Matrilysin Antibodies

Matrilysin (MMP7)

Degrades casein, gelatins of types I, III, IV, and V, and fibronectin.

Activates procollagenase.

.

Gene Information

Human
Gene Name:	MMP7
Uniprot:	P09237
Entrez:	4316

Family

Belongs to:
peptidase M10A family

Alternative Names

EC 3.4.24; EC 3.4.24.23; Matrilysin; matrin; matrix metallopeptidase 7 (matrilysin, uterine); matrix metalloproteinase 7 (matrilysin, uterine); Matrix metalloproteinase-7; MMP7; MMP-7; MPSL1; Pump-1 protease; PUMP1; PUMP-1; uterine matrilysin; Uterine metalloproteinase

Molecular Weight

Mass (kDA):
29.677 kDA

Genomic Context

Human
Location:	11q22.2
Sequence:	11; NC_000011.10 (102520508..102530747, complement)

Subcellular Localizations

Secreted, extracellular space, extracellular matrix.

Diseases

• Malignant Neoplasms
• Neoplasms
• Neoplasm Metastasis
• Carcinoma
• Cell Invasion
• Neoplasm Invasiveness
• Adenocarcinoma
• Colorectal Cancer
• Inflammation
• Malignant Tumor Of Colon
• Colorectal Neoplasms
• Malignant Paraganglionic Neoplasm
• Lung Neoplasms

• Colonic Neoplasms
• Cell Transformation, Neoplastic
• Fibrosis
• Carcinogenesis
• Tissue Adhesions
• Tumor Angiogenesis
• Malignant Neoplasm Of Breast

Interacting Proteins

• LGALS3

Pathways

• Cell Proliferation
• Pathogenesis
• Angiogenesis
• Cell Migration
• Secretion
• Localization
• Cell Cycle
• Tissue Remodeling
• Cell Adhesion
• Inflammatory Response
• Cell Death
• Regeneration
• Immune Response

• Proteolysis
• Reverse Transcription
• Aging
• Cell Motility
• Cell Differentiation
• Cell Cycle Arrest
• Cell Growth

PTMs

• Cleavage
• Phosphorylation
• Methylation
• Amidation

• Demethylation
• Reduction
• Glycosylation
• Oxidation

• Dephosphorylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/MMP7

Best Uses Of The MMP7 Marker

MMP7 is a human recombinant enzyme, which could be used for therapeutic purposes. It has high affinity for human proteins and has been extensively validated in immunohistochemistry, Western Blotting and ELISA. This article will cover the best applications for this marker as well as what to look for in an anti-body. It is also available as a baculovirus which means there are less risks.

MMP-7 is a human recombinant enzyme.

Recombinant human MMP-7 is produced in insect cells through the baculovirus infection. It is produced by serum-free conditioning media. After incubation with 50 mM 4-aminophenylmercuric acetate (AMAC), the enzyme transforms from its zymogen state to an active form.

MMP-7 is a protein that is found in the glandular epithelium. Although it is not involved in the degrading of extracellular matrix in normal tissue MMP-7 is a protein expressed by invaders of colon tumors. It has also been linked to an increase in tumor cell proliferative capacity, metastases, as well as metastases. It isn't known how MMP-7 is created.

The Boster Bio MMP-7 ELISA Kit utilizes the sandwich ELISA method. Monoclonal antibodies that are specific to MMP-7 are coated onto 96-well plates. The wells are then coated with monoclonal antibodies that are specific for MMP-7. Then, an Avidin-Biotin-Peroxidase (HRP) enzymatic reaction is visualized by incubation with the reagent.

In addition to its role in innate host defense MMP-7 can also be linked to the development of pulmonary fibrosis and the herniated discs' resorption. It also cuts FasL to form an insoluble form in a model of prostate involution. MMP-7 is the smallest MMP is composed of two domains. The pro-domain is activated upon activation and is the one that cuts. The catalytic domain contains zinc binding site.

MMP-9 activity is related to lung function as measured by the Tiffeneau-Pinelli Index. It has also been associated to the remodeling of airways in COPD. Further studies are required to confirm the efficacy of this recombinant enzyme in treating COPD. The Boster Bio MMP-7 is a recombinant human enzyme

It is not involved in ECM degradation

MMP7 is not directly involved in ECM degradation. This protein aids in the growth of tumors by altering ECM stiffness. This stiffness can act as an actual barrier that encourages resistance to anticancer drugs. For example lung cancer cells which express high levels collagen IV are protected from apoptosis induced by chemotherapy. Cetuximab, an epidermal Factor receptor inhibitor, may trigger fibronectin production. This could be a mechanism for radioresistance in tumours.

