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SAE0077

Sigma-Aldrich

MMP-9 human

recombinant, ≥1,300 pmol/min/μg, expressed in HEK 293 cells

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Synonym(s):
GELBCLG4B, Gelatinase, Gelatinase B, MANDP2, MMP-9, Matrix Metalloproteinase-9, Type IV collagenase
Enzyme Commission number:
NACRES:
NA.32

biological source

human

Quality Level

recombinant

expressed in HEK 293 cells

Assay

95% (SDS-PAGE)

form

liquid

mol wt

calculated mol wt 76 kDa
observed mol wt 92 kDa (The protein migrates as a 92 kDa protein on SDS-PAGE due to glycosylation)

concentration

30-120 μg/mL (50 μg protein, determined by Bradford. For the lot-specific concentration, see Certificate of Analysis.)

UniProt accession no.

application(s)

cell analysis

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... MMP(4318)

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This Item
SAE0174SAE0078SRP6271
MMP-9 human recombinant, ≥1,300 pmol/min/μg, expressed in HEK 293 cells

Sigma-Aldrich

SAE0077

MMP-9 human

MMP-2 human recombinant, ≥1,000 pmol/min/μg, expressed in HEK 293 cells

Sigma-Aldrich

SAE0174

MMP-2 human

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

Sigma-Aldrich

SRP6271

MMP-9 human

recombinant

expressed in HEK 293 cells

recombinant

expressed in HEK 293 cells

recombinant

expressed in HEK 293 cells

recombinant

expressed in HEK 293 cells

assay

95% (SDS-PAGE)

assay

-

assay

≥95% (SDS-PAGE)

assay

≥95% (SDS-PAGE)

form

liquid

form

-

form

liquid

form

lyophilized powder

mol wt

calculated mol wt 76 kDa, observed mol wt 92 kDa (The protein migrates as a 92 kDa protein on SDS-PAGE due to glycosylation)

mol wt

-

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

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.)

concentration

30-120 μg/mL (50 μg protein, determined by Bradford. For the lot-specific concentration, see Certificate of Analysis.)

concentration

-

concentration

30-120 μg/mL (50 μg protein, determined by Bradford. The protein concentration is 30-120 μg/ml. for the lot-specific concentration, see Certificate of Analysis.)

concentration

-

General description

Recombinant human Matrix Metalloproteinase-9 (MMP-9) is expressed in human HEK 293 cells as a glycoprotein with a calculated molecular mass of 76 kDa (amino acids 20-707). The DTT-reduced protein migrates as a ~92 kDa polypeptide on SDS-PAGE due to glycosylation. This protein is manufactured in human cells, with no serum. The human cells expression system allows human-like glycosylation and folding, and often supports higher specific activity of the protein. The protein is produced with no artificial tags.

Biochem/physiol Actions

MMP-9 is a member of the matrix metalloproteinase (MMP) family of proteins. Proteins of the MMP family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Studies in rhesus monkeys suggest that MMP9 is involved in IL-8 (interleukin-8)-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. Thrombospondins, intervertebral disc proteins, regulate the effective levels of MMP-2 and -9, which are key effectors of extracellular matrix (ECM) remodeling. MMP-9 degrades various substrates including gelatin, collagen types IV and V, and elastin. MMP-9 is involved in a variety of autoimmune diseases such as systemic lupus erythematosus, rheumatoid arthritis, and multiple sclerosis, and be regarded as a potential therapeutic target.
MMP-9 is secreted from neutrophils, macrophages, and a number of transformed cells, and is the most complex family member in terms of domain structure and regulation of its activity.
Structurally, MMP9 maybe be divided into five distinct domains: a pro-domain which is cleaved upon activation, a gelatin binding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a proline rich linker region, and a carboxyl terminal hemopexin like domain.

Other Notes

This product can be activated in vitro by adding 4-Aminophenylmercuric acetate (APMA), Cat. No. A9563, to a final concentration of 1 mM.

Physical form

Liquid solution, 0.22 mm filtered, containing 25 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% Brij-35

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Tamara Filipović et al.
BioMed research international, 2020, 9758289-9758289 (2020-02-20)
Osteoporosis is a disease characterized by decreased bone density and destruction of bone microarchitecture. Indicators for altered bone homeostasis are changes in the serum level of matrix metalloproteinases (MMPs) and their tissue inhibitors (TIMPs). The purpose of the current study

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