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AB81550

Recombinant human MMP2 protein (Active)

5

(1 Review)

|

(10 Publications)

Recombinant human MMP2 protein (Active) is a Human Full Length protein, in the 109 to 660 aa range, expressed in Escherichia coli, with >98%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, HPLC, FuncS.

View Alternative Names

CLG4A, MMP2, 72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, TBE-1, MMP-2

Key facts

Purity

>98% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

Escherichia coli

Tags

Tag free

Applications

HPLC, SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

MMP2 activity was measured by its ability to cleave a chromogenic peptide MMP2 substrate at room temperature.

At an MMP2 concentration of 2.5 μg/ml, 50% cleavage was achieved at an incubation time of approximately 25 minutes.

Accession

P08253

Animal free

No

Carrier free

No

Species

Human

Reconstitution

reconstitute with water at 0.1mg/mL

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>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC","proteinLength":"Full Length","predictedMolecularWeight":"62 kDa","actualMolecularWeight":null,"aminoAcidEnd":660,"aminoAcidStart":109,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P08253","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
True

Supplementary information

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

The MMP-2 protein also known as matrix metalloproteinase-2 or gelatinase A is an enzyme involved in the breakdown of extracellular matrix components. It plays a critical role in tissue remodeling and cell migration. Comprised of a molecular weight of approximately 72 kDa this metalloproteinase is secreted as an inactive proenzyme that requires activation. MMP2 is expressed in various tissues including the brain heart and blood vessels where it contributes to normal physiological processes and pathological conditions.
Biological function summary

Matrix metalloproteinase-2 is mainly involved in the degradation of type IV and V collagens gelatin and fibronectin. As part of the metalloproteinase family it works alongside other MMPs to maintain tissue homeostasis and repair. MMP-2 forms part of a complex network that ensures the timely degradation of matrix components balancing synthesis and breakdown. It remains regulated by tissue inhibitors of metalloproteinases (TIMPs) preventing excessive degradation that could lead to tissue damage.

Pathways

MMP-2 plays a significant role within the extracellular matrix (ECM) remodeling and angiogenesis pathways. It interacts with various proteins including integrins and TIMP-2 to modulate cellular behaviors such as migration and invasion. MMP-2 contributes to processes like wound healing and embryonic development through its involvement in ECM degradation and new tissue formation.

Matrix metalloproteinase-2 is linked to cancer progression and cardiovascular diseases. In cancer abnormal MMP-2 activity facilitates tumor invasion and metastasis by breaking down matrix barriers. Increased MMP-2 expression associates with poor prognosis in cancers like breast and prostate. In cardiovascular diseases such as atherosclerosis it contributes to plaque destabilization and vascular remodeling. The imbalance in MMP-2 activity and its regulation by proteins like TIMP-1 are involved in the pathology of these disorders.

Specifications

Form

Lyophilized

Additional notes

>= 98% HPLC.

General info

Function

Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14.. PEX, the C-terminal non-catalytic fragment of MMP2, possesses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels.. Isoform 2. Mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways.

Sequence similarities

Belongs to the peptidase M10A family.

Post-translational modifications

Phosphorylation on multiple sites modulates enzymatic activity. Phosphorylated by PKC in vitro.. The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-MMP3). Autocatalytic cleavage in the C-terminal produces the anti-angiogenic peptide, PEX. This processing appears to be facilitated by binding integrinv/beta3.

Subcellular localisation

Mitochondrion

Product protocols

Target data

Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14.. PEX, the C-terminal non-catalytic fragment of MMP2, possesses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels.. Isoform 2. Mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways.
See full target information MMP2

Publications (10)

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

Scientific reports 13:19227 PubMed37932474

2023

Human amniotic membrane inhibits migration and invasion of muscle-invasive bladder cancer urothelial cells by downregulating the FAK/PI3K/Akt/mTOR signalling pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Aleksandar Janev,Taja Železnik Ramuta,Urška Dragin Jerman,Hristina Obradović,Urška Kamenšek,Maja Čemažar,Mateja Erdani Kreft

Frontiers in pharmacology 14:1215694 PubMed37492088

2023

Optimizing the enzymatic release of MMAE from DGR-based small molecule drug conjugate by incorporation of a GPLG-PABC enzymatically cleavable linker.

