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Mouse Anti-MMP3 Recombinant Antibody (CBT2825) (V2LY-0625-LY2718)

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Tested Data

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBT2825
Antibody Isotype
IgG1
Application
FC

Basic Information

Immunogen
Purified recombinant fragment of human MMP3 expressed in E. Coli.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal Antibody
Application Notes
ApplicationNote
WB1:500-1:2,000
FC1:200-1:400
ELISA1:10,000

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

Format
Liquid
Buffer
PBS
Preservative
Sodium azide
Concentration
Batch dependent
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Entrez Gene ID
UniProt ID
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.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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