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Die folgenden MAPmates™ sollten nicht zusammen analysiert werden: -MAPmates™, die einen unterschiedlichen Assaypuffer erfordern. -Phosphospezifische und MAPmate™ Gesamtkombinationen wie Gesamt-GSK3β und Gesamt-GSK3β (Ser 9). -PanTyr und locusspezifische MAPmates™, z.B. Phospho-EGF-Rezeptor und Phospho-STAT1 (Tyr701). -Mehr als 1 Phospho-MAPmate™ für ein einziges Target (Akt, STAT3). -GAPDH und β-Tubulin können nicht mit Kits oder MAPmates™, die panTyr enthalten, analysiert werden.
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48-602MAG
Buffer Detection Kit for Magnetic Beads
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AB6070
Anti-MT1-MMP Antibody, hemopexin domain
This Anti-MT1-MMP Antibody, hemopexin domain is validated for use in WB, IH(P) for the detection of MT1-MMP.
More>>This Anti-MT1-MMP Antibody, hemopexin domain is validated for use in WB, IH(P) for the detection of MT1-MMP. Less<<
Anti-MT1-MMP Antibody, hemopexin domain: SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
Matrix metalloproteinases (MMPs) are a family of secreted and membrane-bound zinc endopeptidases. Collectively, these enzymes degrade components of extracellular matrix (ECM), including collagens, fibronectin, laminin and other glycoproteins. MMPs play an important role in wound healing, apoptosis, development, angiogenesis, cancer metastases, and tissue remodeling. Most MMPs are secreted as inactive proproteins which are cleaved and activated; however, MT1-MMP (MMP-14) is a member of the membrane-type subfamily. Each member of this subfamily has a transmembrane domain suggesting these proteins are expressed at the cell’s surface rather than secreted. MT1-MMP is capable of mediating pericellular proteolysis of ECM components and thought to be an important tool for cellular remodeling of the ECM. It is also involved in endothelial cell migration, and although not fully characterized, MT1-MMP activity appears to modulate endothelial invasion, and formation of capillary tubes during angiogenesis. It also appears to be a factor in monocyte recruitment during inflammation. MT1-MMP also activates MMP-2 protein, an activity involved in tumor invasion.
References
Product Information
Format
Purified
HS Code
3002 15 90
Control
HT-1080 cell lysate
Presentation
Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Applications
Application
This Anti-MT1-MMP Antibody, hemopexin domain is validated for use in WB, IH(P) for the detection of MT1-MMP.
Key Applications
Western Blotting
Immunohistochemistry (Paraffin)
Application Notes
Immunohistochemistry Analysis: A 1:400 dilution of this antibody detected MT1-MMP in human and rat colon tissue.
Biological Information
Immunogen
Recombinant protein corresponding to the entire hemopexin-like domain of MT1-MMP.
Epitope
Hemopoxin Domain
Concentration
Please refer to the Certificate of Analysis for the lot-specific concentration.
Host
Rabbit
Specificity
This antibody recognizes the hemopoxin domain of MT1-MMP.
Species Reactivity
Human
Rat
Horse
Chimpanzee
Rhesus Macaque
Species Reactivity Note
Demonstrated to react with Human and Rat. Predicted to react with Horse, Chimpanzee and Rhesus Macaque based on 100% sequence homology. Other homologies: Pig, Bovine, and Canine (98% sequence homology).
Summary: Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. This protein activates MMP2 protein, and this activity may be involved in tumor invasion. [provided by RefSeq].
FUNCTION: Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7.
CATALYTIC ACTIVITY: Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain.
COFACTOR: Binds 1 zinc ion per subunit (by similarity). Calcium (by similarity).
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein (potential). Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
TISSUE SPECIFICITY: Expressed in stromal cells of colon, breast, and head and neck.
DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
POST-TRANSLATIONAL MODIFICATION: The precursor is cleaved by a furin endopeptidase (by similarity).
SEQUENCE SIMILARITIES: Belongs to the peptidase M10A family. Contains 4 hemopexin-like domains.
Molecular Weight
~66 kDa observed
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Western Blot in HT-1080 cell lysate.
Western Blot Analysis: 0.1 µg/mL of this antibody detected MT1-MMP in 10 µg of HT-1080 cell lysate.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.