M5192
Anti-Matrix Metalloproteinase-26, Propeptide Region antibody produced in rabbit
~1 mg/mL, affinity isolated antibody, buffered aqueous glycerol solution
别名:
Anti-MMP-26
biological source
rabbit
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
target post-translational modification
unmodified
Quality Level
Gene Information
human ... MMP26(56547)
General description
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.
Immunogen
synthetic peptide corresponding to the propeptide domain of human matrix metalloproteinase-26.
Biochem/physiol Actions
By immunoblotting against the reduced protein, the antibody identifies a band at 30 kDa (zymogen).
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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存储类别
10 - Combustible liquids
法规信息
新产品
此项目有
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
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
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
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.
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