MMP1 Antibodies
Background
The MMP1 gene encodes matrix metalloproteinase-1, a zinc-dependent protease capable of degrading extracellular matrix components such as collagen. This gene is mainly expressed in connective tissue cells and participates in tissue remodeling and repair processes by decomposing collagen fibers, playing a key role in physiological processes such as wound healing and embryonic development. Research has found that the excessive activation of MMP1 is closely related to pathological conditions such as rheumatoid arthritis and tumor metastasis, and its expression is precisely regulated by cytokines and growth factors. As the first identified member of the matrix metalloproteinase family, the research on MMP1 provides an important model for understanding the mechanism of extracellular matrix degradation, promoting the development process of drugs targeting the matrix metalloproteinase family, especially having significant clinical significance in the field of cancer treatment.
Structure of MMP1
MMP1 is a proteolytic enzyme with a molecular weight of approximately 54 kDa, and its precise molecular weight varies slightly among different species.
| Species | Human | Mouse | Rat | Bovine |
| Molecular Weight (kDa) | 54 | 53.8 | 53.9 | 54.2 |
| Primary Structural Differences | Containing hinge region, the catalytic domain is highly conserved | The substrate binding sites show species specificity | The signal peptide sequences are slightly different | There are variations in the structure of the propeptide |
This enzyme is composed of 469 amino acid residues, and its spatial structure exhibits typical multi-domain characteristics. The core functional region of MMP1 includes the propeptide segment, catalytic domain and heme binding domain. The zinc ion binding site (HEXXHXXGXXH sequence) in the center of its catalytic domain is the key to the enzyme's activity. This structure achieves specific cleavage of the triple helix structure of collagen by the coordinated binding of three histidine residues to zinc ions. The glutamic acid residues located near the active center act as catalytic groups and complete the hydrolysis reaction mediated by water molecules.
Fig. 1 Genomic location and structural characteristics of human MMP1.1
Key structural properties of MMP1:
- Zinc ion-dependent catalytic domains
- Hinge area-mediated substrate recognition module
- Highly conserved HEXXHXXGXXH zinc binding sequence
- Cysteine switch mechanism regulates zymogen activation
Functions of MMP1
The main function of MMP1 is to degrade the extracellular matrix, and it is also involved in various physiological and pathological processes.
| Function | Description |
| Collagen degradation | Specifically hydrolyze the triple helix structure of type I, II and III collagen, initiating the matrix remodeling process. |
| Wound healing | During the repair period, damaged collagen is removed to provide space for new tissues. |
| Embryonic development | Support organ morphogenesis by regulating the stromal environment. |
| Inflammatory regulation | Cut chemokines and cytokine precursors to regulate the recruitment of immune cells. |
| Tumor invasion | Destroy the basement membrane barrier to create a channel for the metastasis of cancer cells. |
The activity of MMP1 shows strict zinc ion dependence. When it forms a 1:1 complex with the tissue inhibitor TIMP-1, it can completely lose its enzymatic activity. This immediate regulatory mechanism ensures its precise spatial control under physiological conditions.
Applications of MMP1 and MMP1 Antibody in Literature
1. Nagasaka, Hirotaka, et al. "MMP1, IL-1β, sTNFR-1, and IL-6 are prognostic factors for patients with unresectable or metastatic renal cell carcinoma treated with immune checkpoint inhibitors." International Journal of Clinical Oncology 29.6 (2024): 832-839. https://doi.org/10.1007/s10147-024-02477-4
This study explored the prognostic factors of immune checkpoint inhibitors in the treatment of renal cell carcinoma and found that MMP1, IL-1β, sTNFR-1 and IL-6 in plasma were significantly associated with patient survival. Among them, MMP1 is an independent predictor of progression-free survival and is associated with the occurrence of serious immune-related adverse events. IL-6 is an independent predictor of overall survival.
2. Zhou, Zhonghan, et al. "A matrix metalloproteinase‐1 polymorphism, MMP1–1607 (1G> 2G), is associated with increased cancer risk: a meta‐analysis including 21,327 patients." Disease markers 2018.1 (2018): 7565834. https://doi.org/10.1155/2018/7565834
This study explored a meta-analysis involving over 20,000 cases, which confirmed that the polymorphism at the -1607 locus (1G>2G) of the MMP1 gene significantly increases the overall risk of multiple cancers. This association holds true in both Asian and white populations, especially in cancer types such as lung cancer, colorectal cancer, and kidney cancer.
