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Mouse Anti-MMP3 Recombinant Antibody (CBFYM-0687) (CBMAB-M0823-FY)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYM-0687
Antibody Isotype
IgG2a
Application
ELISA, IHC

Basic Information

Specificity
Human
Antibody Isotype
IgG2a
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.2
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Matrix Metallopeptidase 3
Introduction
Proteins of the matrix metalloproteinase family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This gene encodes an enzyme which degrades fibronectin, laminin, collagens III, IV, IX, and X, and cartilage proteoglycans. The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.
Entrez Gene ID
4314
UniProt ID
P08254
Alternative Names
Matrix Metallopeptidase 3; Matrix Metalloproteinase 3 (Stromelysin 1, Progelatinase); EC 3.4.24.17; Transin-1; STMY1; MMP-3; SL-1; Matrix Metalloproteinase-3
Function
Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase.
Biological Process
Cellular response to nitric oxide Source: ParkinsonsUK-UCL
Cellular response to UV-A Source: UniProtKB
Collagen catabolic process Source: GO_Central
Extracellular matrix disassembly Source: Reactome
Extracellular matrix organization Source: GO_Central
Negative regulation of hydrogen peroxide metabolic process Source: ParkinsonsUK-UCL
Positive regulation of oxidative stress-induced cell death Source: ParkinsonsUK-UCL
Positive regulation of protein-containing complex assembly Source: ParkinsonsUK-UCL
Proteolysis Source: UniProtKB
Regulation of neuroinflammatory response Source: ARUK-UCL
Response to amyloid-beta Source: ARUK-UCL
Cellular Location
Extracellular matrix
Involvement in disease
Coronary heart disease 6 (CHDS6):
A multifactorial disease characterized by an imbalance between myocardial functional requirements and the capacity of the coronary vessels to supply sufficient blood flow. Decreased capacity of the coronary vessels is often associated with thickening and loss of elasticity of the coronary arteries.
More Infomation

Jehan, F., Zarka, M., de la Houssaye, G., Veziers, J., Ostertag, A., Cohen‐Solal, M., & Geoffroy, V. (2022). New insights into the role of matrix metalloproteinase 3 (MMP3) in bone. FASEB BioAdvances, 4(8), 524.

Kageyama, Y., Nakamura, M., Igari, Y., Yamaguchi, S., Oguchi, A., Murakawa, Y., ... & Sasano, Y. (2022). Expression of matrix metalloproteinase‐3 and‐10 is up‐regulated in the periodontal tissues of aged mice. Journal of Periodontal Research, 57(4), 733-741.

Wan, J., Zhang, G., Li, X., Qiu, X., Ouyang, J., Dai, J., & Min, S. (2021). Matrix metalloproteinase 3: a promoting and destabilizing factor in the pathogenesis of disease and cell differentiation. Frontiers in Physiology, 12, 663978.

Shi, S., Su, M., Shen, G., Hu, Y., Yi, F., Zeng, Z., ... & Xie, X. (2021). Matrix metalloproteinase 3 as a valuable marker for patients with COVID‐19. Journal of medical virology, 93(1), 528-532.

Suhaimi, S. A., Chan, S. C., & Rosli, R. (2020). Matrix metallopeptidase 3 polymorphisms: Emerging genetic markers in human breast cancer metastasis. Journal of breast cancer, 23(1), 1-9.

Balkhi, S., Mashayekhi, F., Salehzadeh, A., & Saedi, H. S. (2020). Matrix metalloproteinase (MMP)-1 and MMP-3 gene variations affect MMP-1 and-3 serum concentration and associates with breast cancer. Molecular Biology Reports, 47(12), 9637-9644.

Manka, S. W., Bihan, D., & Farndale, R. W. (2019). Structural studies of the MMP-3 interaction with triple-helical collagen introduce new roles for the enzyme in tissue remodelling. Scientific reports, 9(1), 18785.

Lee, J. M., Kronbichler, A., Park, S. J., Kim, S. H., Han, K. H., Kang, H. G., ... & Shin, J. I. (2019). Association between serum matrix metalloproteinase-(MMP-) 3 levels and systemic lupus erythematosus: a meta-analysis. Disease markers, 2019.

Lech, A. M., Wiera, G., & Mozrzymas, J. W. (2019). Matrix metalloproteinase-3 in brain physiology and neurodegeneration. Advances in Clinical and Experimental Medicine, 28(12), 1717-1722.

Mirastschijski, U., Lupše, B., Maedler, K., Sarma, B., Radtke, A., Belge, G., ... & Ågren, M. S. (2019). Matrix metalloproteinase-3 is key effector of TNF-α-induced collagen degradation in skin. International journal of molecular sciences, 20(20), 5234.

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For research use only. Not intended for any clinical use.

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