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RNaseOUT™ Recombinant Ribonuclease Inhibitor (Invitrogen™)

RNaseOUT™ Recombinant Ribonuclease Inhibitor is a potent noncompetitive inhibitor of pancreatic-type ribonucleases such as RNase A, and is used to avoid RNA degradation in a variety of applications. RNaseOUT™ Recombinant Ribonuclease Inhibitor is an acidic protein with a molecular weight of ~52 kDa. RNaseOUT™ inhibits RNase A, RNase B, and RNase C.

Applications
cDNA synthesis, RT-PCR, and in vitro transcription and translation

Source
Purified by affinity chromatography from E. coli expressing a cloned porcine gene

Performance and quality testing
SDS-PAGE purity, endodeoxyribonuclease assay, protein concentration, specific activity, performance evaluated by RT-PCR

Unit definition
One unit inhibits 5 ng of RNase A by 50% using cytidine 2´, 3´ cyclic monophosphate (cCMP) as the substrate

Unit reaction conditions
100 mM Tris-acetate (pH 6.5), 1 mM EDTA, 0.2 mM cCMP, 2 µg RNase A in 1 mL from 0 to 10 min at 25°C

RiboLock RNase Inhibitor (40 U/µL) (Thermo Scientific™)

Thermo Scientific RiboLock RNase Inhibitor inhibits the activity of RNases A,B and C by binding them in a noncompetitive mode at a 1:1 ratio. It does not inhibit eukaryotic RNases T1, T2, U1, U2, CL3 as well as prokaryotic RNases I and H.

Highlights

Performs under a wide range of reaction conditions
Protects RNA from degradation at temperatures up to 55°C

Note

DTT provided in the Storage Buffer ensures stability during long term storage, but is not necessary for inhibitor activity. Recommended concentration 1 U/ µL of a reaction mixture.

Paclitaxel (Taxol Equivalent) - for use in research only (Invitrogen™)

Invitrogen offers paclitaxel for research purposes only at a purity of >98% by HPLC. Paclitaxel, formerly referred to as taxol in some scientific literature, is the approved generic name for the anticancer pharmaceutical Taxol (a registered trademark of Bristol-Myers Squibb Co). Paclitaxel promotes tubulin assembly, producing aggregates that cannot be depolymerized by dilution, calcium ions, cold or a number of microtubule-disrupting drugs. Cultured cells treated with paclitaxel are blocked in the G2 and M phases of the cell cycle.

LY294002 (Invitrogen™)

LY294002 is a potent and specific cell-permeable inhibitor of phosphatidylinositol 3-kinase (PI3-kinase).

Format/Formulation: Lyophilized

Pierce™ Protease Inhibitor XL Capsules, EDTA-free (Thermo Scientific™)

Thermo Scientific Pierce Protease Inhibitor XL Capsules, EDTA-free, contain a broad spectrum formulation of four protease inhibitors and each capsule is sufficient for 500 mL of solution.

Features of EDTA-free Protease Inhibitor XL Capsules:
Broad spectrum formulation—contains AEBSF, bestatin, E-64, and pepstatin A for better protection versus PMSF
Large volume format—one capsule is sufficient for 500 mL of solution
Convenient—ready-to-use, dissolves clearly into solution within three minutes
Compatible—use directly with Pierce protein assays
EDTA-free—formulated without EDTA, a metalloproteinase inhibitor

Pierce Protease Inhibitor XL Capsules protect proteins from proteolytic degradation through inhibition of the serine proteases, cysteine proteases, aspartic acid proteases, and aminopeptidases that are typically present in cell lysate samples. The tablets contain AEBSF, bestatin, E-64, and pepstatin A. Each capsule is sufficient for 500 mL of solution, and is suitable for reagent preparation prior to protein extraction from tissue and cultured cells.

Proteases make up a large category of enzymes, including endopeptidases and exopeptidases, which catalyze the hydrolytic breakdown of proteins into peptides or amino acids. Proteases reside in cellular compartments, but upon cell lysis the proteases are released, resulting in the degradation of valuable proteins. For this reason, it is common practice to add multiple compounds known to inactivate or inhibit proteases to cell lysis buffers or cell extracts. PMSF is commonly used for protease protection in large volumes, but does not offer the same level of protection as the capsule formulation.

