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QuickZyme Human MMP-9 Activity Assay Kit 96-Assays

  • Regulatory status:RUO
  • Type:ELISA
  • Other names:Matrix Metalloproteinase-9, MMP9
  • Species:Human
Cat. No. Size Price


Discount QZBMMP9H 96 wells (1 kit) $1242,89
PubMed Product Details
Technical Data

Type

ELISA

Description

The QuickZyme human MMP-9 activity assay enables you to specifically measure in biological samples both active human MMP-9, as well as (pro)MMP-9 which is activated on the plate by APMA. It can be used for the measurement of MMP-9 activity in various biological samples, such as conditioned culture media, tissue homogenates, serum, plasma and urine.

Applications

Serum, Urine, Plasma, Tissue homogenates, Cell culture conditioned medium

Sample Requirements

10 - 100 µl

Shipping

On dry ice. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Unopened kit: Store at -20°C, except for the standard, this vial should be stored at -70°C. Do not use kit, or individual kit components past kit expiration date.

Opened kit / reconstituted reagents: Please refer to kit manual.

Calibration Range

0 - 16 ng/ml

Limit of Detection

0.1 ng/ml (1 hr incubation)

0.005 ng/ml (4 hr incubation)

Summary

Features

  • Measures endogenous active MMP-9 ( naturally occurring ) or total active MMP-9 ( following activation with APMA ).

  • Samples: conditioned cell culture medium, serum, plasma, urine, synovial fluid and tissue homogenates.

  • Quantitative.

  • Range: 0.5 to 16 ng/ml (1 h incubation with detection reagent), 0.01-1 ng/ml (4 h incubation with detection reagent).

  • Sensitivity: 0.005 ng/ml.

  • Ease-of-use: Equivalent to ELISA.

Research topic

Bone and cartilage metabolism, Cardiovascular disease, Extracellular matrix, Immune Response, Infection and Inflammation, Neural tissue markers, Oncology, Others, Pulmonary diseases

Summary

Matrix metalloproteinases (MMPs) are a family of enzymes that function in the remodeling of extracellular matrix proteins. They are essential for various normal physiological processes such as embryonic development, morphogenesis, reproduction tissue resorption and tissue remodeling. They also play a role in a number of pathological processes such as inflammation, arthritis, cardiovascular diseases, fibrosis and cancer. Regulation of MMPs is carried out at various levels. Expression of latent MMPs is regulated at the level of transcription, whereas the proteolytic activity is controlled by specific activation of proMMPs, and by MMP-specific inhibitors, the tissue inhibitors of metalloproteinases (TIMPs) or general circulatory inhibitors, such as α2macroglobulin. The MMPs can be grouped according to their domain structure into collagenases, gelatinases, stromelysins, membrane type MMPs and matrilysins. MMP-9 (also known as type neutrophil gelatinase, IV collagenase, Gelatinase B; EC 3.4.24.35) has a broad range of substrate specificity for denatured collagens (gelatins), native collagens (types IV, V and XI), as well as elastin. Human MMP-9 has a Mw of 92 kDa (pro-form) and 82 kDa (active form). The activity is dependent on Zn2+ and Ca2+. MMP-9 is secreted as proMMP-9, and can be activated in vitro by organo mercurial compounds such as p-aminophenyl mercuric acetate (APMA). MMP-9 is produced by a variety of cell types including monocytes, macrophages, fibroblasts, neutrophils, osteoclasts, chondrocytes, keratinocytes, endothelial and epithelial cells. The QuickZyme human MMP-9 activity assay enables you to specifically measure in biological samples both active human MMP-9, as well as (pro)MMP-9 which is activated on the plate by APMA. It can be used for the measurement of MMP-9 activity in various biological samples, such as conditioned culture media, tissue homogenates, serum, plasma and urine.

Summary References (23)

References to MMP-9

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  • Gingis-Velitski S, Loven D, Benayoun L, Munster M, Bril R, Voloshin T, Alishekevitz D, Bertolini F, Shaked Y. Host response to short-term, single-agent chemotherapy induces matrix metalloproteinase-9 expression and accelerates metastasis in mice. Cancer Res. 2011 Nov 15;71 (22):6986-96
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  • Ohbayashi H. Matrix metalloproteinases in lung diseases. Curr Protein Pept Sci. 2002 Aug;3 (4):409-21
  • Opdenakker G, Nelissen I, Van Damme J. Functional roles and therapeutic targeting of gelatinase B and chemokines in multiple sclerosis. Lancet Neurol. 2003 Dec;2 (12):747-56
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  • Opstad TB, Pettersen AA, Arnesen H, Seljeflot I. The co-existence of the IL-18+183 A/G and MMP-9 -1562 C/T polymorphisms is associated with clinical events in coronary artery disease patients. PLoS One. 2013;8 (9):e74498
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