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M5192

Sigma-Aldrich

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

MDL-Nummer:
MFCD04974757
UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

rabbit

Qualitätsniveau

200

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

Q9NRE1

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

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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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