To use Pierce Protease Inhibitor XL Capsules, simply twist the capsule to open and empty the contents of one capsule into 500 mL of solution. The protease inhibitor formulation is compatible with most detergent-based cell lysis reagents, including Pierce cell lysis solutions. Pierce Protease Inhibitor XL Capsules do not contain phosphatase inhibitors. If necessary, phosphatase inhibitors, such as Pierce phosphatase inhibitors, can be added along with the protease inhibitor capsules.

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Pierce Protease and Phosphatase Inhibitor Mini Tablets,EDTA-free (Thermo Scientific™)

Thermo Scientific Pierce Protease and Phosphatase Inhibitor Mini Tablets, EDTA-free, contain both protease inhibitors and phosphatase inhibitors to provide broad-spectrum complete protection from dephosphorylation and proteolytic degradation.

Features of Protease and Phosphatase Inhibitor Mini Tablets, EDTA-free:
Improved formulation—tablets dissolve quickly to form a clear solution
Economical—more cost effective than other commercially available formulations for equivalent volumes
Convenient—ready-to-use, fully disclosed, broad-spectrum formulations
Compatible—use directly with Pierce BCA assays
EDTA-free—formulated without EDTA, a metalloproteinase inhibitor (only for EDTA-free formulations)

The Pierce Protease and Phosphatase Inhibitor Mini Tablets contain aprotinin, bestatin, E-64, and leupeptin to provide protection from degradation by serine proteases, cysteine proteases, and aspartic acid proteases. To prevent the dephosphorylation activity of serine/threonine and tyrosine phosphatases, each tablet also contains sodium fluoride, sodium orthovanadate, sodium pyrophosphate, and beta-glycerophosphate. Pierce Protease and Phosphatase Inhibitor Tablets are stable at 4°C for up to 12 months, and each tablet is sufficient for 10 mL of solution.

Pierce Protease and Phosphatase Inhibitor Mini Tablets are the first complete inhibitor tablet. Adding one tablet to 10 mL of lysis buffer provides complete protection from protease and phosphatase activity during protein extraction and protein purification. There are two formulations of this inhibitor available, one containing EDTA and one without. While both formulations have metalloprotease inhibitors, an EDTA-free formulation is available for applications that require divalent cations for protein activity. Similarly, EDTA and certain phosphatase inhibitors interfere with immobilized metal chelate affinity chromatography (IMAC) and 2D electrophoresis. Dialyze or desalt the sample before performing these procedures. The Protease and Phosphatase Inhibitor formulation is mass spectrometry-compatible because it does not contain AEBSF.

Related products
Pierce Phosphatase Inhibitor Mini Tablets
Pierce Protease Inhibitor Mini Tablets, EDTA-free

Pierce Protease Inhibitor Mini Tablets (Thermo Scientific™)

Thermo Scientific Pierce Protease Inhibitor Mini Tablets contain broad-spectrum protease inhibitors that are highly effective at preventing proteolytic degradation during cell lysis and protein extraction experiments.

Features of Protease Inhibitor Mini Tablets:
Improved formulation—tablets dissolve quickly to form a clear solution
Economical—more cost effective than other commercially available formulations for equivalent volumes
Convenient—ready-to-use, fully disclosed, broad-spectrum formulations
Compatible—use directly with Pierce BCA assays

Pierce Protease Inhibitor Mini Tablets protect proteins from proteolytic degradation through inhibition of the serine proteases, cysteine proteases, aspartic acid proteases, and aminopeptidases that are typically present in cell lysate samples. The tablets contain AEBSF, aprotinin, bestatin, E-64, leupeptin, and pepstatin A. Stable for storage at 4°C for up to 12 months, each mini tablet is sufficient for 10 mL of solution, and is suitable for reagent preparation prior to protein extraction from tissue and cultured cells.

Proteases make up a large category of enzymes, including endopeptidases and exopeptidases, which catalyze the hydrolytic breakdown of proteins into peptides or amino acids. Proteases reside in cellular compartments, but upon cell lysis the proteases are released, resulting in the degradation of valuable proteins. For this reason, it is common practice to add multiple compounds known to inactivate or inhibit proteases to cell lysis buffers or cell extracts.

