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PF024

Sigma-Aldrich

MMP-9, Active, Human, Recombinant

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Synonym(s):
Gelatinase B, 83 kDa Gelatinase, Matrix Metalloproteinase 9, Matrix Metalloproteinase 9, Gelatinase B, 83 kDa Gelatinase
Enzyme Commission number:

assay

≥90% (SDS-PAGE)

Quality Level

form

liquid

specific activity

≥8.0 ΔA405/h-μg protein (thiopeptide hydrolysis assay)

does not contain

preservative

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
avoid repeated freeze/thaw cycles

shipped in

wet ice

storage temp.

−70°C

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SAE0078SAE0077M8945
Sigma-Aldrich

PF024

MMP-9, Active, Human, Recombinant

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

SAE0078

MMP-9 pre-activated human

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

SAE0077

MMP-9 human

Sigma-Aldrich

M8945

Matrix Metalloproteinase-9 human

specific activity

≥8.0 ΔA405/h-μg protein (thiopeptide hydrolysis assay)

specific activity

-

specific activity

-

specific activity

-

form

liquid

form

liquid

form

liquid

form

buffered aqueous solution

shipped in

wet ice

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

storage temp.

−70°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−70°C

storage condition

OK to freeze, avoid repeated freeze/thaw cycles

storage condition

-

storage condition

-

storage condition

-

General description

Recombinant, human MMP-9 purified from transfected mammalian cells and activated with APMA. Active MMP-9 enzyme is APMA-free.
Recombinant, human MMP-9 purified from transfected mammalian cells and activated with APMA. Active MMP-9 enzyme is APMA-free. Supplied as the ~83 kDa active enzyme. The proenzyme form of MMP-9 was purified from transfected mammalian cells and activated using the organomercurial compound, 4-aminophenyl mercuric acetate (APMA). APMA is removed through a desalting column. The substrate specificity for MMP-9 is collagen (types IV, V, VII, and X), elastin, and gelatin (type I). Useful for immunoblotting, substrate cleavage, and zymography. Titration is recommended for optimal results in individual systems. Matrix metalloproteinases are members of a unique family of proteolytic enzymes that have a zinc ion at their active sites and can degrade collagens, elastin and other components of the extracellular matrix (ECM). These enzymes are present in normal healthy individuals and have been shown to have an important role in processes such as wound healing, pregnancy, and bone resorption. However, overexpression and activation of MMPs have been linked with a range of pathological processes and disease states involved in the breakdown and remodeling of the ECM. Such diseases include tumor invasion and metastasis, rheumatoid arthritis, periodontal disease, and vascular processes such as angiogenesis, intimal hyperplasia, atherosclerosis, and aneurysms. Recently, MMPs have been linked to neurodegenerative diseases such as Alzheimer′s, and amyotrophic lateral sclerosis (ALS). Natural inhibitors of MMPs, tissue inhibitor of matrix metalloproteinases (TIMPs) exist and synthetic inhibitors have been developed which offer hope of new treatment options for these diseases.



Regulation of MMP activity can occur at the level of gene expression, including transcription and translation, level of activation, or at the level of inhibition by TIMPs. Thus, perturbations at any of these points can theoretically lead to alterations in ECM turnover. Expression is under tight control by pro- and anti-inflammatory cytokines and/or growth factors and, once produced the enzymes are usually secreted as inactive zymograms. Upon activation (removal of the inhibitory propeptide region of the molecules) MMPs are subject to control by locally produced TIMPs. All MMPs can be activated in vitro with organomercurial compounds (e.g. 4-aminophenylmercuric acetate), but the agents responsible for the physiological activation of all MMPs have not been clearly defined. Numerous studies indicate that members of the MMP family have the ability to activate one another. The activation of the MMPs in vivo is likely to be a critical step in terms of their biological behavior, because it is this activation that will tip the balance in favor of ECM degradation. The hallmark of diseases involving MMPs appear to be stoichiometric imbalance between active MMPs and TIMPs, leading to excessive tissue disruption and often degradation. Determination of the mechanisms that control this imbalance may open up some important therapeutic options of specific enzyme inhibitors.

Packaging

Please refer to vial label for lot-specific concentration.

Warning

Toxicity: Standard Handling (A)

Physical form

In 50 mM HEPES, 10 mM CaCl₂, 20% glycerol, 0.005% BRIJ®-35 Detergent, pH 7.5.

Reconstitution

Following initial use, aliquot into siliconized vials and freeze (-70°C).

Other Notes

Parsons, S.L., et al. 1997. Br. J. Surg.84, 160.
Backstrom, J.R., et al. 1996. J. Neuro.16, 7910.
Lim, G.P., et al. 1996. J. Neurochem.67, 251.
Xia, T., et al. 1996. Biochim. Biophys. Acta1293, 259.
Sang, Q.X., et al. 1995. Biochim. Biophys. Acta1251, 99.
Zempo, N., et al. 1994. J. Vasc. Surg.20, 217.
Birkedal-Hansen, H. 1993. J. Periodontol.64, 484.
Stetler-Stevenson, W.G., et al. 1993. FASEB J.7, 1434.
Jeffrey, J.J. 1991. Semin. Perinatol.15, 118.
Liotta, L.A., et al. 1991. Cell64, 327.
Harris, E. 1990. N. Engl. J. Med.322, 1277.

Legal Information

Brij is a registered trademark of Croda International PLC
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Frontiers in aging neuroscience, 12, 92-92 (2020-04-23)
Despite the extensive use of hormonal methods as either contraception or menopausal hormone therapy (HT), there is very little known about the potential effects of these compounds on the cellular processes of the brain. Medroxyprogesterone Acetate (MPA) is a progestogen
Kyle J Isaacson et al.
Journal of drug targeting, 28(7-8), 766-779 (2020-04-21)
Silk-elastinlike protein polymers (SELPs) self-assemble into nanostructures when designed with appropriate silk-to-elastin ratios. Here, we investigate the effect of insertion of a matrix metalloproteinase-responsive peptide sequence, GPQGIFGQ, into various locations within the SELP backbone on supramolecular self-assembly. Insertion of the
Rupak Mukherjee et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 24(10), 3819-3828 (2010-06-10)
Radiofrequency (RF) ablation of the myocardium causes discrete sites of injury. RF scars can expand, altering the extracellular matrix (ECM) structure and the continuity of the electrical syncytium of the adjacent myocardium. Matrix metalloproteinases (MMPs), such as MMP-9, contribute to
Gae-Baik Kim et al.
International journal of molecular sciences, 23(3) (2022-02-16)
Activity-based monitoring of cell-secreted proteases has gained significant interest due to the implication of these substances in diverse cellular functions. Here, we demonstrated a cell-based method of monitoring protease activity using fluorescent cell-permeable peptides. The activatable peptide consists of anionic
Arek Szklarczyk et al.
Journal of neurochemistry, 102(4), 1256-1263 (2007-05-03)
Matrix metalloproteinases (MMPs) belong to a family of zinc dependent enzymes best studied for their role in cancer and inflammation. Though MMPs typically target extracellular proteins, here we show that MMP-7, an MMP family member which lacks a C-terminal hemopexin-like

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