MAB3308
Anti-MMP-2 Antibody, a.a. 468-483 hMMP2, clone 42-5D11
clone 42-5D11, Chemicon®, from mouse
Sinonimo/i:
Gelatinase A, 72 kDa Type IV Collagenase
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About This Item
Codice UNSPSC:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Prodotti consigliati
Origine biologica
mouse
Livello qualitativo
Forma dell’anticorpo
purified antibody
Tipo di anticorpo
primary antibodies
Clone
42-5D11, monoclonal
Reattività contro le specie
rat, bovine, human, rabbit, horse, mouse, pig
Produttore/marchio commerciale
Chemicon®
tecniche
ELISA: suitable
immunohistochemistry: suitable (paraffin)
western blot: suitable
Isotipo
IgG1κ
N° accesso NCBI
N° accesso UniProt
Condizioni di spedizione
dry ice
modifica post-traduzionali bersaglio
unmodified
Informazioni sul gene
human ... MMP2(4313)
Descrizione generale
The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane-bound zinc endopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non-fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer′s, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.
MMP2, also known as Gelatinase A, is a type IV collagenase that specifically cleaves type IV collagen, the major structural component of basement membranes. The metastatic potential of tumor cells has been found to correlate with the activity of this enzyme.
MMP2, also known as Gelatinase A, is a type IV collagenase that specifically cleaves type IV collagen, the major structural component of basement membranes. The metastatic potential of tumor cells has been found to correlate with the activity of this enzyme.
Specificità
Specifically reacts with precursor and active forms of human MMP-2. Does not cross react with human MMP-1, -3, -9, or -13. Also reacts with rat, mouse, and bovine MMP2, other species not tested.
Immunogeno
Epitope: a.a. 468-483 hMMP2
Synthetic oligopeptide corresponding to amino acid residue 468-483 (VTPRDKPMGPLLVATF) of human matrix metalloproteinase 2 (human MMP-2, gelatinase A).
Applicazioni
Immunoblotting 1-5 μg/mL
Immunohistochemistry on frozen and paraffin-embedded tissues using PLP fixation: 1-5 μg/mL (has not been tested in traditional formalin fixed tissues)
ElA
Immunohistochemistry on frozen and paraffin-embedded tissues using PLP fixation: 1-5 μg/mL (has not been tested in traditional formalin fixed tissues)
ElA
Research Category
Cell Structure
Cell Structure
Research Sub Category
MMPs & TIMPs
MMPs & TIMPs
This Anti-MMP-2 Antibody, a.a. 468-483 hMMP2, clone 42-5D11 is validated for use in ELISA, IH(P), WB for the detection of MMP-2.
Descrizione del bersaglio
72 kDa
Stato fisico
Format: Purified
Liquid in 0.1 M sodium phosphate buffer, pH 7.0 containing 2% protease free bovine Serum albumin.
Protein A purified
Stoccaggio e stabilità
Maintain for 1 year at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Risultati analitici
Control
Lung, nerve, and various soft tissue tumors
Lung, nerve, and various soft tissue tumors
Altre note
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Note legali
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
Esclusione di responsabilità
Manufactured by Daiichi Fine Chemical Co., Ltd
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.
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.
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Codice della classe di stoccaggio
12 - Non Combustible Liquids
Classe di pericolosità dell'acqua (WGK)
WGK 2
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Certificati d'analisi (COA)
Cerca il Certificati d'analisi (COA) digitando il numero di lotto/batch corrispondente. I numeri di lotto o di batch sono stampati sull'etichetta dei prodotti dopo la parola ‘Lotto’ o ‘Batch’.
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I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
A one-step sandwich enzyme immunoassay for human matrix metalloproteinase 2 (72-kDa gelatinase/type IV collagenase) using monoclonal antibodies
Fujimoto, N. et al.
Clinica Chimica Acta; International Journal of Clinical Chemistry, 221, 91-103 (1993)
Alteration of matrix metalloproteinases in selective left ventricular adriamycin-induced cardiomyopathy in the pig.
Goetzenich A, Hatam N, Zernecke A, Weber C, Czarnotta T, Autschbach R, Christiansen S
The Journal of Heart and Lung Transplantation : the Official Publication of the International Society For Heart Transplantation null
Expression of MMP-2 and MMP-9 in the rat trigeminal ganglion during the development of temporomandibular joint inflammation.
Nascimento, GC; Rizzi, E; Gerlach, RF; Leite-Panissi, CR
Brazilian journal of medical and biological research null
Glycogen synthase kinase-3beta is activated by matrix metalloproteinase-2 mediated proteolysis in cardiomyoblasts.
Kandasamy, Arulmozhi D and Schulz, Richard
Cardiovascular Research, 83, 698-706 (2009)
C S Ceron et al.
British journal of pharmacology, 160(1), 77-87 (2010-03-25)
Increased oxidative stress and up-regulation of matrix metalloproteinases (MMPs) may cause structural and functional vascular changes in renovascular hypertension. We examined whether treatment with spironolactone (SPRL), hydrochlorothiazide (HCTZ) or both drugs together modified hypertension-induced changes in arterial blood pressure, aortic
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