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Facts about Matrix metalloproteinase-9.
Cleaves KiSS1 at a Gly-.
Human | |
---|---|
Gene Name: | MMP9 |
Uniprot: | P14780 |
Entrez: | 4318 |
Belongs to: |
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peptidase M10A family |
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
Mass (kDA):
78.458 kDA
Human | |
---|---|
Location: | 20q13.12 |
Sequence: | 20; NC_000020.11 (46008908..46016561) |
Produced by normal alveolar macrophages and granulocytes.
Secreted, extracellular space, extracellular matrix.
MMP-9, a recombinant , human-derived protein human beings, is released into the bloodstream. It can be used as a biomarker for diagnostic purposes or a an chemiluminescent test. The Boster product credits are open to any scientist around the globe. This article will provide more information about MMP-9. Here, you'll learn about the most effective uses of the MMP9 marker.
Recombinant MMP-9 A purified recombinant proteins from the human body, has an N-terminal tag with hexahistidine that corresponds to the catalytic domain. It has residues 113-450. It is used as an immunological control that can be used as a positive in tests. MMP-9 is a potent proteolytic enzyme involved in the pathogenesis of various cancers and inflammatory diseases.
The His-Tag variant of MMP-9 is created from human 293 cells. The protein is a mixture of AA Ala 20 - Pro 469 and needs activation to develop hydrolytic activity. This protein has a polyhistidine tag located at the C-terminus. It has a molecular mass (MW) 50.8 kDa. Under reducing conditions, it migrates at a size between the 58 and 66kDa.
MMP-9 is produced by neutrophils and macrophages, and the recombinant MMP-9 was purified from monocytes from humans. The gelatin affinity-sepharose chromatography was used to determine the purified MMP-9 and it was cleaved by the bigh3 protein. The purified MMP-9 inhibits bigh3 protein degradation. This is an interesting clinical trial for MMP-9.
MMP-9 is a human recombinational protein that regulates extracellular matrix composition. Big-h3, the recombinant protein of human, is composed of 182 amino acids which corresponds to the C-terminal segment of big-h3. The recombinant human protein induces macrophage migratory patterns and enhances phosphorylation FAK/Src. The Food and Drug Administration approved the purified MMP-9 as a powerful recombinant protein.
MMP-9 is a protein found in the cytosol and released into cells by cells. It is a zinc-dependent peptidase that is involved in the process of tissue remodeling and wound healing. MMP-9 is known to perform many functions, which include inflammation, infection, and oxidative stresses. This recombinant human protein is an effective medical supplement.
The docking site for MMP-9 is vital for its activity. MMP-9 releases big-h3 from the cell's surface when it cleaves bigh3. This might reduce MMP-9's capacity to interact with ECM proteins. However, the exact mechanism behind MMP-9's actions is unknown. It is important to note that MMP-9 can inhibit the invasion of tumors and their migration.
MMP9 protein is easily detectable in peripheral blood samples of patients with melanoma. MMP-9 has been found to be a good marker for aggression and therapeutic response in patients with melanoma. The protein is used in a variety of ways in pathology and biotechnology. This article will highlight the most effective uses for the MMP9 marker. You might also be interested in learning more about its biochemical properties.
The expression of MMP9 is influenced by AAA's maximum aortic diameter with MMP9 activity rising with an increase in the size of the aneurysm. Studies by Freestone and colleagues. discovered that MMP9 expression was elevated in AAA with a diameter ranging between 5 and 6 centimeters. However, other studies, like those of Eugster and colleagues, discovered no significant relationship between MMP9 and AAA diameter.
While there are a variety of uses for MMP-9, its value as an diagnostic biomarker is being studied. It is being investigated as a biomarker that can be used to diagnose diseases. However, there are few aspects that must be considered before making any decision. This article will review the advantages and disadvantages of MMP-9 biomarkers as cancer biomarkers.
MMP9 is a type of protein produced by smooth muscle cells, endothelial cells from the aortic and infiltrating inflammation-related cells. Its presence is strongly associated with the presence of an aortic aneurysm. Therefore, it may be an important diagnostic biomarker in both AAA and TAA. Recent research has revealed that MMP9 can be used to aid doctors in identifying the two conditions.
In pancreatic tissue of PDAC patients The MMP9 enzyme is abundantly expressed. An immunohistochemical study and western blot analysis confirmed the discovery. The levels of MMP-9 in blood were significantly higher in PDAC patients than chronic pancreatitis patients. More research is required to confirm the diagnostic function of MMP-9 for pancreatic cancer.
A study, published in JACC: Journal of the American College of Cardiology & the Society of Hypertension, has been published.
It was extremely accurate to diagnose breast cancer by taking the serum levels of MMP-9 and Trx-1. Additionally the levels of these two enzymes were correlated with the clinical pathological characteristics of patients suffering from breast cancer. Additionally, MMP-9 has demonstrated a positive correlation with levels of CA15-3 and CEA in breast cancer. Boster Bio MMP9 is used as a diagnostic biomarker.
The metastasis of breast cancer is also affected by the MMP9 enzyme. Sinha and. found that MMP-9 upregulation decreased the IC50 value of chemotherapy drugs in breast cancer cells. This study also showed that MMP-9 was a potential therapeutic target for breast cancer metastasis. However, further research is needed to prove the effectiveness of MMP-9 as an indicator of diagnosis.
The MMP-9 chemiluminescent test provides an exact and quantifiable measure of the concentration of this protein. This test uses lyophilized protein that has been reconstituted in 50uL of MilliQ Water. The reagents then used in the assay. This assay will determine the concentrations of MMP-9, TIMP-1, and TIMP-1. They will be zero, thirty and one hundred, three hundred, three hundred, and one million ng/mL. All readings will be subtracted from the luminescence of the blank, that is equal to zero ng/mL MMP-9 or zero ng/mL of TIMP-1.
MMP-9, a crucial protein, performs a variety of roles in the body, including tissue remodeling, inflammation cell migration, cell migration. The blood level of MMP-9 is increased in inflammatory situations such as atherosclerosis, hepatitis C virus cancer, and colorectal. MMP-9 is a marker for many types of diseases. Its high levels are detected in various types of tumors, inflammatory conditions and autoimmune conditions.
MMP-9 and TIMP-1 are two of the major enzymes that are found in the body. Both of these enzymes are vital for proper functioning of your body. This test is able to detect both proteins in urine and blood. After use, the results are available immediately. The Boster Bio MMP9 chemiluminescent test is easy and affordable. It delivers quick and reliable results.
The reagents that were used in the assay were bought from various vendors. First, SO-RB50 cells are lysed in RIPA buffer, and then centrifuged at 4,472x grams for five minutes at 4°C. After lysis the protein extract was dilute twofold in the sample buffer. Then, the protein extract was transferred onto the membranes of nitrocellulose.
The reagents that are used in the MMP-9 cheiluminescent test are supplied with pre-dilutions of 100 uL of Tween-20 and 10% of ethanol. The final reaction volume is 200 U. Before proceeding to step three, the 400 mM NaBH3CN solution has to be prepared fresh. The assay will take about 20 minutes.
PMID: 2551898 by Wilhelm S.M., et al. SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages.
PMID: 1653238 by Huhtala P., et al. Complete structure of the human gene for 92-kDa type IV collagenase. Divergent regulation of expression for the 92- and 72-kilodalton enzyme genes in HT-1080 cells.
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