Product Pathways - Protein Stability
MMP-2 Antibody #4022
PhosphoSitePlus® protein, site, and accession data: MMP2
| Applications | Reactivity | Sensitivity | MW (kDa) | Source |
|---|---|---|---|---|
| W | H (M) (R) | Endogenous | 64, 72 | Rabbit |
Applications Key:
W=Western Blotting
Reactivity Key:
H=Human
M=Mouse
R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Protocols
- 4022:
- Western Blotting
Specificity / Sensitivity
MMP-2 Antibody detects full length (proenzyme, 72 kDa) and cleaved (active enzyme, 64 kDa) MMP-2.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Lys116 of human MMP-2. Antibodies are purified by protein A and peptide affinity chromatography.
Background
The matrix metalloproteinases (MMPs) are a family of proteases that target many extracellular proteins including other proteases, growth factors, cell surface receptors and adhesion molecules (1). Among the family members, MMP-2, MMP-3, MMP-7 and MMP-9 have been characterized as important factors for normal tissue remodeling during embryonic development, wound healing, tumor invasion, angiogenesis, carcinogenesis and apoptosis (2-4). MMP activity correlates with cancer development (2). One mechanism of MMP regulation is transcriptional (5). Once synthesized, MMP exists as a latent proenzyme. Maximum MMP activity requires proteolytic cleavage to generate active MMPs by releasing the inhibitory propeptide domain from the full length protein (5).
- McCawley, L.J. and Matrisian, L.M. (2001) Curr. Opin. Cell Biol. 13, 534-540.
- Coussens, L.M. et al. (2002) Science 295, 2387-2391.
- Sternlicht, M.D. et al. (1999) Cell 98, 137-146.
- Vu, T.H. et al. (1998) Cell 93, 411-422.
- Nagase, H. et al. (1990) Biochemistry 29, 5783-5789.
Application References
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For Research Use Only. Not For Use In Diagnostic Procedures.