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Principaux documents

AB19167

Sigma-Aldrich

Anti-MMP-2 Antibody, whole molecule

Chemicon®, from rabbit

Synonyme(s) :

72 kDa gelatinase, 72kD type IV collagenase, Gelatinase A, Matrix metalloproteinase-2, collagenase type IV-A, matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase), matrix metalloproteinase 2, matrix metalloproteinase 2 (g

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About This Item

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

Source biologique

rabbit

Forme d'anticorps

purified antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Espèces réactives

bovine, rat

Réactivité de l'espèce (prédite par homologie)

human, mouse

Fabricant/nom de marque

Chemicon®

Technique(s)

immunohistochemistry: suitable (paraffin)
western blot: suitable

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Informations sur le gène

human ... MMP2(4313)

Description générale

MMPs have a common mode of activation, a conserved amino acid sequence in the putative metal-binding active site region and are inhibited by specific tissue inhibitors of metalloproteinases (TIMPs). These MMPs and TIMPs could be expressed by either the cancer of the stromal cells. There is a co-operation between tumor and stromal cells, in particular for the production of 72-kD type IV collagenase, involved in the disruption of basement membranes. A lack of TIMP-1 expression from invasive cancer cells could also contribute to matrix destruction.

Spécificité

AB19167 recognizes protein at 72 kDa, identified as matrix metalloproteinase 2. MMP-2 is also known as 72 kDa collagenase IV or gelatinase A. It is synthesized as a 631 amino acid proenzyme that is activated by cleavage of the first 80 amino acids. AB19167 shows no cross-reaction with (pro) and active forms of other MMPs. Cytoplasmic localization.
Reactivity with other species has not been confirmed.

Immunogène

A synthetic peptide from the second half of human MMP-2.
Epitope: Whole molecule

Application

Detect MMP-2 using this Anti-MMP-2 Antibody, whole molecule validated for use in IH(P) & WB.
Immunohistochemistry (formalin/paraffin):
10-20 µg/mL of a previous lot was kept for 30 min at RT. No special pretreatment is required for staining formalin-fixed paraffin-embedded sections.

Optimal working dilutions must be determined by the end user.
Research Category
Cell Structure
Research Sub Category
MMPs & TIMPs

Qualité

Routinely evaluated by Western Blot on PC12 lysates.

Western Blot Analysis: 1:500 dilution of this lot detected MMP-2 on 10 µg of PC12 lysates.

Description de la cible

72 kDa

Liaison

Replaces: 04-1048

Forme physique

Format: Purified
Protein A chromatography
Purified rabbit polyclonal in buffer containing 10 mM PBS, pH 7.4, with 0.2% BSA and 0.09% sodium azide.

Stockage et stabilité

Stable for 1 year at 2-8ºC from date of receipt.

Remarque sur l'analyse

Control
Positive control: Conditioned, serum-free medium from TPA-treated human fetal lung (HFL-1) cells. Placenta or bladder, breast, or ovarian carcinomas.

Autres remarques

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

Informations légales

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

Clause de non-responsabilité

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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Code de la classe de stockage

10-13 - German Storage Class 10 to 13


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Hong-Yi Kuo et al.
Cell cycle (Georgetown, Tex.), 13(19), 3132-3142 (2014-12-09)
Promyelocytic leukemia protein (PML) is emerging as an important tumor suppressor. Its expression is lost during the progression of several types of cancer, including lung cancer. The EGF receptor (EGFR), a membrane-bound receptor tyrosine kinase, transduces intracellular signals responsible for
Lies De Groef et al.
Mediators of inflammation, 2015, 108617-108617 (2015-10-10)
Matrix metalloproteinases (MMPs) have been designated as both friend and foe in the central nervous system (CNS): while being involved in many neurodegenerative and neuroinflammatory diseases, their actions appear to be indispensable to a healthy CNS. Pathological conditions in the
Silibinin inhibits established prostate tumor growth, progression, invasion, and metastasis and suppresses tumor angiogenesis and epithelial-mesenchymal transition in transgenic adenocarcinoma of the mouse prostate model mice.
Singh, RP; Raina, K; Sharma, G; Agarwal, R
Clinical cancer research : an official journal of the American Association for Cancer Research null
Qi Sun et al.
Frontiers in neuroscience, 10, 593-593 (2017-01-20)
This study was to explore the mechanisms underlying 1,2-dichloroethane (1,2-DCE) induced brain edema by focusing on alteration of matrix metalloproteinase-2 (MMP-2) in rat astrocytes induced by 2-chloroethanol (2-CE), an intermediate metabolite of 1,2-DCE in vivo. Protein and mRNA levels of
Marvin Ferrer et al.
Cell and tissue research, 349(3), 881-895 (2012-06-26)
Sperm-zona pellucida (ZP) penetration during fertilization is a process that most likely involves enzymatic digestion of this extracellular coat by spermatozoa. Since the inner acrosomal membrane (IAM) is the leading edge of spermatozoa during penetration and proteins required for secondary

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