Mouse/Rat MMP-2 Alexa Fluor™ Plus 405-conjugated Antibody
R&D Systems, part of Bio-Techne | Catalog # AF1488AFP405
Conjugate
Catalog #
Key Product Details
Species Reactivity
Mouse, Rat
Applications
Immunohistochemistry, Western Blot, Immunoprecipitation
Label
Alexa Fluor Plus 405 (Excitation = 404 nm, Emission = 455 nm)
Antibody Source
Polyclonal Goat IgG
Product Specifications
Immunogen
Mouse myeloma cell line NS0-derived recombinant mouse MMP-2
Specificity
Detects mouse and rat MMP-2 in direct ELISAs and Western blots. In direct ELISAs, less than 40% cross-reactivity with recombinant human MMP-2 is observed and less than 1% cross-reactivity with recombinant mouse (rm) MMP-3 and rmMMP-9 is observed.
Clonality
Polyclonal
Host
Goat
Isotype
IgG
Applications
Application
Recommended Usage
Immunohistochemistry
Optimal dilution of this antibody should be experimentally determined.
Immunoprecipitation
Optimal dilution of this antibody should be experimentally determined.
Western Blot
Optimal dilution of this antibody should be experimentally determined.
Formulation, Preparation, and Storage
Formulation
Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide.
Shipping
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied
Background: MMP-2
Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-2 (gelatinase A), a type IV collagenase, can degrade a broad range of substrates including type IV, V, VII and X collagens as well as elastin and fibronectin. It is believed to act synergistically with interstitial collagenase (MMP-1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-2 has been shown to be associated with many connective tissue cells as well as neutrophils, macrophages and monocytes. Structurally, MMP-2 may be divided into several distinct domains: a pro-domain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a fibronectin-like domain thought to play a role in substrate targeting; and a carboxyl terminal (hemopexin-like) domain containing 2 N-linked glycosylation sites. The amino acid sequences of the proenzymes are identical between mouse and rat.
Long Name
Matrix Metalloproteinase 2
Alternate Names
Gelatinase A, MMP2
Gene Symbol
MMP2
UniProt
Additional MMP-2 Products
Product Specific Notices
This product is provided under an intellectual property license from Life Technologies Corporation. The transfer of this product is conditioned on the buyer using the purchased product solely in research conducted by the buyer, excluding contract research or any fee for service research, and the buyer must not (1) use this product or its components for (a) diagnostic, therapeutic or prophylactic purposes; (b) testing, analysis or screening services, or information in return for compensation on a per-test basis; or (c) manufacturing or quality assurance or quality control, and/or (2) sell or transfer this product or its components for resale, whether or not resold for use in research. For information on purchasing a license to this product for purposes other than as described above, contact Life Technologies Corporation, 5781 Van Allen Way, Carlsbad, CA 92008 USA or outlicensing@thermofisher.com.
For research use only
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