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AB96555

Recombinant human MMP3 protein (Active)

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(4 Publications)

Recombinant human MMP3 protein (Active) is a Human Full Length protein, in the 101 to 477 aa range, expressed in Escherichia coli, with >98%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, HPLC, WB, FuncS.

View Alternative Names

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

1 Images
Western blot - Recombinant human MMP3 protein (Active) (AB96555)
  • WB

Unknown

Western blot - Recombinant human MMP3 protein (Active) (AB96555)

All lanes:

Anti-MMP3 antibody (<a href='/en-us/products/unavailable/mmp3-antibody-ab18898'>ab18898</a>) at 1 µg/mL

All lanes:

Western blot - Recombinant human MMP3 protein (Active) (ab96555) at 0.1 µg

Secondary

All lanes:

Rabbit polyclonal to Goat IgG - H&L - Pre-Adsorbed (HRP) (ab65486) at 1/3000 dilution

true

Exposure time: 3min

Key facts

Purity

>98% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

Escherichia coli

Tags

Tag free

Applications

HPLC, WB, SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

ab96555 activity was measured by its ability to cleave a chromogenic peptide MMP3 substrate at room temperature.

At a MMP3 concentration of 2.5 μg/ml, 50% cleavage was achieved at an incubation time of approximately 75 minutes.

Accession

P08254

Animal free

No

Carrier free

No

Species

Human

Reconstitution

Reconstitute in water

Storage buffer

Constituents: 0.164% Sodium phosphate, 0.1% 3-[(3-Cholamidopropyl)dimethylammonio]-1-propanesulfonate, 0.002% Ethylenediaminetetraacetic acid, disodium, dihydrate, 0.00111% Calcium chloride

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "HPLC": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>ab96555 can be used as a WB positive control in conjunction with <a href='/en-us/products/unavailable/mmp3-antibody-ab18898'>ab18898</a>.</p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPPDSPETPLVPTEPVPPEPGTPANCDPALSFDAVSTLRGEILIFKDRHFWRKSLRKLEPELHLISSFWPSLPSGVDAAYEVTSKDLVFIFKGNQFWAIRGNEVRAGYPRGIHTLGFPPTVRKIDAAISDKEKNKTYFFVEDKYWRFDEKRNSMEPGFPKQIAEDFPGIDSKIDAVFEEFGFFYFFTGSSQLEFDPNAKKVTHTLKSNSWLNC","proteinLength":"Full Length","predictedMolecularWeight":"42.8 kDa","actualMolecularWeight":null,"aminoAcidEnd":477,"aminoAcidStart":101,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P08254","tags":[]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle|For long term storage it is recommended to add a carrier protein on reconstitution (0.1% HSA or BSA)|Working aliquots stored with a carrier protein are stable for at least 3 months at -20°C to -80°C.
True

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

>=98% HPLC analyses.

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.

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

Publications (4)

Recent publications for all applications. Explore the full list and refine your search

Science advances 9:eadf6537 PubMed37075118

2023

Matrix metalloproteinase-3 (MMP-3)-mediated gene therapy for glaucoma.

Applications

Unspecified application

Species

Unspecified reactive species

Jeffrey O'Callaghan,Conor Delaney,Merissa O'Connor,Joseph van Batenburg-Sherwood,Martin Schicht,Elke Lütjen-Drecoll,Natalie Hudson,Sorcha Ni Dhubhghaill,Peter Humphries,Chris Stanley,Annahita Keravala,Thomas Chalberg,Matthew S Lawrence,Matthew Campbell

Neurobiology of disease 148:105150 PubMed33130223

2020

A new role for matrix metalloproteinase-3 in the NGF metabolic pathway: Proteolysis of mature NGF and sex-specific differences in the continuum of Alzheimer's pathology.

Applications

Unspecified application

Species

Unspecified reactive species

Rowan Pentz,M Florencia Iulita,Maya Mikutra-Cencora,Adriana Ducatenzeiler,David A Bennett,A Claudio Cuello

Oncogene 39:204-218 PubMed31467432

2019

Notch3 promotes prostate cancer-induced bone lesion development via MMP-3.

Applications

Unspecified application

Species

Unspecified reactive species

Sourik S Ganguly,Galen Hostetter,Lin Tang,Sander B Frank,Kathylynn Saboda,Rohit Mehra,Lisha Wang,Xiaohong Li,Evan T Keller,Cindy K Miranti

Human molecular genetics 26:1230-1246 PubMed28158775

2017

Therapeutic potential of AAV-mediated MMP-3 secretion from corneal endothelium in treating glaucoma.

Applications

Unspecified application

Species

Unspecified reactive species

Jeffrey O'Callaghan,Darragh E Crosbie,Paul S Cassidy,Joseph M Sherwood,Cassandra Flügel-Koch,Elke Lütjen-Drecoll,Marian M Humphries,Ester Reina-Torres,Deborah Wallace,Anna-Sophia Kiang,Matthew Campbell,W Daniel Stamer,Darryl R Overby,Colm O'Brien,Lawrence C S Tam,Peter Humphries
View all publications

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