To use Pierce Protease Inhibitor Mini Tablets, simply dissolve 1 tablet in 10 mL of buffer or lysate. The protease inhibitor formulation is compatible with most detergent-based cell lysis reagents, including Pierce Cell Lysis solutions. Pierce Protease Inhibitor Mini Tablets do not contain phosphatase inhibitors. If necessary, phosphatase inhibitors, such as Pierce Phosphatase Inhibitor Mini Tablets, can be added along with the protease inhibitor tablets.

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Pierce Protease Inhibitor Mini Tablets, EDTA-free
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Pierce Phosphatase Inhibitor Mini Tablets
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RNase Inhibitor (Applied Biosystems™)

RNase Inhibitor (ribonuclease inhibitor) is a 50 kDa recombinant enzyme used to inhibit RNase activity. It does not contain DNase or endonuclease activity. Features of this enzyme:

• Inhibits RNase activity—preventing degradation of RNA template
• Lacks DNA endonuclease activity—for better product yield

PD98059 (Invitrogen™)

PD98059 is a potent and selective cell permeable inhibitor of MAP kinase kinase (MEK). It selectively blocks the activation of MEK, thereby inhibiting the phosphorylation and the activation of MAP kinase.

Format/Formulation: Lyophilized

Pierce Protease Inhibitor Tablets (Thermo Scientific™)

Thermo Scientific Pierce Protease Inhibitor Tablets contain broad-spectrum protease inhibitors that are highly effective at preventing proteolytic degradation during cell lysis and protein extraction experiments.

Features of Protease Inhibitor Tablets:
Improved formulation—tablets dissolve quickly to form a clear solution
Economical—more cost effective than other commercially available formulations for equivalent volumes
Convenient—ready-to-use, fully disclosed, broad-spectrum formulations
Compatible—use directly with Pierce BCA assays

Pierce Protease Inhibitor Tablets protect proteins from proteolytic degradation through inhibition of the serine proteases, cysteine proteases, aspartic acid proteases, and aminopeptidases that are typically present in cell lysate samples. The tablets contain AEBSF, aprotinin, bestatin, E-64, leupeptin, and pepstatin A. Stable for storage at 4°C for up to 12 months, each tablet is sufficient for 50 mL of solution, and is suitable for reagent preparation prior to protein extraction from tissue and cultured cells.

Proteases make up a large category of enzymes, including endopeptidases and exopeptidases, which catalyze the hydrolytic breakdown of proteins into peptides or amino acids. Proteases reside in cellular compartments, but upon cell lysis the proteases are released, resulting in the degradation of valuable proteins. For this reason, it is common practice to add multiple compounds known to inactivate or inhibit proteases to cell lysis buffers or cell extracts.

To use Pierce Protease Inhibitor Tablets, simply dissolve 1 tablet in 50 mL of buffer or lysate. The protease inhibitor formulation is compatible with most detergent-based cell lysis reagents, including Pierce Cell Lysis solutions. Pierce Protease Inhibitor Tablets do not contain phosphatase inhibitors. If necessary, phosphatase inhibitors, such as Pierce Phosphatase Inhibitor Mini Tablets, can be added along with the protease inhibitor tablets.

Related products
Pierce Protease Inhibitor Tablets, EDTA-free
Pierce Protease Inhibitor Mini Tablets
Pierce Phosphatase Inhibitor Mini Tablets
Pierce Protease and Phosphatase Inhibitor Mini Tablets

Pierce™ Protease Inhibitor Mini Tablets, EDTA-free (Thermo Scientific™)

Thermo Scientific Pierce Protease Inhibitor Mini Tablets, EDTA-free, contain broad-spectrum protease inhibitors that are highly effective at preventing proteolytic degradation during cell lysis and protein extraction experiments.

Features of EDTA-free Protease Inhibitor Mini Tablets:
Improved formulation—tablets dissolve quickly to form a clear solution
Economical—more cost effective than other commercially available formulations for equivalent volumes
Convenient—ready-to-use, fully disclosed, broad-spectrum formulations
Compatible—use directly with Pierce BCA assays
EDTA-free—formulated without EDTA, a metalloproteinase inhibitor (only for EDTA-free formulations)

Pierce Protease Inhibitor Mini Tablets protect proteins from proteolytic degradation through inhibition of the serine proteases, cysteine proteases, aspartic acid proteases, and aminopeptidases that are typically present in cell lysate samples. The tablets contain AEBSF, aprotinin, bestatin, E-64, leupeptin, and pepstatin A. Stable for storage at 4°C for up to 12 months, each mini tablet is sufficient for 10 mL of solution, and is suitable for reagent preparation prior to protein extraction from tissue and cultured cells.

