Human Recombinant MMP3 protein (V2LY-0526-LY5617)

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Basic Information

Expressed Host
E. coli
Protein Species
Human
Protein Construction
This product is Human Recombinant MMP3 protein consist of Amino Acid: 18-272 and predicts a molecular mass of 29 kDa.
Molecule Mass
29 kDa
Verified
HPLC
Sequence
Amino Acid: 18-272
Species
Human

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

Purity
≥90% as determined by SDS-PAGE. ≥90% as determined by SEC-HPLC.
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Matrix Metallopeptidase 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.

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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