3. Dai, Lei, et al. "Comprehensive bioinformatic analysis of MMP1 in hepatocellular carcinoma and establishment of relevant prognostic model." Scientific Reports 12.1 (2022): 13639. https://doi.org/10.1038/s41598-022-17954-x
Studies have shown that the expression of MMP1 is significantly upregulated in hepatocellular carcinoma and is closely related to the poor prognosis of patients. MMP1 not only participates in tumor invasion but also has extensive associations with immune cells and related genes in the tumor immune microenvironment, suggesting that it can serve as a potential prognostic biomarker and indicator of the immune microenvironment status for liver cancer.
4. Wang, Tianyu, et al. "MMP1 and MMP9 are potential prognostic biomarkers and targets for uveal melanoma." BMC cancer 21.1 (2021): 1068. https://doi.org/10.1186/s12885-021-08788-3
Studies have shown that in uveal melanoma, the expression of multiple matrix metalloproteinases such as MMP1 is upregulated. Research has found that the expression of MMP1 is positively correlated with the overall survival and disease-free survival of patients, and plays an important role in the progression of tumors from stage 3 to stage 4, suggesting that it can serve as a potential prognostic biomarker.
5. Muneshige, Kyoko, et al. "Elevation of MMP1 and ADAMTS5 mRNA expression in glenohumeral synovia of patients with hypercholesterolemia." Journal of Orthopaedic Surgery and Research 17.1 (2022): 97. https://doi.org/10.1186/s13018-022-02998-6
This study found that the mRNA expression level of MMP1 was significantly upregulated in the shoulder joint synovium of patients with hypercholesterolemia. This indicates that hypercholesterolemia may affect the shoulder joint environment by altering the metabolism of matrices such as MMP1 and be involved in the pathological process of shoulder diseases.
Creative Biolabs: MMP1 Antibodies for Research
Creative Biolabs specializes in the production of high-quality MMP1 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.
- Custom MMP1 Antibody Development: Tailor-made solutions to meet specific research requirements.
- Bulk Production: Large-scale antibody manufacturing for industry partners.
- Technical Support: Expert consultation for protocol optimization and troubleshooting.
- Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.
For more details on our MMP1 antibodies, custom preparations, or technical support, contact us at email.
Reference
- Dai, Lei, et al. "Comprehensive bioinformatic analysis of MMP1 in hepatocellular carcinoma and establishment of relevant prognostic model." Scientific Reports 12.1 (2022): 13639. https://doi.org/10.1038/s41598-022-17954-x
Anti-MMP1 antibodies
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- AActivation
- AGAgonist
- APApoptosis
- BBlocking
- BABioassay
- BIBioimaging
- CImmunohistochemistry-Frozen Sections
- CIChromatin Immunoprecipitation
- CTCytotoxicity
- CSCostimulation
- DDepletion
- DBDot Blot
- EELISA
- ECELISA(Cap)
- EDELISA(Det)
- ESELISpot
- EMElectron Microscopy
- FFlow Cytometry
- FNFunction Assay
- GSGel Supershift
- IInhibition
- IAEnzyme Immunoassay
- ICImmunocytochemistry
- IDImmunodiffusion
- IEImmunoelectrophoresis
- IFImmunofluorescence
- IGImmunochromatography
- IHImmunohistochemistry
- IMImmunomicroscopy
- IOImmunoassay
- IPImmunoprecipitation
- ISIntracellular Staining for Flow Cytometry
- LALuminex Assay
- LFLateral Flow Immunoassay
- MMicroarray
- MCMass Cytometry/CyTOF
- MDMeDIP
- MSElectrophoretic Mobility Shift Assay
- NNeutralization
- PImmunohistologyp-Paraffin Sections
- PAPeptide Array
- PEPeptide ELISA
- PLProximity Ligation Assay
- RRadioimmunoassay
- SStimulation
- SESandwich ELISA
- SHIn situ hybridization
- TCTissue Culture
- WBWestern Blot




