M5442
Anti-Matrix Metalloproteinase-26, Hinge Region antibody produced in rabbit
~1 mg/mL, affinity isolated antibody, buffered aqueous glycerol solution
Synonym(s):
Anti-MMP-26
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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
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 ... MMP26(56547)
General description
Matrix metalloproteinase-26 (MMP-26) is also known as endometase and matrilysin-2. 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.
Specificity
By immunoblotting against the reduced protein, the antibody identifies bands at 30 kDa and 18 kDa (zymogen and active MMP-26, respectively).
Immunogen
synthetic peptide corresponding to the hinge region of human matrix metalloproteinase-26.
Biochem/physiol Actions
Matrix metalloproteinase-26 (MMP-26) degrades fibronectin, type IV collagen and activated pro-metalloproteinase-9. MMP-26 also aids in development of tumors.
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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Qinglin Hu et al.
Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine, 35(4), 3569-3574 (2013-12-10)
Tumor recurrence and metastasis are pressing issues of patients with colorectal cancer who receive surgery. Matrilysin-2 (MMP-26) has been proved to play an important role during invasion and metastasis of some human solid tumor. We aimed to investigate the clinical
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
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
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.
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
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