GW21125
Anti-MMP14 antibody produced in chicken
affinity isolated antibody, buffered aqueous solution
Synonym(s):
Anti-MT1-MMP, Anti-Matrix metalloproteinase 14
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About This Item
biological source
chicken
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
species reactivity
rat, human
manufacturer/tradename
Genway 15-288-21125
technique(s)
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... MMP14(4323)
Immunogen
Immunogen Sequence: GI # 4826834, sequence 126-230
Recombinant matrix metalloproteinase 14 preproprotein
Application
Anti-MMP14 antibody produced in chicken is suitable for western blotting analysis at a dilution of 1:500, for tissue or cell staining at a dilution of 1:200.
Biochem/physiol Actions
Matrix metalloproteinase-14 is an enzyme encoded by the MMP14 gene in humans. It is an important member of the matrix metalloproteinase (MMP) family. It is a degrading enzyme having complex and specific regulation networks. MMP-14 facilitates local extracellular matrix (ECM) degradation and acts as a major mediator of cell migration, angiogenesis and invasion. It is involved in the breakdown of extracellular matrix in normal physiological processes, such as mediating cell invasion through the extracellular matrix (ECM).[1] Knockdown of this gene results in increase of N-cadherin adhesions, which are prerequisite for fibronectin matrix formation. MMP-14 signals autophagy, a process which may contribute to the chemoresistance phenotype in brain cancer cells. Mutation in MMP14 causes an autosomal-recessive, multicentric disorder, winchester syndrome, with multicentric osteolysis and arthritis.
Physical form
Solution in phosphate buffered saline containing 0.02% 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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Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Jonathan Pratt et al.
Cellular signalling, 26(5), 917-924 (2014-01-28)
Plant lectins have been considered as possible anti-tumor drugs because of their property to induce autophagic cell death. Given that expression of membrane type-1 matrix metalloproteinase (MT1-MMP) has been found to regulate expression of the autophagy biomarker Bcl-2/adenovirus E1B 19kDa
Brad R Evans et al.
American journal of human genetics, 91(3), 572-576 (2012-08-28)
The "vanishing bone" syndromes represent a group of rare skeletal disorders characterized by osteolysis and joint destruction, which can mimic severe rheumatoid arthritis. Winchester syndrome was one of the first recognized autosomal-recessive, multicentric forms of the disorder. It was originally
Takahisa Takino et al.
Biochemical and biophysical research communications, 450(2), 1016-1020 (2014-07-01)
Fibronectin matrix formation requires the increased cytoskeletal tension generated by cadherin adhesions, and is suppressed by membrane-type 1 matrix metalloproteinase (MT1-MMP). In a co-culture of Rat1 fibroblasts and MT1-MMP-silenced HT1080 cells, fibronectin fibrils extended from Rat1 to cell-matrix adhesions in
Amanda Haage et al.
Biochemical and biophysical research communications, 450(1), 213-218 (2014-06-01)
Matrix metalloproteinases (MMPs) are extracellular matrix (ECM) degrading enzymes and have complex and specific regulation networks. This includes activation interactions, where one MMP family member activates another. ECM degradation and MMP activation can be initiated by several different stimuli including
Dane K Lund et al.
American journal of physiology. Cell physiology, 307(2), C140-C149 (2014-06-06)
The twenty-five known matrix metalloproteases (MMPs) and their endogenous inhibitors, tissue inhibitors of metalloproteases (TIMPs), mediate cell invasion through the extracellular matrix (ECM). In a comparative three-dimensional assay, we analyzed human and mouse satellite cells' competence to invade an artificial
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