Human MMP-9 Quantikine ELISA Kit

Images

 

Product Details

Summary
Reactivity HuSpecies Glossary
Applications ELISA
Conjugate
HRP

Order Details

View Available Conjugates
Catalog# & Conjugate Size Price

Human MMP-9 Quantikine ELISA Kit Summary

Background
The Quantikine Human MMP-9 Immunoassay is a 3.5 hour solid phase ELISA designed to measure MMP-9 (92 kDa pro- and 82 kDa active forms but not the 65 kDa form) in cell culture supernates, saliva, serum, plasma, and urine. It is calibrated with CHO cell-expressed recombinant human pro-MMP-9 and the antibodies were raised against the recombinant factor. Natural human MMP-9 showed dose-response ...curves that were parallel to the standard curves obtained using the recombinant Quantikine kit standards, indicating that this kit can be used to determine relative mass values of natural human MMP-9.
Show More
Specificity
Natural and recombinant human 92 kDa Pro-MMP-9 and the 82 kDa active MMP-9
Source
N/A
Assay Type
Solid Phase Sandwich ELISA
Inter-Assay
See PDF Datasheet for details
Intra-Assay
See PDF Datasheet for details
Spike Recovery
See PDF Datasheet for details
Sample Volume
See PDF Datasheet for details
Gene
MMP9

Applications/Dilutions

Dilutions
  • ELISA
Application Notes
Interference observed with 1 or more available related molecules.
Publications
Read Publications using
DMP900 in the following applications:

Packaging, Storage & Formulations

Storage
Store the unopened product at 2 - 8 °C. Do not use past expiration date.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Human MMP-9 Quantikine ELISA Kit

  • 92 kDa gelatinase
  • 92 kDa type IV collagenase
  • CLG4B
  • EC 3.4.24
  • EC 3.4.24.35
  • Gelatinase B
  • GELB
  • macrophage gelatinase
  • MANDP2
  • matrix metallopeptidase 9
  • matrix metalloproteinase 9
  • matrix metalloproteinase-9
  • MMP9
  • MMP-9
  • type V collagenase

Background

Matrix metalloproteinases (MMPs), also called matrixins, constitute a family of zinc and calcium dependent endopeptidases that function in the breakdown of the extracellular matrix (ECM) and in the processing of a variety of molecules in different subcellular environments. They play an important role in many normal physiological processes such as embryonic development, morphogenesis, reproduction, and tissue remodeling (1, 2). They also participate in inflammatory and autoimmune disorders such as arthritis, cancer, and cardiovascular disease (3-5). While the amounts of newly synthesized MMPs are regulated mainly at the levels of transcription, the proteolytic activities of existing MMPs are controlled through both the activation of proenzymes or zymogens and the inhibition of active enzymes by endogenous inhibitors, alpha 2-Macroglobulin, and tissue inhibitors of metalloproteinases (TIMPs) (6). 
MMP-9 (also referred to as gelatinase B, 92 kDa type IV collagenase, 92 kDa gelatinase, and type V collagenase) is secreted as a glycosylated proenzyme (6-8). Activation of the proenzyme involves proteolytic removal of the N-terminal pro region, resulting in the 82 kDa active enzyme (9, 10). Active human MMP-9 shares 72% and 74% amino acid sequence identity with mouse and rat MMP-9, respectively. In addition to the zinc-binding site, the catalytic domain also contains three contiguous fibronectin type II homology units responsible for binding gelatin (11). A proline-rich hinge region links the catalytic domain to the C-terminal hemopexin-like domain. In vitro treatment of the proenzyme with 4-aminophenylmercuric acetate (APMA) produces not only the active enzyme but also a C-terminal truncated form with activity comparable to that of the active form (12). MMP-9 degrades components of the ECM with high specific activity for denatured collagens (gelatin). It can cleave native collagens of type III, IV, V, and XI, as well as Elastin, Nidogen-1, and Vitronectin (2, 3). MMP-9 can also cleave a variety of chemokines and growth factors (e.g. IL-1 beta , CXCL8/IL-8, CXCL7, CXCL4, CXCL1, Latent TGF-beta , membrane bound TNF-alpha , VEGF, and FGF basic), Amyloid beta peptide, Substance P, and Myelin Basic Protein (3, 13-15). This action can increase or decrease the biological activity of soluble factors and can also liberate them from association with the ECM (16, 17). MMP-9 can also trigger signaling through various transmembrane proteins or inhibit signaling by inducing their shedding from the cell surface (e.g. CD44, E-Cadherin, Integrins, ICAM-1, and IL-2 R alpha ) (3, 18-20). 
MMP-9 is produced by a variety of normal and transformed cells including neutrophils, monocytes, macrophages, astrocytes, fibroblasts, osteoclasts, chondrocytes, keratinocytes, endothelial and epithelial cells. It exerts physiological and pathological angiogenic and remodeling effects on the vasculature (21-25). Activated neutrophils release proMMP-9 which is free of TIMP-1, allowing the liberation of pro-angiogenic FGF-2 from the ECM (17). MMP-9 in complex with TIMP-1 does not induce FGF-2 release (17). Neutrophil-derived MMP-9 exacerbates the inflammatory response, in part by generating collagen-derived peptides that induce the release of additional neutrophil MMP9 (26). MMP-9 also plays a role in bone formation and remodeling (1, 21, 27), methamphetamineinduced behavioral sensitization and reward (28), the regulation of neuronal synapse remodeling (29), trophoblast invasion during implantation (30), and the inactivation of Serpin alpha 1-Proteinase Inhibitor (31). The shedding of adhesion proteins by MMP-9 has a direct effect on tumor cell invasiveness (18-20). 
Circulating levels of MMP-9 are increased in many inflammatory disorders including intraluminal thrombus formation (32), atherosclerosis (33), Crohn's disease (34), hepatitis C virus infection (35), colorectal cancer (36), and Duchenne muscular dystrophy (37). The ratio of MMP-9 to TIMP-1 is also increased in multiple sclerosis serum (38) and cystic fibrosis sputum (39), but it is decreased in the serum during cytomegalovirus infection (40). Levels of free MMP-9 and complexes of MMP-9 with Lipocalin-2/NGAL are elevated in the urine of ovarian cancer and uterine tract infection patients, respectively (41, 42).

