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AB285962

Recombinant Human MMP3 protein

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Recombinant Human MMP3 protein is a Human Full Length protein, expressed in Escherichia coli, with >95%, < 1 EU/µg endotoxin level.

View Alternative Names

STMY1, MMP3, Stromelysin-1, SL-1, Matrix metalloproteinase-3, Transin-1, MMP-3

Key facts

Purity

>95% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

Escherichia coli

Tags

Tag free

Biologically active

No

Accession

P08254

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.4 Constituents: 10.269% Trehalose, 0.727% Dibasic monohydrogen potassium phosphate, 0.248% Potassium phosphate monobasic

storage-buffer

Product details

This product is manufactured by BioVision, an Abcam company and was previously called 7783 MMP-3, human recombinant. 7783-10 is the same size as the 10 μg size of ab285962.

Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"53 kDa","actualMolecularWeight":"19.5 kDa","aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P08254","tags":[]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

MMP3 also known as stromelysin-1 is a member of the matrix metalloproteinase (MMP) family. These proteins are zinc-dependent endopeptidases. MMP3 specifically has a molecular weight of approximately 54 kDa and is responsible for degrading extracellular matrix components such as collagen fibronectin and laminin. MMP3 is expressed in various tissues including fibroblasts chondrocytes and endothelial cells. It plays a significant role in tissue remodeling wound healing and potentially aids in the breakdown of cellular matrices.
Biological function summary

MMP3 contributes to multiple physiological and pathological processes. It supports the remodeling of connective tissues and assists in normal developmental processes. MMP3 can work as part of a complex with other MMP proteins which can enhance or inhibit its activity. The balance of MMPs including MMP3 regulates the extracellular matrix turnover and is important for maintaining tissue homeostasis.

Pathways

MMP3 participates in pathways involved in tissue remodeling and inflammatory responses. It is part of cellular pathways regulated by cytokines like interleukin-1 (IL-1) and tumor necrosis factor-alpha (TNF-alpha). These pathways link MMP3 to other proteins such as MMP1 and MMP9 which perform overlapping and distinct roles in matrix degradation during inflammation and tissue repair.

MMP3 is implicated in conditions like arthritis and cardiovascular diseases. MMP3 contributes to cartilage degradation in rheumatoid arthritis and is associated with the breakdown of vascular structures in atherosclerosis. Proteins like MMP9 and MMP13 often interact with MMP3 in these pathological conditions forming a network that exacerbates tissue damage and disease progression.

Specifications

Form

Lyophilized

Additional notes

>95% by HPLC

General info

Function

Metalloproteinase with a rather broad substrate specificity that can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates different molecules including growth factors, plasminogen or other matrix metalloproteinases such as MMP9 (PubMed : 11029580, PubMed : 1371271). Once released into the extracellular matrix (ECM), the inactive pro-enzyme is activated by the plasmin cascade signaling pathway (PubMed : 2383557). Acts also intracellularly (PubMed : 22265821). For example, in dopaminergic neurons, gets activated by the serine protease HTRA2 upon stress and plays a pivotal role in DA neuronal degeneration by mediating microglial activation and alpha-synuclein/SNCA cleavage (PubMed : 21330369). In addition, plays a role in immune response and possesses antiviral activity against various viruses such as vesicular stomatitis virus, influenza A virus (H1N1) and human herpes virus 1 (PubMed : 35940311). Mechanistically, translocates from the cytoplasm into the cell nucleus upon virus infection to influence NF-kappa-B activities (PubMed : 35940311).

Sequence similarities

Belongs to the peptidase M10A family.

Post-translational modifications

Directly cleaved by HTRA2 to produce active form.

Subcellular localisation

Nucleus

Product protocols

Target data

Metalloproteinase with a rather broad substrate specificity that can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates different molecules including growth factors, plasminogen or other matrix metalloproteinases such as MMP9 (PubMed : 11029580, PubMed : 1371271). Once released into the extracellular matrix (ECM), the inactive pro-enzyme is activated by the plasmin cascade signaling pathway (PubMed : 2383557). Acts also intracellularly (PubMed : 22265821). For example, in dopaminergic neurons, gets activated by the serine protease HTRA2 upon stress and plays a pivotal role in DA neuronal degeneration by mediating microglial activation and alpha-synuclein/SNCA cleavage (PubMed : 21330369). In addition, plays a role in immune response and possesses antiviral activity against various viruses such as vesicular stomatitis virus, influenza A virus (H1N1) and human herpes virus 1 (PubMed : 35940311). Mechanistically, translocates from the cytoplasm into the cell nucleus upon virus infection to influence NF-kappa-B activities (PubMed : 35940311).
See full target information MMP3

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