SB-3CT

BML-EI325

Datasheet
Manual
SDS
CofA

Already have an account?

MMP inhibitor

Competitive, mechanism-based inhibitor of matrix metalloproteinases 2 and 9 (MMP-2 and MMP-9). It possesses K_i values in the nanomolar range against the gelatinases (14nM for MMP-2; 600nM for MMP-9), but in the micromolar range against other metalloproteinases (206µM for MMP-1, 15µM for MMP-3, 96µM for MMP-7, and 4µM for ADAM17/TACE). This inhibitor has also been used in vitro, in vivo, and in tissue culture. In vivo, it is metabolized to an even more potent gelatinase inhibitor.

Shipping: Available products typically ship within 24/48h, via priority shipping.

Do you need support? Contact Customer Service or Technical Support.

Online Account
Access or Create Your Account

Product Details

Appearance	White solid.
CAS	292605-14-2
Couple Target	MMP, MMP-2, MMP-9
Couple Type	Inhibitor
Formula	C₁₅H₁₄O₃S₂
MW	306.4
Purity	≥98% (TLC)
Solubility	Soluble in DMSO (at least 30mM) or 100% ethanol.

Handling & Storage

Use/Stability	As indicated on product label or CoA when stored as recommended.
Long Term Storage	-20°C
Shipping	Blue Ice

Regulatory Status	RUO – Research Use Only

ADAM17 Mediates Proteolytic Maturation of Voltage-Gated Calcium Channel Auxiliary α2δ Subunits, and Enables Calcium Current Enhancement: I. Kadurin, et al.; Function (Oxf.) 3, zqac013 (2022), Abstract
Primitive macrophages control HSPC mobilization and definitive haematopoiesis: J. Travnickova, et al.; Nat. Commun. 6, 6227 (2015), Application(s): Cell Culture, Assay, Abstract
Metabolism of a highly selective gelatinase inhibitor generates active metabolite: M. Lee et al.; Chem. Biol. Drug. Des. 70, 371 (2007), Abstract
Inhibition of human prostate cancer growth, osteolysis and angiogenesis in a bone metastasis model by a novel mechanism-based selective gelatinase inhibitor: R. D. Bonfil et al.; Cancer Res. 118, 2721 (2006), Abstract
Antimetastatic activity of a novel mechanism-based gelatinase inhibitor: A. Krüger, et al.; Cancer Res. 65, 3523 (2005), Abstract — Full Text
Pronounced diversity in electronic and chemical properties between the catalytic zinc sites of tumor necrosis factor-alpha-converting enzyme and matrix metalloproteinases despite their high structural similarity: A. Solomon et al.; J. Biol. Chem. 279, 31646 (2004), Abstract
A Convenient Synthesis of a Selective Gelatinase Inhibitor as an Antimetastatic Agent: I.T. Lim, et al.; J. Org. Chem. 69, 3572 (2004), Abstract
Complex pattern of membrane type 1 matrix metalloproteinase shedding. Regulation by autocatalytic cells surface inactivation of active enzyme: M. Toth et al.; J. Biol. Chem. 277, 26340 (2002), Abstract
X-ray absorption studies of human matrix metalloproteinase-2 (MMP-2) bound to a highly selective mechanism-based inhibitor. comparison with the latent and active forms of the enzyme: O. Kleifeld et al.; J. Biol. Chem. 276, 17125 (2001), Abstract
Potent and Selective Mechanism-Based Inhibition of Gelatinases: S. Brown et al.; J. Am. Chem. Soc. 122, 6799 (2000), Abstract

Datasheet, Manuals, SDS & CofA

Manuals And Inserts

Datasheet

Certificate of Analysis

Please enter the lot number as featured on the product label

Lot No. :

SDS

Enzo Life Science provides GHS Compliant SDS

If your language is not available please fill out the SDS request form

Your Cart

Your Cart

SB-3CT

BML-EI325

Product Details

Handling & Storage

Datasheet, Manuals, SDS & CofA

Manuals And Inserts

Certificate of Analysis

SDS

Change Country

Tell us about You

Tell us about your paper

Tell us about You

Tell us about your project