生物来源
rabbit
质量水平
偶联物
unconjugated
抗体形式
affinity isolated antibody
抗体产品类型
primary antibodies
克隆
polyclonal
表单
buffered aqueous glycerol solution
种属反应性
human
浓度
~1 mg/mL
技术
western blot: 1:1,000
UniProt登记号
运输
wet ice
储存温度
−20°C
靶向翻译后修饰
unmodified
基因信息
human ... MMP26(56547)
一般描述
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.
特异性
By immunoblotting against the reduced protein, the antibody identifies a band at 30 kDa (zymogen).
免疫原
synthetic peptide corresponding to the propeptide domain of human matrix metalloproteinase-26.
生化/生理作用
Matrix metalloproteinase-26 (MMP-26) degrades fibronectin, type IV collagen and activated pro-metalloproteinase-9. MMP-26 also aids in development of tumors.
外形
Solution in 0.01 M phosphate buffered saline containing 50% glycerol and 0.05% sodium azide.
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储存分类代码
10 - Combustible liquids
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
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
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
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