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IM09L

Sigma-Aldrich

Anti-MMP-9 (Ab-1) Mouse mAb (6-6B)

lyophilized, clone 6-6B, Calbiochem®

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

Forme d'anticorps

purified antibody

Type de produit anticorps

primary antibodies

Clone

6-6B, monoclonal

Forme

lyophilized

Ne contient pas

preservative

Espèces réactives

human

Fabricant/nom de marque

Calbiochem®

Conditions de stockage

OK to freeze

Isotype

IgG1

Conditions d'expédition

ambient

Température de stockage

2-8°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... MMP9(4318)

Description générale

Matrix metalloproteinases (MMP′s) are a family of enzymes that are responsible for the degradation of extracellular matrix components such as collagen, laminin and proteoglycans. In addition to sequence homology, all MMP′s share the following characteristics: the catalytic mechanism is dependent upon a zinc ion at the active center, they cleave one or more extracellular matrix components, they are secreted as zymogens which are activated by removal of an ~10 kDa segment from the N terminus and they are inhibited by tissue inhibitor of metalloproteinases (TIMP). These enzymes are involved in normal physiological processes such as embryogenesis and tissue remodeling and may play an important role in arthritis, periodontitis, and metastasis.MMP-9 (Gelatinase B, 92 kDa gelatinase/type IV collagenase) is secreted as a 92 kDa zymogen which is proteolytically processed to the 83 kDa active form; a 68 kDa has also been detected. MMP-9, along with its most closely related member of the MMP family, MMP-2, show substrate specificity toward type IV and V collagens, gelatin and elastin. Numerous studies have shown a correlation between collagenase expression and metastatic potential. Elevated levels of MMP-9 in plasma suggest that it may be a useful marker for the diagnosis or prognosis of cancer in general.
Purified mouse monoclonal antibody. Recognizes the ~92 kDa latent and the ~83 kDa active forms of human MMP-9 under non-reducing conditions, but only the latent form under reducing conditions.
Recognizes the ~92 kDa latent and the ~83 kDa active forms of MMP-9 under non-reducing conditions, but only the latent form under reducing conditions. Inhibits the enzymatic activity of MMP-9. For paraffin sections, use Cat. No. IM37L.
This Anti-MMP-9 (Ab-1) Mouse mAb (6-6B) is validated for use in Immunoblotting, Immunoprecipitation, Neutralization Studies, Paraffin Sections for the detection of MMP-9 (Ab-1).

Immunogène

Human
MMP-9 from conditioned medium of PMA-stimulated HT-1080 human fibrosarcoma cells

Application

Immunoblotting (2 µg/ml)

Immunoprecipitation (see appplication references)

Neutralization Studies (see comments and application references)

Paraffin Sections (not recommended)

Avertissement

Toxicity: Standard Handling (A)

Forme physique

Lyophilized from a volatile buffer, 100 µg BSA.

Reconstitution

Store at 4°C until reconstituted, then store in aliquots at -20°C or at 4°C with 0.1% azide. Resuspend the antibody with sterile PBS, pH 7.4, or sterile 20 mM Tris-saline, pH 7.4, to yield a final concentration of 100 µg/ml; product will be more stable if 0.1% sodium azide is included (do not add azide if antibody is to be used with viable cells). Lyophilized antibodies should be resuspended at 4°C with occasional gentle mixing for at least 2 h. Freezing of aliquots is best for long-term storage of reconstituted product; repetitive freezing and thawing should be avoided.

Remarque sur l'analyse

Positive Control
MMP-9 protein (Cat. Nos. PF024 or PF038)

Autres remarques

Cottam, D.W. and Rees, R.C. 1993. Intl. J. of Oncol.2, 861.
Nakajima, M., et al. 1993. Cancer Res.53, 5802.
Ramos-DeSimone, et al. 1993. Hybridoma. 12, 349.
Stetler-Stevenson, W.G., et al. 1993. FASEB.7, 1434.
Zucker, S., et al. 1993. Cancer Res.53, 140.
Woessner, J.F. 1991. FASEB. 5, 2145.
Liotta, L.A. and Stetler-Stevenson, W.G. 1990. in Seminars in Cancer Biology, ed. M.M. Gottesman. Vol. 1; 99-106.
Inhibits MMP-9 enzymatic activity. For staining paraffin sections, use Anti-MMP-9 (626-644) (Ab-3) Mouse mAb (56-2A4) (Cat. No. IM37L). Antibody should be titrated for optimal results in individual systems.

Informations légales

Not available for sale in Japan.
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2


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Consulter la Bibliothèque de documents

N Buisson-Legendre et al.
The Journal of investigative dermatology, 115(2), 213-218 (2000-08-22)
Primary cultures of psoriatic keratinocytes proliferated at a higher rate and produced lower amounts of matrix metalloproteinase 9 than normal keratinocytes cultured under similar conditions. Sup- plementation of psoriatic keratinocyte cell culture medium with batimastat or the use of a
Yao Tong et al.
Journal of inflammation research, 14, 5079-5094 (2021-10-23)
Acute lung injury (ALI) is a severe respiratory disease with high rates of morbidity and mortality. Many mediators regarding endogenous or exogenous are involved in the pathophysiology of ALI. Here, we have uncovered the involvement of integrins and matrix metalloproteinases
Min Hee Park et al.
Stem cells (Dayton, Ohio), 34(8), 2145-2156 (2016-04-20)
Hematopoietic stem/progenitor cell (HSPC) mobilization is an essential homeostatic process regulated by the interaction of cellular and molecular components in bone marrow niches. It has been shown by others that neurotransmitters released from the sympathetic nervous system regulate HSPC egress
Menna R Clatworthy et al.
Nature medicine, 20(12), 1458-1463 (2014-11-11)
Antibodies are critical for defense against a variety of microbes, but they may also be pathogenic in some autoimmune diseases. Many effector functions of antibodies are mediated by Fcγ receptors (FcγRs), which are found on most immune cells, including dendritic
Andreas Behren et al.
Cancer research, 65(24), 11613-11621 (2005-12-17)
Papillomaviruses are involved in the development of cancers of the female cervix, head and neck, and skin. An excellent model to study papillomavirus-induced tumor induction and progression is the New Zealand White rabbit, where the skin is infected with the

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