详细说明
Species Reactivity
Human
Specificity
Detects the pro and active forms of human MMP-2 in Western blots. In dot blots, no cross-reactivity with recombinant human MMP-1, -3, -7,
-8, -9, -10, -12, or -13 is observed.Source
Monoclonal Mouse IgG 2A Clone # 1A10
Purification
Protein A or G purified from hybridoma culture supernatant
Immunogen
Chinese hamster ovary cell line CHO-derived recombinant human MMP-2
Accession # P08253Formulation
Supplied in a saline solution containing BSA and Sodium Azide.
Label
Phycoerythrin
Applications
Recommended
ConcentrationSample
Intracellular Staining by Flow Cytometry
10 µL/10 6 cells
See below
Please Note: Optimal dilutions should be determined by each laboratory for each application. are available in the Technical Information section on our website.
Data Examples
Intracellular Staining by Flow Cytometry | Detection of MMP‑2 in MG‑63 Human Cell Line by Flow Cytometry. MG‑63 human osteosarcoma cell line was stained with Mouse Anti-Human MMP‑2 PE‑conjugated Monoclonal Antibody (Catalog # IC9023P, filled histogram) or isotype control antibody (Catalog # , open histogram). To facilitate intracellular staining, cells were fixed with Flow Cytometry Fixation Buffer (Catalog # ) and permeabilized with Flow Cytometry Permeabilization/Wash Buffer I (Catalog # ). View our protocol for . |
Preparation and Storage
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 that have a 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 collagen, 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.
Long Name:
Matrix Metalloproteinase 2
Entrez Gene IDs:
4313 (Human); 17390 (Mouse)
Alternate Names:
72 kDa gelatinase; CLG4; CLG4A72 kDa type IV collagenase; collagenase type IV-A; EC 3.4.24; EC 3.4.24.24; Gelatinase A; matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IVcollagenase); matrix metalloproteinase 2 (gelatinase A, 72kD gelatinase, 72kD type IVcollagenase); Matrix metalloproteinase-2; matrix metalloproteinase-II; MMP2; MMP-2; MMP-II; MONA; neutrophil gelatinase; TBE-1matrix metalloproteinase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IVcollagenase)