Proteases make up a large category of enzymes, including endopeptidases and exopeptidases, which catalyze the hydrolytic breakdown of proteins into peptides or amino acids. Proteases reside in cellular compartments, but upon cell lysis the proteases are released, resulting in the degradation of valuable proteins. For this reason, it is common practice to add multiple compounds known to inactivate or inhibit proteases to cell lysis buffers or cell extracts.

To use Pierce Protease Inhibitor Mini Tablets, simply dissolve 1 tablet in 10 mL of buffer or lysate. The protease inhibitor formulation is compatible with most detergent-based cell lysis reagents, including Pierce Cell Lysis solutions. Pierce Protease Inhibitor Mini Tablets do not contain phosphatase inhibitors. If necessary, phosphatase inhibitors, such as Pierce Phosphatase Inhibitor Mini Tablets, can be added along with the protease inhibitor tablets.

Related products
Pierce Protease Inhibitor Mini Tablets
Pierce Protease Inhibitor Tablets
Pierce Phosphatase Inhibitor Mini Tablets
Pierce Protease and Phosphatase Inhibitor Mini Tablets

Rapamycin (Invitrogen™)

Rapamycin is a member of a family of macrolide immunosuppressants that bind to and inhibit the FK506 binding protein (FKBP) proline rotamase.

Format/Formulation: Lyophilized

Ambion™ RNase Inhibitor, cloned, 40 U/µL (Invitrogen™)

Ambion® RNase Inhibitor, a recombinant human protein produced in E. coli, is a potent inhibitor of neutral pancreatic RNase A type enzymes. The mode of inhibition is noncompetitive; the inhibitor tightly binds RNases in a 1:1 ratio. Supplied in one tube containing 10,000 U (40 U/ µL). The enzyme has been shown to inactivate RNases present in many tissues and cell types. Addition of the ribonuclease inhibitor (RI) has been shown to be useful whenever the integrity of RNA must be maintained such as in the preparation of cDNA by reverse transcription, in vitro RNA transcription, and in in vitro protein synthesis. RI does not inhibit RNase I, T1, T2, H, U1, U2, or CL3. RI requires a minimum of 1 mM DTT to maintain activity, and has an activity range between pH 5.0 to 8.0 with maximal activity between pH 7.0 and 8.0. Since the mode of inhibition is the formation of a 1:1 complex with RNases, care must be taken to avoid denaturation or oxidation of the ribonuclease inhibitor (e.g. by addition of SDS, urea, etc.). RI should be added to transcription, translation, and cDNA synthesis reactions to give a final concentration of 1 U/ µL. RNase Inhibitor is rigorously tested for contaminating RNase, exonuclease, endonuclease, and protease activity.

Unit Definition:
One unit is the amount of protein required to inhibit the activity of 5 ng of RNase A by 50%. Unit assay conditions: 100 mM Tris-acetate (pH 6.5), 1 mM EDTA, 1 mM cyclic 2',3'-CMP, and RNase inhibitor. Addition of RNase A initiates the reaction. RNase Inhibitor activity is measured by the inhibition of hydrolysis of cyclic 2', 3'-CMP by RNase A.

Ribonuclease Inhibitor, Cloned (Invitrogen™)

Ribonuclease Inhibitor, Cloned is a potent non-competitive inhibitor of neutral pancreatic ribonucleases.

Applications:
Cell-free translation systems (1). Reverse transcription of mRNA (2).

Source:
Recombinant, purified from E. coli.

Performance and Quality Testing:
No detectable contaminating activity is observed in DNA nicking, ribonuclease, and protease assays.

Unit Definition:
One unit inhibits 5 ng RNase A by 50% using cytidine 2´, 3´ cyclic monophosphate (cCMP) as the substrate (3).

PKI [14 22] Myristoylated PTD (Invitrogen™)

cAMP-dependent protein kinase (PKA) inhibitor. This peptide is a highly specific inhibitor of cAMP-dependent protein kinase (PKA).

Format/Formulation: Lyophilized trifluoroacetate salt, >97% purity by HPLC.

Molecular Weight: 1208