M5192
Anti-Matrix Metalloproteinase-26, Propeptide Region antibody produced in rabbit
~1 mg/mL, affinity isolated antibody, buffered aqueous glycerol solution
Synonym(e):
Anti-MMP-26
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About This Item
Biologische Quelle
rabbit
Qualitätsniveau
Konjugat
unconjugated
Antikörperform
affinity isolated antibody
Antikörper-Produkttyp
primary antibodies
Klon
polyclonal
Form
buffered aqueous glycerol solution
Speziesreaktivität
human
Konzentration
~1 mg/mL
Methode(n)
western blot: 1:1,000
UniProt-Hinterlegungsnummer
Versandbedingung
wet ice
Lagertemp.
−20°C
Posttranslationale Modifikation Target
unmodified
Angaben zum Gen
human ... MMP26(56547)
Allgemeine Beschreibung
Matrix metalloproteinase-26 (MMP-26) is also known as matrilysin-2 and endometase. It is expressed in normal tissues and also in human carcinoma cells. MMP-26 possesses a propeptide domain, a signal peptide and a catalytic domain but does not have the hemopexin-like domain which is common to other members of its family. The MMP-26 gene is localized to human chromosome 11p15.3.
Spezifität
By immunoblotting against the reduced protein, the antibody identifies a band at 30 kDa (zymogen).
Immunogen
synthetic peptide corresponding to the propeptide domain of human matrix metalloproteinase-26.
Biochem./physiol. Wirkung
Matrix metalloproteinase-26 (MMP-26) degrades fibronectin, type IV collagen and activated pro-metalloproteinase-9. MMP-26 also aids in development of tumors.
Physikalische Form
Solution in 0.01 M phosphate buffered saline containing 50% glycerol and 0.05% sodium azide.
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Lagerklassenschlüssel
10 - Combustible liquids
Analysenzertifikate (COA)
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Zahraa I Khamis et al.
Journal of Cancer, 4(4), 296-303 (2013-04-10)
Human endometase/matrilysin-2/matrix metalloproteinase-26 (MMP-26) is an endopeptidase mostly produced by human carcinoma cells. While MMPs are thought to regulate the dynamics of extracellular matrix turnover, new evidence shows that these enzymes may play a critical regulatory role in inflammation. To
G N Marchenko et al.
The Biochemical journal, 356(Pt 3), 705-718 (2001-06-08)
Identification of expanding roles for matrix metalloproteinases (MMPs) in complex regulatory processes of tissue remodelling has stimulated the search for genes encoding proteinases with unique functions, regulation and expression patterns. By using a novel cloning strategy, we identified three previously
Helen E Gruber et al.
Experimental and molecular pathology, 92(1), 59-63 (2011-09-29)
Matrix metalloproteinase (MMP) regulation and expression is important in the aging/degenerating human intervertebral disc. MMP-26 (also known as matrilysin-2 or endometase) is a newly discovered MMP which degrades type IV collagen, fibronectin, fibrinogen, vitronectin, denatured collagen types I-IV, insulin-like growth
Yang Zhang et al.
Molecular medicine reports, 4(6), 1201-1209 (2011-08-02)
Matrix metalloproteinase 26 (MMP-26) is a novel member of the matrix metalloproteinase (MMP) family and is widely expressed in cancer cells of epithelial origin. MMP-26 has been shown to contribute to tumor development and to the restoration of tissue injury.
Hirotaka Nishi et al.
Oncology reports, 30(2), 751-756 (2013-06-12)
The human matrix metalloproteinase (MMP)-26, also called matrilysin-2 or endometase, has been isolated as a matrilysin (MMP-7) homolog. Several reports describe that MMP-26 may be related to the development of endometrial carcinomas. Total RNAs were isolated from 51 normal endometrial
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