72 kDa latent and ~66 kDa active forms of MMP-2 in HUVEC cells and bladder, breast, and ovarian carcinoma tissue.
Catalogue NumberIM68
Brand Family Calbiochem®
SynonymsAnti-Gelatinase A, Anti-72 kDa Gelatinase, Anti-Matrix Metalloproteinase 2
Application Data
Detection of human MMP-2 by immunoblotting. Sample: Human MMP-2. Primary antibody: Anti-MMP-2 (Ab-8) Mouse mAb (VB3) (Cat. No. IM68) (1 µg/ml). Detection: chemiluminescence.
References
ReferencesCottam, D.W. and Rees, R.C. 1993. Intl. J. Oncol. 2, 861.
Stetler-Stevenson, W.G., et al. 1993. FASEB J. 7, 1434.
Woessner, J.F., 1991. FASEB J. 5, 2145.
Liotta, L.A. and Stetler-Stevenson, W.G. 1990. In Seminars in Cancer Biology, ed. M.M. Gottesman. Vol. 1, 99.
Product Information
DeclarationNot available for sale in Japan.
FormLiquid
FormulationIn 10 mM PBS, pH 7.4.
Positive controlConditioned medium from dexamethasone-treated HT-1080 or HUVEC cells or bladder, breast, or ovarian carcinoma tissue
PreservativeNone
Quality LevelMQ100
Applications
Key Applications Immunoblotting (Western Blotting)
Immunofluorescence
Application NotesImmunoblotting (1:200-1:400, chemiluminescence)
Immunofluorescence (4-5 µg/ml, indirect)
Application CommentsAntibody should be titrated for optimal results in individual systems.
Biological Information
Immunogennative human pro-MMP-2
ImmunogenHuman
CloneVB3
HostMouse
IsotypeIgG₁
Species Reactivity
  • Human
Antibody TypeMonoclonal Antibody
Concentration Label Please refer to vial label for lot-specific concentration
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 -20°C
Avoid freeze/thaw Avoid freeze/thaw
Do not freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-20°C).
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Katalogové číslo GTIN
IM68 0

Documentation

Anti-MMP-2 (Ab-8) Mouse mAb (VB3) Certificates of Analysis

TitleLot Number
IM68

References

Přehled odkazů
Cottam, D.W. and Rees, R.C. 1993. Intl. J. Oncol. 2, 861.
Stetler-Stevenson, W.G., et al. 1993. FASEB J. 7, 1434.
Woessner, J.F., 1991. FASEB J. 5, 2145.
Liotta, L.A. and Stetler-Stevenson, W.G. 1990. In Seminars in Cancer Biology, ed. M.M. Gottesman. Vol. 1, 99.
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.

Revision03-Febuary-2009 RFH
SynonymsAnti-Gelatinase A, Anti-72 kDa Gelatinase, Anti-Matrix Metalloproteinase 2
ApplicationImmunoblotting (1:200-1:400, chemiluminescence)
Immunofluorescence (4-5 µg/ml, indirect)
Application Data
Detection of human MMP-2 by immunoblotting. Sample: Human MMP-2. Primary antibody: Anti-MMP-2 (Ab-8) Mouse mAb (VB3) (Cat. No. IM68) (1 µg/ml). Detection: chemiluminescence.
DescriptionPurified mouse monoclonal antibody generated by immunizing BALB/c mice with the specified immunogen and fusing splenocytes with mouse myeloma p3-X63-Ag8.653 cells. Recognizes the ~72 kDa latent and the ~66 kDa active forms of MMP-2.
BackgroundMatrix metalloproteinases (MMPs) 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 MMPs 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 angiogenesis, arthritis, periodontitis, and metastasis. Matrix metalloproteinase-2 (MMP-2) also known by its alternative names of 72 kDa gelatinase/type IV collagenase and gelatinase A (EC 3.4.24.24) cleaves a number of substrates including gelatins, collagen types I, IV, V, VII, X, XI, and XIV, fibronectin, elastin and proteoglycan. MMP-2 is synthesized as a 631 amino acid proenzyme (~72 kDa zymogen) which is proteolytically processed at the first 80 amino acids to the 66 kDa active form. MMP-2 has been identified in a number of tissues, cells, and plasma/serum. It is secreted in a pro-enzyme form (pro-MMP-2) and is activated in vitro by organomercurials (e.g., 4aminophenylmercuric acetate, APMA). Pro-MMP-2 and pro-MMP-2/TIMP-2 complex are specifically activated in vitro by active MT1-MMPs on the surface of tumor cells. Numerous studies have shown a correlation between collagenase expression and metastatic potential and suggest that MMP-2 may be a useful marker for the diagnosis or prognosis of cancer.
HostMouse
Immunogen speciesHuman
Immunogennative human pro-MMP-2
CloneVB3
IsotypeIgG₁
Specieshuman
Positive controlConditioned medium from dexamethasone-treated HT-1080 or HUVEC cells or bladder, breast, or ovarian carcinoma tissue
FormLiquid
FormulationIn 10 mM PBS, pH 7.4.
Concentration Label Please refer to vial label for lot-specific concentration
PreservativeNone
CommentsAntibody should be titrated for optimal results in individual systems.
Storage Avoid freeze/thaw
-20°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-20°C).
Toxicity Standard Handling
ReferencesCottam, D.W. and Rees, R.C. 1993. Intl. J. Oncol. 2, 861.
Stetler-Stevenson, W.G., et al. 1993. FASEB J. 7, 1434.
Woessner, J.F., 1991. FASEB J. 5, 2145.
Liotta, L.A. and Stetler-Stevenson, W.G. 1990. In Seminars in Cancer Biology, ed. M.M. Gottesman. Vol. 1, 99.