Human Recombinant MMP1 protein, His Tag (V2LY-0526-LY5610)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant MMP1 protein, His Tag consist of Amino Acid: 1-469 and predicts a molecular mass of 55 kDa.
Molecule Mass
55 kDa
Verified
HPLC
Sequence
Amino Acid: 1-469
Species
Human

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

Purity
≥95% as determined by SDS-PAGE. ≥95% 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 Tris, Brij35, Arginine
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 1
Function
Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X (PubMed:2557822, PubMed:2153297, PubMed:1645757).

In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity (PubMed:16807369).
Biological Process
Cellular protein metabolic process Source: Reactome
Cellular response to UV-A Source: UniProtKB
Collagen catabolic process Source: GO_Central
Extracellular matrix disassembly Source: Reactome
Extracellular matrix organization Source: GO_Central
Positive regulation of protein-containing complex assembly Source: ParkinsonsUK-UCL
Proteolysis Source: ParkinsonsUK-UCL
Cellular Location
Extracellular matrix
PTM
Undergoes autolytic cleavage to two major forms (22 kDa and 27 kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa form. The 27 kDa form has no activity while the 22/25 kDa form can act as activator for collagenase.
Tyrosine phosphorylated in platelets by PKDCC/VLK.

Bartold, K., Iskierko, Z., Borowicz, P., Noworyta, K., Lin, C. Y., Kalecki, J., ... & Kutner, W. (2022). Molecularly imprinted polymer-based extended-gate field-effect transistor (EG-FET) chemosensor for selective determination of matrix metalloproteinase-1 (MMP-1) protein. Biosensors and Bioelectronics, 208, 114203.

Alwan, I. T., & Ghali, K. H. (2021). Association Risk of Metalomatrix Proteinase Enzymes Levels (MMP-1, MMP-9 And MMP-13) with Development of Rheumatoid Arthritis. Annals of the Romanian Society for Cell Biology, 11369-11378.

Cárcel-Márquez, J., Cullell, N., Muiño, E., Gallego-Fabrega, C., Lledós, M., Ibañez, L., ... & Fernandez-Cadenas, I. (2021). Causal effect of MMP-1 (matrix metalloproteinase-1), MMP-8, and MMP-12 levels on ischemic stroke: a Mendelian randomization study.

Wang, M., Zhou, Y., Huang, W., Zeng, Y., & Li, X. (2020). Association between matrix metalloproteinase-1 (MMP-1) protein level and the risk of rheumatoid arthritis and osteoarthritis: a meta-analysis. Brazilian Journal of Medical and Biological Research, 54, e10366.

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.

Mohammadian, H., Sharifi, R., Amirdehi, S. R., Taheri, E., & Bedoustani, A. B. (2020). Matrix metalloproteinase MMP1 and MMP9 genes expression in breast cancer tissue. Gene Reports, 21, 100906.

Zamolo, G., Grahovac, M., Žauhar, G., Vučinić, D., Kovač, L., Brajenić, N., & Grahovac, B. (2020). Matrix metalloproteinases MMP‐1, MMP‐2, and MMP‐13 are overexpressed in primary nodular melanoma. Journal of cutaneous pathology, 47(2), 139-145.

Chang, Y. T., Chu, L. J., Liu, Y. C., Chen, C. J., Wu, S. F., Chen, C. H., ... & Yu, J. S. (2020). Verification of saliva matrix metalloproteinase-1 as a strong diagnostic marker of oral cavity cancer. Cancers, 12(8), 2273.

Szóstek-Mioduchowska, A., Słowińska, M., Pacewicz, J., Skarzynski, D. J., & Okuda, K. (2020). Matrix metallopeptidase expression and modulation by transforming growth factor-β1 in equine endometrosis. Scientific Reports, 10(1), 1119.

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

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