M5317
Anti-Matrix Metalloproteinase-26, N-Terminal Active 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
Conjugate:
unconjugated
Clone:
polyclonal
Application:
WB
Citations:
6
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 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 chromosome 11p15.3.
Immunogen
synthetic peptide corresponding to the N-terminal of active human matrix metalloproteinase-26.
Biochem/physiol Actions
By immunoblotting against the reduced protein, the antibody identifies bands at 30 kDa and 18 kDa (zymogen and active MMP-26, respectively).
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
Regulatory Information
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Related Content
Datasheet
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
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
Global Trade Item Number
| SKU | GTIN |
|---|---|
| M5317-100UG | 04061835808694 |