Shop All Enzyme Inhibitors

MYR PKC Zeta Pseudosubstrate (Invitrogen™)

Selective protein kinase C (PKC) zeta inhibitor.

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

Molecular Weight: 1928

BacMam Enhancer Solution

The BacMam Enhancer helps to increase expression of BacMam reagents in mammalian cells.

To use, simply add the BacMam enhancer to cell culture media with or without serum that have already been treated with the BacMam reagent, then incubate cells and replace with fresh medium. Different cell types vary in their response to the BacMam enhancer and for best results the amount and treatment time will need to be optimized.

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).

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

BacMam Enhancer Kit (Invitrogen™)

The BacMam Enhancer helps to increase expression of BacMam reagents in mammalian cells.

To use, simply add the BacMam enhancer to cell culture media with or without serum that have already been treated with the BacMam reagent, then incubate cells for 1.5–2 hours at 37°C and 5% CO2 and replace with fresh medium. Different cell types vary in their response to the BacMam enhancer and for best results the amount and treatment time will need to be optimized. Once prepared, the enhancer solution is stable to multiple freeze⁄thaw cycles following the recommended storage conditions. If desired, the solution can be divided into aliquots following reconstitution.

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
Pierce Protease Inhibitor Tablets
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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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T-PER Tissue Protein Extraction Reagent

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

IBMX (Invitrogen™)

IBMX is a nonspecific inhibitor of phosphodiesterases that also possesses adenosine agonist activity.

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

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

Calyculin A (Invitrogen™)

Calyculin A is a structurally unique marine toxin with potent and specific protein phosphatase inhibiting activity. This compound inhibits PP2A with similar potency to okadaic acid, but inhibits PP1 with a 10- to 100-fold greater potency.

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 2,500 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.

SUPERase• In™ RNase Inhibitor (20 U/μL) (Invitrogen™)

SUPERase• In™ RNase Inhibitor is a protein-based inhibitor of nonhuman origin that noncovalently binds and inhibits the most common and troublesome RNases, including RNase A, B, C, 1, and T1. Features of SUPERase• In™ RNase Inhibitor:

• Completely removes RNase contamination from glass and plastic surfaces
• Excels at removing high levels of RNase contamination where similar products fail
• Proven effective at removing high concentrations of dried-on RNase A
• Ideal for cleaning work surfaces, pipettors, and equipment that must be RNase-free

SUPERase• In™ RNase Inhibitor can be used in any application where RNase contamination could be problematic. Because it inhibits a broader range of RNases than traditional RNase inhibitors, SUPERase• In™ is the most effective RNase inhibitor available, providing a higher level of protection against degradation.

SUPERase• In™ does not interfere with other enzymes such as RNA polymerases, reverse transcriptase, or Taq DNA polymerase. Additionally, SUPERase• In™ is active up to 65°C and over a pH range of 5.5 to 8.5.

If you are plannning to use this product with standard antibody purification methods, please contact our technical support to discuss experimental design.

Unit definition
SUPERase• In™ RNase Inhibitor at 1 U/µL will block the degradation of 0.1 µg/µL labeled RNA by 2.5 pg/µL of RNase A, 2.5 pg/µL of RNase I, and 0.0075 U/µL of RNase T1, for 4 hours at 37°C, in 20 mM Tris-HCl, pH 7.5, 50 mM NaCl, 1 mM EDTA. Analysis is by denaturing PAGE. SUPERase
• In is currently the only ribonuclease inhibitor for which the unit activity is defined by such a functional assay.

Pertussis Toxin (Invitrogen™)

Islet-activating protein Pertussis toxin consists of an A protomer subunit (S1) which possesses both NAD+ glycohydrolase and ADP-ribosyltransferase activities, and B oligomer subunits (S2, S3, S4, and S5) which are responsible for attachment of the native toxin to eukaryotic cell surfaces. Pertussis toxin uncouples G proteins from receptors by ADP ribosylating a cysteine residue near the carboxyl terminus of the α subunit.

Format/Formulation:
Lyophilized