M4065
Anti-Matrix Metalloproteinase-2 antibody produced in rabbit
~1 mg/mL, IgG fraction of antiserum, buffered aqueous solution
Synonym(s):
Anti-MMP-2
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About This Item
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biological source
rabbit
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 72 kDa (proform)
species reactivity
mouse, bovine, rat, human
concentration
~1 mg/mL
technique(s)
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 10-20 μg/mL
western blot: 5-10 μg/mL
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... MMP2(4313)
Specificity
Recognizes MMP-2, cytoplasmic localization. Shows no cross-reactivity with the pro and active forms of other MMPs.
Immunogen
synthetic peptide from the second half of human MMP-2 (Gelatinase-A, 72 kDa Gelatinase). The immunogen is synthesized as a 631 amino acid proenzyme that is activated by cleavage of the the first 80 amino acids.
Application
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
Western Blotting (1 paper)
Physical form
Solution in 10 mM phosphate buffered saline, pH 7.4, containing 0.2% bovine serum albumin and 0.09% sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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PloS one, 11(3), e0152376-e0152376 (2016-03-26)
AGEs accumulation in the skin affects extracellular matrix (ECM) turnover and triggers diabetes associated skin conditions and accelerated skin aging. The receptor of AGEs (RAGE) has an essential contribution to cellular dysfunction driven by chronic inflammatory responses while TGF-β1 is
Vascular cell, 3(1), 6-6 (2011-02-26)
The mechanism of cell-cell contact dependent regulation of pericellular proteolysis in angiogenesis was examined by studying the expression of MMPs using isolated HUVECs in culture. Zymography, Immunoblot and RT-PCR analysis showed that the production and secretion of matrixmetalloproteinase-2 and matrixmetalloproteinase-9
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