Customers Who Viewed This Item Also Viewed...

MMP200
Species: Ca, Hu, Mu, Po, Rt
Applications: ELISA
DTM100
Species: Hu
Applications: ELISA
DVE00
Species: Hu
Applications: ELISA
DTM200
Species: Hu
Applications: ELISA
D6050
Species: Hu
Applications: ELISA
DMP300
Species: Hu
Applications: ELISA
NBP2-67360
Species: Hu, Mu, Rt
Applications: Flow, ICC/IF, IHC, IHC-P, IP, WB
NBP2-67471
Species: Hu, Mu, Rt
Applications: ICC/IF, IHC, IHC-P, WB
NBP2-22203
Species: Hu, Pm, Mu, Rt
Applications: ELISA, Flow, ICC/IF, IHC, IHC-P, WB
1310-SE
Species: Hu
Applications: EnzAct
DMP100
Species: Hu
Applications: ELISA
NB100-56583
Species: Hu, Rb, Rt
Applications: Flow, IHC, IHC-P, KO, WB
NBP2-67415
Species: Hu, Mu, Rt
Applications: Flow, ICC/IF, IHC, IHC-P, IP, WB
DM1300
Species: Hu
Applications: ELISA
NBP2-50037
Species: Hu, Mu, Rt
Applications: ICC/IF, IHC, KO, WB
⚠ WARNING: This product can expose you to chemicals including N,N-Dimethylforamide, which is known to the State of California to cause cancer. For more information, go to www.P65Warnings.ca.gov.

Publications for MMP-9 (DMP900)(186)

We have publications tested in 3 confirmed species: Human, Mouse, Primate.

We have publications tested in 1 application: ELISA Capture.


