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Rabbit Anti-MMP1 Recombinant Antibody (E9S9N) (CBMAB-CP1564-LY)


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Summary

Host Animal
Rabbit
Specificity
Human
Clone
E9S9N
Antibody Isotype
IgG
Application
WB, IP

Basic Information

Immunogen
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val267 of human MMP-1 protein.
Specificity
Human
Antibody Isotype
IgG
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
100 µg/ml BSA, 50% glycerol
Preservative
0.02% sodium azide
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

Full Name
Matrix Metallopeptidase 1
Introduction
This gene encodes a member of the peptidase M10 family of matrix metalloproteinases (MMPs). Proteins in this 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. The encoded preproprotein is proteolytically processed to generate the mature protease. This secreted protease breaks down the interstitial collagens, including types I, II, and III. The gene is part of a cluster of MMP genes on chromosome 11. Mutations in this gene are associated with chronic obstructive pulmonary disease (COPD). Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that is proteolytically processed. [provided by RefSeq, Jan 2016]
Entrez Gene ID
4312
UniProt ID
P03956
Alternative Names
Matrix Metallopeptidase 1; Interstitial Collagenase; Fibroblast Collagenase; EC 3.4.24.7; CLG; Matrix Metalloproteinase 1 (Interstitial Collagenase); Matrix Metallopeptidase 1 (Interstitial Collagenase);
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.
More Infomation

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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