The degradation of ECM removes physical barriers and releases biologically active molecules. It also uncovers previously undiscovered locations in the ECM. Invadopodia are a part of this process. They are protrusions of actin that extend from the plasma membrane. Invadopodia accumulate MT-1MMP. Soluble MMPs attach on to the integrins, CD44 and other surfaces of invadopodia. Different ECM ingredients are degraded by soluble MMPs, releasing various types of molecules.

In reality, the degrading of ECM components is a key element in the development of organs and tissues. Although it is well-controlled in physiological conditions, the dysfunction of ECM is associated with numerous diseases, including cancer. This process requires a variety of proteases, such as MMPs. Matrix metalloproteinases is the family of enzymes that are responsible for MMP degradation. They are cell membrane-anchored or soluble enzymes. They are the most important players in ECM degrading due to their broad substrate-specificity.

In certain situations there are instances where excessive ECM deposition could lead to organ failure. Myelofibrosis can result from chronic liver injuries and bone marrow. This can increase the risk of developing cancer. Similar to breast cancer, in breast an increase in mammographic density has been linked to a higher incidence of breast cancer. These are just some of the conditions in which MMP7 is overexpressed.

It could be a therapeutic target

The MMP7 protein is the smallest secreted proteolytic enzyme. It is extremely specific against a range of molecules and ECM elements. It is implicated in a number of malignant diseases , including lung cancer, prostate cancer and pancreatic cancer. The overexpression of MMP-7 may contribute to invasion or metastasis. There are currently no approved drugs for MMP-7.

MMPs are an important component of carcinogenesis. They act as physical barriers to metastasis. They are especially important regulators of fibrosis. While MMPs are expressed in a wide range in various malignancies but they have significant impacts on nearly every stage of tumor growth. MMP7 expression is associated with metastasis and invasion of a variety of kinds of renal cancer.

Boster Bio's MMP7 marker targets IL-8. It has also shown promising results in animal studies. It is the first protein molecule developed for the treatment and prevention of cancer. This breakthrough is a significant move towards the development of new anti-cancer treatments. However the MMP7 protein is not a cure-all. It is a biomarker that can be used to predict the progress of a disease. It isn't known whether this molecule is suitable for this function.

Although MMP7 is not a therapeutic target however, it is believed to play an important part in the development and growth of fibrotic lesions within the kidneys. It is important to note that MMP-7 contributes to fibrotic lesions in three different pathways: epithelial-mesenchymal transition, TGF-b signaling, and deposition of ECM. Therefore, a better understanding of the crosstalk among these pathways can help to identify new ways to treat this disease.

It is also available as Baculovirus

Baculovirus Recombinant MMP7 is a popular recombinant protein that is available as an baculo virus or as a baculovirus derivative. Baculoviruses come from baculoviruses and have been shown to induce MMP7 breaking down in the human body. Baculovirus MMP7 recombinant MMP7 can be utilized as a reagent in research in many fields that include cancer, neuroscience, and inflammation. The antibodies are available in the form of baculovirus recombinant protein and are extremely sensitive, with picogram-level sensitivity.

Boster Bio MMP7 is a baculovirus that is found to be recombinant in Spodoptera frugiperdaIPLB-SF21AE cells. It is a baculovirus that is recombinant as well as expressing BmCPV polyhedrin under the control of an baculovirus promoter. It was cultured for 10 days at 27 degC and then collected by centrifugation.

It is a recombinant enzyme from the human body

MMP-7 is a Recombinant human protease, which has been discovered to activate pro-MMP-1 and -9, but not MMP-2. MMP-7 is extensively expressed and plays a significant function in ECM remodeling and innate immune system in organs. It is also involved in the activation of signals, cytokines and other functions.

Boster Bio MMP7 marker is an enzyme recombinant from humans that was created from bacteria infected with the Baculovirus. It is produced in a serum-free conditioned medium which is where the enzyme lives in its pro-form. This enzyme is then converted into an active form through incubation with 50 mM 4-aminophenylmercuric acetate, which is available from Sigma.

To determine the MMP activity of Boster Bio MMP7 Marker we first performed an assay using microtiters. We used a microtiter 96-well plate coated with MMPs in 5 mg/mL. Then, we added a 10 mM of Brij35 and GSM192. Then, we measured the fluorescence in each well.

Boster Bio MMP7 Marker is made by the ligation of full-length cDNA clones of the MMP-7 gene into a Baculovirus vector. The MMP-7 protein was then expressed by Sf9 insect cell lines. These cells produced a high amount of protein, and were then cultured in a serum-free insect medium. Finally, we screened the MMP-7 Marker recombinant MMP-7 Marker in a variety of tests to test its efficacy.