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Key Documents

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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Referencia del producto
Descripción
Precios

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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Anna M Woskowicz et al.
The Journal of biological chemistry, 288(49), 35126-35137 (2013-10-30)
Localization of membrane type I matrix metalloproteinase (MT1-MMP) to the leading edge is thought to be a crucial step during cancer cell invasion. However, its mechanisms and functional impact on cellular invasion have not been clearly defined. In this report
Giovanna De Cunto et al.
Mediators of inflammation, 2017, 9524594-9524594 (2017-11-04)
Little is known about the cause and pathophysiology of middermal elastolysis (MDE). In this condition, variable inflammatory infiltrate may be present or not together with loss of elastic fibres in the middermis that spares both papillary and lower reticular dermis.
Membrane-type-3 matrix metalloproteinase (MT3-MMP) functions as a matrix composition-dependent effector of melanoma cell invasion.
Tatti, O; Arjama, M; Ranki, A; Weiss, SJ; Keski-Oja, J; Lehti, K
Testing null
Juhyeon Son et al.
Journal of biochemical and molecular toxicology, 35(10), e22868-e22868 (2021-08-03)
Osteosarcoma (OS) is a primary bone neoplasm that is highly malignant. As advances in chemotherapy for the treatment of OS have stagnated, discovery of new reagents is required. Emetine is a phytochemical which can be isolated from a medicinal herb Cephaelis
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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