Filter By Application
ELISA Capture
(3)
All Applications
Filter By Species
Human
(183)
Mouse
(1)
Primate
(2)
All Species
Showing Publications 1 - 10 of 186. Show All 186 Publications.
Publications using DMP900 Applications Species
MM Ali, I Mirza, D Naquiallah, C Hassan, M Masrur, FM Bianco, AM Mahmoud CD147 Levels in Blood and Adipose Tissues Correlate with Vascular Dysfunction in Obese Diabetic Adults Journal of cardiovascular development and disease, 2021;9(1):. 2021 [PMID: 35050217] (Human) Human
D Bakkalci, A Jay, A Rezaei, CA Howard, HJ Haugen, J Pape, S Kishida, M Kishida, G Jell, TR Arnett, S Fedele, U Cheema Bioengineering the ameloblastoma tumour to study its effect on bone nodule formation Scientific Reports, 2021;11(1):24088. 2021 [PMID: 34916549] (Human) Human
S Nawrocka-M, J Biegus, M Hurkacz, M Guzik, M Rosiek-Bie, EA Jankowska, P Ponikowski, R Zymli?ski Differences in the Biomarker Profile of De Novo Acute Heart Failure versus Decompensation of Chronic Heart Failure Biomolecules, 2021;11(11):. 2021 [PMID: 34827701] (Human) Human
A Kuzumi, A Yoshizaki, KM Matsuda, H Kotani, Y Norimatsu, M Fukayama, S Ebata, T Fukasawa, A Yoshizaki-, Y Asano, K Morikawa, Y Kazoe, K Mawatari, T Kitamori, S Sato Interleukin-31 promotes fibrosis and T helper 2 polarization in systemic sclerosis Nature Communications, 2021;12(1):5947. 2021 [PMID: 34642338] (Human) Human
K Wadowska, P B?asiak, A Rzechonek, I Bil-Lula, M ?liwi?ska- New Insights on Old Biomarkers Involved in Tumor Microenvironment Changes and Their Diagnostic Relevance in Non-Small Cell Lung Carcinoma Biomolecules, 2021;11(8):. 2021 [PMID: 34439874] (Human) Human
L Scola, RM Giarratana, V Marinello, V Cancila, C Pisano, G Ruvolo, G Frati, D Lio, CR Balistreri Polymorphisms of Pro-Inflammatory IL-6 and IL-1&beta Cytokines in Ascending Aortic Aneurysms as Genetic Modifiers and Predictive and Prognostic Biomarkers Biomolecules, 2021;11(7):. 2021 [PMID: 34202072] (Human) Human
Y Wu, K Brennan, AB Fernández, MM Mc Gee Cyclophilin A regulates secretion of tumour-derived extracellular vesicles Translational Oncology, 2021;14(8):101112. 2021 [PMID: 33984826] (Human) Human
M Jamka, P Bogda?ski, P Krzy?anows, A Mi?kiewicz, J Karolkiewi, M Du?-?uchow, R M?dry, A Lisowska, A Gotz-Wi?ck, S Iskakova, J Walkowiak, E M?dry Endurance Training Depletes Antioxidant System but Does Not Affect Endothelial Functions in Women with Abdominal Obesity: A Randomized Trial with a Comparison to Endurance-Strength Training Journal of Clinical Medicine, 2021;10(8):. 2021 [PMID: 33921520] (Human) Human
J Jarecki, T Ma?ecka-Ma, I Polkowska, B Potoczniak, E Kosior-Jar, I Szerb, E Tomaszewsk, M Gutbier, M Dobrzy?ski, T Blicharski Level of Adiponectin, Leptin and Selected Matrix Metalloproteinases in Female Overweight Patients with Primary Gonarthrosis Journal of Clinical Medicine, 2021;10(6):. 2021 [PMID: 33803785] (Human) Human
S Sriphoosan, K Thanapirom, SJ Kerr, S Suksawatam, P Thaimai, S Sittisomwo, K Sonsiri, N Srisoontho, N Teeratorn, N Tanpowpong, B Chaopathom, S Treepraser, Y Poovorawan, P Komolmit Effect of vitamin D supplementation in patients with chronic hepatitis C after direct-acting antiviral treatment: a randomized, double-blind, placebo-controlled trial PeerJ, 2021;9(0):e10709. 2021 [PMID: 33614272] (Human) Human
Show All 186 Publications.

Reviews for MMP-9 (DMP900) (0)

There are no reviews for MMP-9 (DMP900). By submitting a review you will receive an Amazon e-Gift Card or Novus Product Discount.
  • Review with no image -- $10/€7/£6/$10 CAD/¥70 Yuan/¥1110 Yen
  • Review with an image -- $25/€18/£15/$25 CAD/¥150 Yuan/¥2500 Yen

Product General Protocols

Find general support by application which include: protocols, troubleshooting, illustrated assays, videos and webinars.

FAQs for MMP-9 (DMP900). (Showing 1 - 1 of 1 FAQs).

  1.  I’m looking for a pair of antibodies to MMP-9 that can be used in a sandwich assay. Do you carry any? 
    • We have 10 primary antibodies for MMP-9 that have been tested in ELISA.https://www.novusbio.com/search?keywords=MMP-9&category=Primary%20Antibodies&applications=ELISA&common_name=MMP-9It looks like 2 have been tested for capture (please note the tested species for each of these).https://www.novusbio.com/search?keywords=MMP-9&category=Primary%20Antibodies&common_name=MMP-9&applications=ELISA%20Capture%20(Matched%20Antibody%20Pair)1 has been tested for detection.https://www.novusbio.com/search?keywords=MMP-9&category=Primary%20Antibodies&common_name=MMP-9&applications=ELISA%20Detection%20(Matched%20Antibody%20Pair)

Additional MMP-9 Products

Bioinformatics Tool for MMP-9 (DMP900)

Discover related pathways, diseases and genes to MMP-9 (DMP900). Need help? Read the Bioinformatics Tool Guide for instructions on using this tool.
Visit Tool

Diseases for MMP-9 (DMP900)

Discover more about diseases related to MMP-9 (DMP900).
 

Pathways for MMP-9 (DMP900)

View related products by pathway.

PTMs for MMP-9 (DMP900)

Learn more about PTMs related to MMP-9 (DMP900).

Blogs on MMP-9.

Cytokeratin 18 - A Intermediate Filament Cyotskeletal Component
Keratins, also called cytokeratins, are a family of filamentous structural proteins that form the intermediate filaments within epithelial cells. Keratins are differentially expressed depending on both the epithelial cell origin and degree of differen...  Read full blog post.

Customers Who Bought This Also Bought

Contact Information

Product PDFs

Review this Product

Be the first to review our Human MMP-9 Quantikine ELISA Kit and receive a gift card or discount.

Bioinformatics

Gene Symbol MMP9