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M2699

Sigma-Aldrich

Marimastat

≥98% (HPLC), solid, MMP inhibitor

Sinonimo/i:

BB2516, (2S,3R)-N4-[(1S)-2,2-Dimethyl-1-[(methylamino)carbonyl] propyl]-N1,2-dihydroxy-3-(2-methylpropyl)butanediamide

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CHF 211.00
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CHF 933.00

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5 MG
CHF 211.00
25 MG
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About This Item

Formula empirica (notazione di Hill):
C15H29N3O5
Numero CAS:
154039-60-8
Peso molecolare:
331.41
Numero MDL:
MFCD00866242
Codice UNSPSC:
12352200
ID PubChem:
329817950
NACRES:
NA.77

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Nome del prodotto

Marimastat, ≥98% (HPLC)

Livello qualitativo

100

Saggio

≥98% (HPLC)

Stato

solid

Solubilità

DMSO: ≥20 mg/mL

Condizioni di spedizione

wet ice

Temperatura di conservazione

−20°C

Stringa SMILE

CNC(=O)[C@@H](NC(=O)[C@H](CC(C)C)[C@H](O)C(=O)NO)C(C)(C)C

InChI

1S/C15H29N3O5/c1-8(2)7-9(10(19)13(21)18-23)12(20)17-11(14(22)16-6)15(3,4)5/h8-11,19,23H,7H2,1-6H3,(H,16,22)(H,17,20)(H,18,21)/t9-,10+,11-/m1/s1
OCSMOTCMPXTDND-OUAUKWLOSA-N

Informazioni sul gene

Applicazioni

Marimastat has been used as an inhibitor of:
  • metalloproteinase 2/9 (MMP2/9), to study its effects on exercise-mediated interleukin-6 (IL-6) release in mice[1]
  • metalloproteinase, to determine protease activity in Pseudomonas aeruginosa cultures[2]
  • metalloproteinase 10 (MMP10), to study its effect on monoclonal antibody H3 binding to MMP10[3]

Azioni biochim/fisiol

Marimastat is a broad spectrum matrix metalloprotease (MMP) inhibitor

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

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Certificati d'analisi (COA)

Lot/Batch Number
0000394101
0000333793
0000333793
0000394101
0000237518

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MMP-13 Substrate, Fluorogenic A quenched fluorescence substrate for MMP-13 (collagenase-3; kcat/Km = 1.09 x 10⁶ M⁻¹s⁻¹).

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D-(−)-Ribose suitable for cell culture, BioReagent

Sigma-Aldrich

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TAPI-0 ≥95% (HPLC)

Sigma-Aldrich

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Varespladib ≥98% (HPLC)

Sigma-Aldrich

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Varespladib

Amir S Razai et al.
The Journal of biological chemistry, 295(8), 2464-2472 (2020-01-19)
Since their discovery, the matrix metalloproteinase (MMP) family proteases have been considered as therapeutic targets in numerous diseases and disorders. Unfortunately, clinical trials with MMP inhibitors have failed to yield any clinical benefits of these inhibitors. These failures were largely
Stefanie K Menzies et al.
Toxicon: X, 14, 100118-100118 (2022-03-25)
Snakebite envenoming affects more than 250,000 people annually in sub-Saharan Africa. Envenoming by Dispholidus typus (boomslang) results in venom-induced consumption coagulopathy (VICC), whereby highly abundant prothrombin-activating snake venom metalloproteinases (SVMPs) consume clotting factors and deplete fibrinogen. The only available treatment
Nicholas J Youngman et al.
Molecules (Basel, Switzerland), 27(5) (2022-03-11)
Snakebite remains a significant public health burden globally, disproportionately affecting low-income and impoverished regions of the world. Recently, researchers have begun to focus on the use of small-molecule inhibitors as potential candidates for the neutralisation of key snake venom toxins
Timothy W Failes et al.
Journal of inorganic biochemistry, 101(3), 396-403 (2007-01-02)
Fe(III)-salen (N,N-bis(salicylidene)-ethane-1,2-diimine) complexes of simple hydroxamic acids and the MMP (matrix metalloproteinase) inhibitor marimastat have been evaluated as hypoxia activated drug carriers. The aceto- (aha), propion- (pha), benzohydroxamato (bha), and marimastat complexes were prepared and characterised by single crystal X-ray
J Thomas Peterson
Cardiovascular research, 69(3), 677-687 (2006-01-18)
At least 56 matrix metalloproteinase (MMP) inhibitors have been pursued as clinical candidates since the late 1970's when the first drug discovery program targeting this enzyme family began. Some of these clinical candidates were pursued for multiple indications. However, the
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