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MMP-2/MMP-9 SUBSTRATE II is a fluorogenic peptide substrate specifically designed for the continuous assay of matrix metalloproteinases (MMPs), including MMP-2 (gelatinase-A) and MMP-9 (gelatinase B). These proteases play a crucial role in the breakdown of the extracellular matrix in both normal physiological conditions and disease progression. The substrate fluoresces upon cleavage by the respective MMP, allowing for easy and accurate detection, which can enhance our understanding of diseases like cancer and conditions such as tissue remodeling and inflammation.

98992-65-5

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98992-65-5 Usage

Uses

Used in Biomedical Research:
MMP-2/MMP-9 SUBSTRATE II is used as a research tool for studying the activity and regulation of matrix metalloproteinases in various biological processes. The substrate's fluorescence upon cleavage by MMPs allows for the monitoring of enzyme activity in real-time, providing valuable insights into the role of these proteases in disease progression and tissue remodeling.
Used in Drug Discovery and Development:
MMP-2/MMP-9 SUBSTRATE II is used as a screening tool in the development of new drugs targeting matrix metalloproteinases. By monitoring the substrate's fluorescence in the presence of potential inhibitors, researchers can assess the efficacy of these compounds in inhibiting MMP activity, aiding in the identification of promising drug candidates for the treatment of diseases associated with abnormal MMP activity.
Used in Diagnostic Applications:
MMP-2/MMP-9 SUBSTRATE II is used as a diagnostic tool for detecting and monitoring diseases characterized by altered MMP activity, such as cancer and inflammatory conditions. The substrate's fluorescence upon cleavage by MMPs can be measured to assess the levels of these proteases in biological samples, providing valuable information for disease diagnosis and monitoring treatment efficacy.
Used in Tissue Engineering and Regenerative Medicine:
MMP-2/MMP-9 SUBSTRATE II is used as a component in tissue engineering and regenerative medicine applications to study the role of matrix metalloproteinases in tissue remodeling and repair. By monitoring the substrate's fluorescence in response to MMP activity, researchers can gain insights into the mechanisms of tissue regeneration and develop strategies to enhance the healing process.

Check Digit Verification of cas no

The CAS Registry Mumber 98992-65-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 9,8,9,9 and 2 respectively; the second part has 2 digits, 6 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 98992-65:
(7*9)+(6*8)+(5*9)+(4*9)+(3*2)+(2*6)+(1*5)=215
215 % 10 = 5
So 98992-65-5 is a valid CAS Registry Number.

98992-65-5SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 12, 2017

Revision Date: Aug 12, 2017

1.Identification

1.1 GHS Product identifier

Product name MMP-2/MMP-9 SUBSTRATE II

1.2 Other means of identification

Product number -
Other names -

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:98992-65-5 SDS

98992-65-5Downstream Products

98992-65-5Relevant academic research and scientific papers

Phosphoramidate peptide inhibitors of human skin fibroblast collagenase

Kortylewicz,Galardy

, p. 263 - 273 (2007/10/02)

An extensive series of N-(monoethylphosphoryl)peptides was synthesized and their inhibition of purified human skin fibroblast collagenase examined. At the cleavage site S1 all reported compounds have the (EtO)(OK)P(O) group and the peptide side chain extended toward the C-terminal end (up to P5') of the substrate sequence. These phosphoramidates with a tetrahedrally hybridized phosphorus atom are thought to be transition state analogue inhibitors. They exhibited fair inhibitory potency against this vertebrate collagenase having K(i) values in the micromolar range. The most potent of these, (EtO)(OK)P(O)-Ile-TrpNHCH3 (68), inhibits with a K(i) value of 1.5 μM and is nearly 100 times stronger than (EtO)(OK)P(O)-Ile-Ala-GlyOK (51) (K(i) of 140 μM), which has the sequence matching that of the α1(I) chain of collagen in P1', P2', P3' after the cleavage site. Several compounds were prepared in an attempt to identify the nature of the S2', S3', and S4' binding sites. Alanine at the P2' position was replaced by leucine, phenylalanine, tryptophan, or tyrosine derivatives, resulting in K(i) values in a significantly lower range, 1.0-40 μM, compared to 51. No upper size limitation or specificity has been found at this position, yet similar replacements at the P3' position, which is occupied naturally by a glycine residue, gave weaker inhibitors: (EtO)(OK)P(O)-Ile-Tyr(OBzl)-PheOK (57) had a K(i) of 120 μM. Hexapeptide derivatives had weaker activities in the 270 μM-2 mM range. All inhibitors were evaluated by using the synthetic thio peptolide spectrophotometric assay.

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