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SRP7783

Sigma-Aldrich

MMP-3 human

recombinant, expressed in E. coli, ≥95% (SDS-PAGE), ≥95% (HPLC)

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Synonym(s):
EC 3, Matrix metalloproteinase-3, Stromelysin-1
CAS Number:
MDL number:
NACRES:
NA.32

biological source

human

recombinant

expressed in E. coli

assay

≥95% (HPLC)
≥95% (SDS-PAGE)

form

lyophilized

mol wt

~19.5 kDa

packaging

pkg of 10 μg

technique(s)

western blot (chemiluminescent): suitable

impurities

endotoxin, tested

NCBI accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... MMP3(4314)

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This Item
SRP6271SAE0078444217
Sigma-Aldrich

SRP7783

MMP-3 human

MMP-9 human recombinant, expressed in HEK 293 cells, ≥95% (SDS-PAGE)

SRP6271

MMP-9 human

MMP-9 pre-activated human recombinant, ≥1,300 pmol/min/μg, expressed in HEK 293 cells

SAE0078

MMP-9 pre-activated human

assay

≥95% (HPLC), ≥95% (SDS-PAGE)

assay

≥95% (SDS-PAGE)

assay

≥95% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

technique(s)

western blot (chemiluminescent): suitable

technique(s)

-

technique(s)

-

technique(s)

-

recombinant

expressed in E. coli

recombinant

expressed in HEK 293 cells

recombinant

expressed in HEK 293 cells

recombinant

-

mol wt

~19.5 kDa

mol wt

calculated mol wt 50.8 kDa, observed mol wt 55-65 kDa (DTT-reduced. Protein migrates due to different glycosylation. Ala 20 is the predicted N-terminus.)

mol wt

calculated mol wt 66 kDa, observed mol wt 82 kDa by SDS-PAGE (The protein migrates as a 82 kDa protein on SDS-PAGE due to glycosylation)

mol wt

-

form

lyophilized

form

lyophilized powder

form

liquid

form

liquid

General description

Active MMP-3 catalytic domain from human cDNA, expressed in E. coli and purified using proprietary technologies. The active MMP-3 is very useful in studying enzyme kinetics, cleave target substrates, and screen for inhibitors.
The gene JE is an early growth response gene that was first identified in mouse 3T3 cells. The gene is mapped to mouse chromosome 11. It encodes a member of the CC subfamily, the members of which contain characteristic two adjacent cysteine residues.

Application

MCP-1 has been used to induce chemotaxis in mice macrophages.
MMP-3 human has been used to develop a simple and sensitive electrogenerated chemiluminescence (electrochemiluminescence (ECL)) peptide-based bioassay for the detection of matrix metalloproteinases releasing from living cells.

Biochem/physiol Actions

Matrix metallopeptidase 3 (MMP3) has a broad substrate specificity and is capable of degrading fibronectin, laminin, collagens III, IV, IX, and X, and cartilage proteoglycans. It participates in wound repair, progression of atherosclerosis, tissue remodeling and tumor initiation. MMP3 variants can be associated with hypertrophy of interventricular septum or hypertrophic cardiomyopathy.
The gene JE, also referred to as MCP-1 (monocyte chemoattractant protein-1), encodes a secreted chemokine that functions as a chemoattractant for monocytes and may activate their anti-tumor properties. This protein may serve as a potential therapeutic anticancer agent.

Physical form

Lyophilized powder.

Reconstitution

Centrifuge the vial prior to opening. Avoid freeze-thaw cycles.
Reconstitute in sterile PBS to a concentration of 0.1-1.0 mg/mL. This solution can then be diluted into other aqueous buffers.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Customers Also Viewed

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Simple and sensitive electrogenerated chemiluminescence peptide-based biosensor for detection of matrix metalloproteinase 2 released from living cells
Dang Q, et al.
Analytical and Bioanalytical Chemistry, 408(25), 7067-7075 (2016)
Rowan Pentz et al.
Neurobiology of disease, 148, 105150-105150 (2020-11-02)
Matrix metalloproteinase-3 (MMP-3) has been associated with risk of Alzheimer's disease (AD). In this study we introduce a novel role for MMP-3 in degrading nerve growth factor (NGF) in vivo and examine its mRNA and protein expression across the continuum
Grzegorz Wiera et al.
Cellular and molecular life sciences : CMLS, 78(5), 2279-2298 (2020-09-23)
Learning and memory are known to depend on synaptic plasticity. Whereas the involvement of plastic changes at excitatory synapses is well established, plasticity mechanisms at inhibitory synapses only start to be discovered. Extracellular proteolysis is known to be a key
E V Privalova et al.
Kardiologiia, 54(5), 4-7 (2014-09-02)
Prognosis of patients with hypertrophic cardiomyopathy (HCMP) to a great extent is determined by clinical variant of the disease. As the system of matrix metalloproteinases (MMPs) plays an important role in development and progression of the processes of fibroformation and
Suppression of tumor formation in vivo by expression of the JE gene in malignant cells.
Rollins BJ and Sunday ME
Molecular and Cellular Biology, 11, 3125-3131 (1991)

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