Applications

Unspecified application

Species

Unspecified reactive species

Marco Zambra,Ivan Ranđelović,Francesco Talarico,Adina Borbély,Laura Svajda,József Tóvári,Gábor Mező,Lizeth Bodero,Sveva Colombo,Federico Arrigoni,Elettra Fasola,Silvia Gazzola,Umberto Piarulli

Science advances 9:eabq8225 PubMed36857458

2023

A bispecific glycopeptide spatiotemporally regulates tumor microenvironment for inhibiting bladder cancer recurrence.

Applications

Unspecified application

Species

Unspecified reactive species

Hong-Wei An,Da-Yong Hou,Jia Yang,Zi-Qi Wang,Man-Di Wang,Rui Zheng,Ni-Yuan Zhang,Xing-Jie Hu,Zhi-Jia Wang,Lu Wang,Di Liu,Jun-Feng Hao,Wanhai Xu,Yuliang Zhao,Hao Wang

BMC cancer 22:1335 PubMed36539774

2022

Interactions of the chemokines CXCL11 and CXCL12 in human tumor cells.

Applications

Unspecified application

Species

Unspecified reactive species

Christian Koch,Nina Charlotte Fischer,Malte Puchert,Jürgen Engele

Scientific reports 12:14462 PubMed36002564

2022

Investigation of the long-term healing response of the liver to boiling histotripsy treatment in vivo.

Applications

Unspecified application

Species

Unspecified reactive species

Jeongmin Heo,Chanmin Joung,Kisoo Pahk,Ki Joo Pahk

International journal of molecular sciences 22: PubMed34070317

2021

Attachment of Cancer Urothelial Cells to the Bladder Epithelium Occurs on Uroplakin-Negative Cells and Is Mediated by Desmosomal and Not by Classical Cadherins.

Applications

Unspecified application

Species

Unspecified reactive species

Urška Dragin Jerman,Tanja Višnjar,Iva Hafner Bratkovič,Nataša Resnik,Mojca Pavlin,Peter Veranič,Mateja Erdani Kreft

Scientific reports 9:4340 PubMed30867536

2019

Identification of fibrinogen as a natural inhibitor of MMP-2.

Applications

Unspecified application

Species

Unspecified reactive species

Hassan Sarker,Eugenio Hardy,Ayman Haimour,Walter P Maksymowych,Lorenzo D Botto,Carlos Fernandez-Patron

International journal of molecular sciences 19: PubMed29463024

2018

Overexpression of the Vitronectin V10 Subunit in Patients with Nonalcoholic Steatohepatitis: Implications for Noninvasive Diagnosis of NASH.

Applications

Unspecified application

Species

Unspecified reactive species

Maria Del Ben,Diletta Overi,Licia Polimeni,Guido Carpino,Giancarlo Labbadia,Francesco Baratta,Daniele Pastori,Valeria Noce,Eugenio Gaudio,Francesco Angelico,Carmine Mancone

Mediators of inflammation 2017:9524594 PubMed29097850

2017

Middermal Elastolysis: Dermal Fibroblasts Cooperate with Inflammatory Cells to the Elastolytic Disorder.

Applications

Unspecified application

Species

Unspecified reactive species

Giovanna De Cunto,Arianna Lamberti,Maria Margherita de Santi,Clelia Miracco,Michele Fimiani,Giuseppe Lungarella,Eleonora Cavarra

Biochimica et biophysica acta. Molecular basis of 1863:2808-2820 PubMed28712835

2017

Biological impact of advanced glycation endproducts on estrogen receptor-positive MCF-7 breast cancer cells.

Applications

Unspecified application

Species

Unspecified reactive species

Sabine Matou-Nasri,Hana Sharaf,Qiuyu Wang,Nasser Almobadel,Zaki Rabhan,Hamad Al-Eidi,Wesam Bin Yahya,Thadeo Trivilegio,Rizwan Ali,Nasser Al-Shanti,Nessar Ahmed
View all publications

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