M5067
Anti-Matrix Metalloproteinase-25, Propeptide Region antibody produced in rabbit
~1 mg/mL, affinity isolated antibody, buffered aqueous glycerol solution
Synonym(s):
Anti-MMP-25, Anti-MT6-MMP
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About This Item
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous glycerol solution
species reactivity
mouse, human
concentration
~1 mg/mL
technique(s)
western blot: 1:1,000
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Gene Information
human ... MMP25(64386)
mouse ... Mmp25(240047)
General description
Matrix metalloproteinase-25 (MMP-25) belongs to the membrane-anchored matrix metalloproteinase subfamily. It is produced as a 57-60kDa monomer and is later expressed as a homodimer of 120kDa. This glycophosphatidylinositol (GPI)-anchored metalloproteinase is expressed in the polymorphonuclear neutrophils. MMP-25 possesses an extracellular prodomain along with other functional domains. The gene encoding it is localized on human chromosome 16p13.3.
Specificity
By immunoblotting against the reduced protein, the antibody identifies a band at 65 kDa as well as breakdown products. The antibody recognizes the zymogen and not activated forms of the enzyme.
Immunogen
synthetic peptide corresponding to the propeptide region of human matrix metalloproteinase-25 (membrane-type matrix metalloproteinase-6).
Biochem/physiol Actions
Matrix metalloproteinase-25 (MMP-25) acts as a marker for chronic respiratory diseases. Studies have indicated that MMP-25 can degrade fibrin, fibronectin, gelatin and type IV collagen. It may have a role in the degradation of the pericellular extracellular matrix.
Physical form
Solution in 0.01 M phosphate buffered saline containing 50% glycerol and 0.05% sodium azide.
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Storage Class
10 - Combustible liquids
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Ilian A Radichev et al.
The Journal of biological chemistry, 285(21), 16076-16086 (2010-03-24)
Ubiquitously expressed membrane type-1 matrix metalloproteinase (MT1-MMP), an archetype member of the MMP family, binds tissue inhibitor of metalloproteinases-2 (TIMP-2), activates matrix metalloproteinase-2 (MMP-2), and stimulates cell migration in various cell types. In contrast with MT1-MMP, the structurally similar MT6-MMP
Susan H Blanton et al.
American journal of medical genetics. Part A, 125A(1), 23-27 (2004-02-03)
Approximately 4,000 babies with nonsyndromic cleft lip with or without cleft palate (NSCLP) are born each year in the United States. Because NSCLP exhibits both etiologic and genetic heterogeneity, attempts to identify the underlying genetic causes have met with limited
Qing Sun et al.
The Journal of biological chemistry, 282(30), 21998-22010 (2007-05-22)
MMP25 (MT6-MMP) is one of the two glycosylphosphatidylinositol-anchored matrix metalloproteinases (MMPs) that have been suggested to play a role in pericellular proteolysis. However, its role in cancer is unknown, and its biochemical properties are not well established. Here we found
M N Blumenthal et al.
Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology, 40(6), 859-866 (2010-03-27)
Leukolysin is a novel matrix metalloproteinase (MMP-25/MT-6) released mainly by granulocytic cells, primarily neutrophils, which are implicated in chronic airways inflammation. To determine if leukolysin might be a serum marker for atopic asthma or chronic obstructive pulmonary disease (COPD). Three
Carl F Fortin et al.
International immunology, 22(8), 637-649 (2010-05-27)
Polymorphonuclear neutrophils (PMNs) are the first line of defense against invading organisms in humans; in addition, PMNs contribute to the linking of innate and adaptive immunity. To fulfill their biological behavior, PMNs utilize an arsenal of proteolytic enzymes, including members
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