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AB6004

Sigma-Aldrich

Anti-MT1-MMP Antibody, hinge region

from rabbit, purified by affinity chromatography

Sinónimos:

MT-MMP 1, Membrane-type matrix metalloproteinase 1, Membrane-type-1 matrix metalloproteinase, matrix metallopeptidase 14 (membrane-inserted), matrix metalloproteinase 14, matrix metalloproteinase 14 (membrane-inserted), membrane type 1 metalloprotease

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

purified by

affinity chromatography

species reactivity

human, rat

technique(s)

immunohistochemistry: suitable (paraffin)
western blot: suitable

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... MMP14(4323)

General description

Matrix metalloproteinases (MMPs) are a family of secreted and membrane-bound zinc endopeptidases. Collectively, these enzymes degrade the components of extracellular matrix, including fibrillar and non-fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. MMPs play an important role in wound healing, apoptosis, bone elongation, embryo development, angiogenesis, cancer metastases, and tissue remodeling within many disease states.
Most MMP′s are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, MT1-MMP (MMP-14) is a member of the membrane-type subfamily. Each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. MT1-MMP is capable of mediating pericellular proteolysis of extracellular matrix components and is therefore thought to be an important molecular tool for cellular remodeling of the surrounding matrix. This protein also activates MMP2 protein, and this activity may be involved in tumor invasion.

Specificity

Predicted to cross react with mouse, (95% sequence homology) and monkey chimpanzee, canine and bovine (100% sequence homology). Reactivity with other species has not been tested.
The antibody recognizes human and rat MT1-MMP. It does not cross react with MMP-1, MMP-2, MMP-8, MMP-9, and MMP-13.

Immunogen

KLH conjugated synthetic peptide selected from the hinge region of human MT1-MMP.

Application

Detect MT1-MMP using this Anti-MT1-MMP Antibody, hinge region validated for use in WB, IH(P).

Quality

Evaluated on a representative lot by Western blot on rat lung lysate using Anti-MT1-MMP.

Target description

~ 65 kDa

Linkage

Replaces: AB815

Analysis Note

Control
Rat lung lysate.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

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Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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J A Willson et al.
Journal of cell communication and signaling, 12(2), 479-488 (2017-08-30)
The membrane bound matrix metalloproteinase MT1-MMP plays roles in modulating cell movement, independent of its abilities to remodel the extracellular matrix. Unlike many MMPs, MT1-MMP is activated in the Golgi prior to secretion by a pro-protein convertase, primarily furin. Regulation
N Akanuma et al.
British journal of cancer, 110(1), 189-198 (2013-11-08)
FSCN1 and matrix metalloproteinase 14 (MMP14) are both invadopodia-related proteins. We herein elucidate the tumourigenicity of these proteins and identify novel therapeutic agents in esophageal squamous cell carcinoma (ESCC). FSCN1 and MMP14 were evaluated by immunohistochemistry and quantitative PCR, and
Immunolocalization of membrane-type 1 MMP in human rheumatoid synovium tissues.
Qin, S; Wang, F; Zhou, M; Ding, W; Chen, L; Lu, Y
International Journal of Clinical and Experimental Pathology null
Yuko Matsuura-Hachiya et al.
Biochemistry and biophysics reports, 4, 180-186 (2015-09-21)
The renin-angiotensin system is known to be involved in skin remodeling and inflammation. Previously, we reported that ultraviolet B (UVB) irradiation enhanced angiotensin-converting enzyme (ACE) expression and angiotensin II levels in hairless mouse skin, and an ACE inhibitor, enalapril maleate
Mario A Cepeda et al.
Molecular cancer, 15(1), 65-65 (2016-10-21)
Membrane Type-1 Matrix Metalloproteinase (MT1-MMP) is a multifunctional protease implicated in metastatic progression ostensibly due to its ability to degrade extracellular matrix (ECM) components and allow migration of cells through the basement membrane. Despite in vitro studies demonstrating this principle

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