Modifying Enzymes
Sigma Aldrich Fine Chemicals Biosciences Phosphoglucose Isomerase from rabbit muscle Type XI, lyophilized powder, >=200 units/mg protein | 9001-41-6 | MFCD00131887 | 1KU
Phosphoglucose Isomerase from rabbit muscle Type XI, lyophilized powder, >=200 units/mg protein | 9001-41-6 | MFCD00131887 | 1KU
ABclonal Technology Endonuclease IV
Endonuclease IV derived from E. coli recognizes the depurine/depyrimidine (AP) site on the double- stranded DNA molecule, and cleaves the first phosphodiester bond at the 5 ?end of the AP site to form 3-OH and 5dRP . In addition, Endonuclease IV has 3?diesterase activity, which releases phosphoglyceraldehyde, intact deoxyribose 5 -phosphate, and phosphoric acid from the 3 ?end of DNA. The best substrate for this enzyme is AP double-stranded DNA, but it is also active against AP single-stranded DNA.
ABclonal Technology T4 DNA Ligase (High Conc.)
T4 DNA Ligase catalyzes the formation of a phosphodiester bond between juxtaposed 5 phosphate and 3 hydroxyl termini in duplex DNA or RNA. This enzyme will join blunt end and cohesive end termini as well as repair single stranded nicks in duplex DNA and some DNA/RNA hybrids. T4 DNA ligase will seal nicks for these DNA substrates. T4 DNA Ligase is applicable to cloning of restriction fragments and to joining linkers and adapters to blunt-ended DNA.
ABclonal Technology T3 DNA Ligase
T3 DNA Ligase is an ATP-dependent ds DNA ligase from bacteriophage T3. It can catalyze the formation of a phosphodiester bond between juxtaposed 5 phosphate and 3 hydroxyl termini in duplex DNA or RNA. T3 DNA Ligase will join blunt end and cohesive end termini. It and can also repair single-stranded nicks in duplex DNA, RNA or DNA/RNA hybrids and close the gaps in these DNA substrates. In addition, T3 DNA Ligase is more tolerant to NaCl than T4 DNA Ligase (2-fold). As with T4 DNA Ligase , addition of PEG 6000 to the T3 DNA Ligase reaction system can improve the ligation efficiency of the blunt end. 1X T4 DNA Ligase Reaction Buffer can be used in some experiments where PEG 6000 is not available, but the activity of T3 DNA Ligase is reduced to 1/10. In applications where high concentrations of NaCl need to be maintained, we recommend the use of reaction buffers without PEG 6000.
Sigma Aldrich Fine Chemicals Biosciences Proteinase K from Tritirachium album lyophilized powder, >=30 units/mg protein | 39450-01-6 | MFCD00132129 | 10MG
Proteinase K from Tritirachium album lyophilized powder, >=30 units/mg protein | 39450-01-6 | MFCD00132129 | 10MG
Sigma Aldrich Fine Chemicals Biosciences Proteinase K from Tritirachium album | 39450-01-6 | MFCD00132129 | 25mg
Proteinase K from Tritirachium album | Mol Wt: 28.93 kDa | 39450-01-6 | MFCD00132129 | 25mg
Sigma Aldrich Fine Chemicals Biosciences Proteinase K from Tritirachium album | 39450-01-6 | MFCD00132129 | 100mg
Proteinase K from Tritirachium album | Mol Wt: 28.93 kDa | 39450-01-6 | MFCD00132129 | 100mg
Sigma Aldrich Fine Chemicals Biosciences Proteinase K from Tritirachium album | 39450-01-6 | MFCD00132129 | 5mg
Proteinase K from Tritirachium album | Mol Wt: 28.93 kDa | 39450-01-6 | MFCD00132129 | 5mg
Sigma Aldrich Fine Chemicals Biosciences Proteinase K from Tritirachium album | 39450-01-6 | MFCD00132129 | 5ml
Proteinase K from Tritirachium album | 39450-01-6 | MFCD00132129 | 5ml
Sigma Aldrich Fine Chemicals Biosciences Proteinase K from Tritirachium Album | 39450-01-6 | MFCD00132129 | 1ml
Proteinase K from Tritirachium Album | 39450-01-6 | MFCD00132129 | 1ml
Sigma Aldrich Fine Chemicals Biosciences Heparinase I and III Blend
Heparinase is an inducible non-extracellular heparin-degrading enzyme. Three types of heparinises are produced by flavobacterium heparinum and contains specific sequences of heparin.
Medchemexpress LLC Amylase | 9000-92-4 | 1 G
Amylase is an enzyme produced by the pancreas and salivary glands that catalyzes the hydrolysis of starch into sugars. Amylase is broadly classified into α, β, and γ subtypes. It is for research use only. A mixture of glycosylated amylase and proline-rich proteins or fractions containing mostly non-glycosylated amylase predominantly promotes adhesion of *S. gordonii G9B*. Fractions containing amylase do not promote adhesion of *S. sanguis 10556* to HAP.
- Catalyzes the hydrolysis of starch into sugars
- Available in α, β, and γ subtypes
- Suitable for research applications
- Offered in various quantities
- Includes data sheet, SDS, COA, and handling instructions
- Appears as a solid, with a color ranging from light yellow to khaki
- Can be sourced from plants, animals, and microorganisms