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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

UNSPSC Code:
12352203

biological source

mouse

Quality Level

antibody form

purified antibody

antibody product type

primary antibodies

clone

6-6B, monoclonal

form

lyophilized

does not contain

preservative

species reactivity

human

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze

isotype

IgG1

shipped in

ambient

storage temp.

2-8°C

target post-translational modification

unmodified

Gene Information

human ... MMP9(4318)

General description

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).

Immunogen

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)

Warning

Toxicity: Standard Handling (A)

Physical form

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.

Analysis Note

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

Other Notes

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.

Legal Information

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

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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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
Daniel J Price et al.
Cell communication & adhesion, 9(2), 87-102 (2002-12-19)
We studied the invasion of HMT-3522 breast epithelial cells in response to epidermal growth factor (EGF), and the associated signaling pathways. HMT-3522 T4-2 cells were shown to invade Matrigel-coated Transwell membranes in response to EGF while HMT-3522 S-1 cells failed
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
Agnes Schäfer et al.
Frontiers in oncology, 12, 826273-826273 (2022-04-05)
Glioblastoma (GBM) as the most common and aggressive brain tumor is characterized by genetic heterogeneity, invasiveness, radio-/chemoresistance, and occurrence of GBM stem-like cells. The metalloprotease-disintegrin ADAM8 is highly expressed in GBM tumor and immune cells and correlates with poor survival.

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