Modifying Enzymes
Enzo Life Sciences MMP-10 (catalytic domain) (human), (recombinant) (10 µg)
Alternative name: Matrix metalloproteinase 10, Stromelysin 2. Formulation: Liquid. In 50mM TRIS, 5mM CaCl2, 300mM NaCl, 20µM ZnCl2, 0.5% Brij-35, and 30% glycerol. Source: Produced in E. coli. Active Matrix Metalloproteinase-10 (MMP-10, stromelysin-2, transin-2) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-10 (Phe99-Glu271, NM_2425) with a C-terminal purification tag. This comprises an active form of MMP-10 which lacks the C-terminal hemopexin domain. MMPs lacking this domain cannot cleave native collagens; however, activity toward other targets such as gelatin, casein, or peptide substrates is unaffected. Long Term Storage: -80°C.
Active Motif Preindex Tn5 Transposomes 1x96
Pre-indexed Assembled Tn5 Transposomes are provided in a flexible breakaway 96-well plate format to enable higher throughput ATAC-Seq assays. Each well contains a transposome loaded with a unique i5 and i7 index, enabling direct indexing during tagmentation. By having a unique i7 & i5 Indexed Primer combination in each well, it is easy to perform multiple ATAC-Seq reactions without having to pipette primers separately and keep track of the combinations.
Research Products International Corp Macerozyme R-10, 1 Gram
Macerating enzyme from Rhizopus sp. Often used in combination with Cellulase (C32200). Optimum pH range 3.5 - 7.0.
Sigma Aldrich Fine Chemicals Biosciences Apyrase from potatoes, 9000-95-7, MFCD00130542, 500UN
Suitable for manufacturing of diagnostic kits and reagents, ATPase ≥200 units/mg protein. Synonym: Adenosine 5′-diphosphatase, Adenosine 5′-triphosphatase, Apyrase from potatoes. Apyrase is used to hydrolyze nucleoside triphosphates and diphosphates. For hydrolysis of organic di and triphosphates, the optimal pH is 6, and for inorganic substrates, the optimal pH is 5.1. Apyrase, from Sigma, has been used in inhibition studies of platelet-aggregation.
Sigma Aldrich Fine Chemicals Biosciences Carbonic Anhydrase from bovine erythrocytes | 9001-03-0 | MFCD00081467 | 100 mg
Carbonic Anhydrase from bovine erythrocytes | Purity: ≥95% | 9001-03-0 | MFCD00081467 | 100 mg
Sigma Aldrich Fine Chemicals Biosciences Phosphatase, Alkaline from bovine intestinal mucosa buffered aqueous glycerol solution, >=4,000 DEA units/mg protein | 9001-78-9 | MFCD00131849 | 2KU
Phosphatase, Alkaline from bovine intestinal mucosa buffered aqueous glycerol solution, >=4,000 DEA units/mg protein | 9001-78-9 | MFCD00131849 | 2KU
New England Biolabs, Inc. SplintR Ligase – 1250 units
SplintR Ligase efficiently catalyzes the ligation of adjacent, single-stranded DNA splinted by a complementary RNA strand. This activity may enable novel approaches for characterization of miRNAs and mRNAs, including SNPs. The robust activity of the enzyme and its affinity for RNA-splinted DNA substrates (apparent Km = 1 nM) enable sub-nanomolar detection of unique RNA species within a complex mixture, making SplintR ligase a superior choice for demanding RNA detection technologies. The activity is enhanced at higher temperatures (up to 37°C), and by supplementation with 5 mM Mn2+. The reaction is inhibited by salt concentrations in excess of 100 mM. The enzyme tolerates all base pair combinations at the ligation junction, but is partially inhibited by dC/G and dG/C base pairs at the donor (phosphorylated) side ligation junction, particularly when the +2 base was also a C/G base pair.
New England Biolabs, Inc. T4 RNA Ligase 2, truncated KQ – 2000 units
T4 RNA Ligase 2, truncated KQ (T4 Rnl2tr R55K, K227Q) specifically ligates the preadenylated 5' end of DNA or RNA to the 3' OH end of RNA. The enzyme does not use ATP for ligation but requires pre-adenylated linkers. T4 Rnl2tr R55K, K227Q is a double-point mutant of T4 RNA Ligase 2, truncated . Mutation of K227 in T4 RNA Ligase 2 reduces enzyme lysyl adenylation. K227Q reduces the formation of undesired ligation products (concatemers and circles) by T4 Rnl2tr, by reducing the trace activity of T4 Rnl2tr in transfer of adenylyl groups from linkers to the 5-phosphates of input RNAs. Mutation of R55K in T4 Rnl2tr K227Q increases the ligation activity of the enzyme to levels similar to T4 Rnl2tr. The exclusion of ATP, use of pre-adenylated linkers, and the reduced enzyme lysyl adenylation activity provide the lowest possible background in ligation reactions. This enzyme has been used for optimized linker ligation for high-throughput sequencing library construction of small RNA .
Apexbio Technology LLC EZ Cap ER-EGFP Probe mRNA (m1Ψ) 5x1mg (1mg/mL)
ER-EGFP mRNA encodes a fusion protein comprising an endoplasmic reticulum (ER) targeting signal sequence and enhanced green fluorescent protein (EGFP) EGFP is a widely used fluorescent marker protein for biological imaging By fusing EGFP to the ER signal sequence dynamic changes in the ER can be observed in real-time in live cells making it particularly useful for studying the structure function and interactions of the ER with other cellular organelles ER-EGFP s efficient fluorescent properties and specific localization to the ER position it as an ideal tool for studying ER-related processes The EZ Cap ER-EGFP Probe mRNA (m1 ) is provided at 1 mg/mL specifically designed for targeted expression of a green fluorescent protein label at the ER This mRNA is synthesized through co-transcriptional capping resulting in a Cap 1 structure The incorporation of m1 modifications poly(A) tail significantly enhances mRNA stability and lifetime both in vitro and in vivo
ABclonal Technology Exonuclease III (E. coli)
Exonuclease III (E.coli) catalyzes the stepwise removal of mononucleotides from 3?-hydroxyl termini of duplex DNA. The preferred substrates are dsDNA with blunt or recessed 3?-, termini although the enzyme also acts at nicks in dsDNA to produce single-strand gaps. dsDNA with 3?-overhang are resistant to cleavage; when overhangs length is ≥ 4 bases，dsDNA are able to fully prevent ExoIII cleavage process. Exonuclease III has also been reported to have RNase H, 3?-phosphatase and AP-endonuclease activities.
New England Biolabs, Inc. ShortCut RNase III – 1000 units
ShortCut RNase III, used with its manganese-containing reaction buffer, converts long double-stranded RNA into a heterogeneous mix of short (18-25 bp) interfering RNAs (siRNA) suitable for RNA interference in mammalian cells. 1.5 units (1 µl) of ShortCut RNase III is sufficient to convert 1µ g of dsRNA into siRNA suitable for RNA interference in mammalian cells.
Abcam NADP, Coenzyme, 1G
MW 787.37 g/mol, Purity >=93%. NADP and NADPH form a redox pair. NADP is the oxidised form of NADPH. NADP/NADPH is a coenzyme that supports redox reactions via the transport of electrons in a vast array of applications. Acts as a coenzyme couple in various cytochrome P450 systems and oxidase/reductase reaction systems.
The product is subject to the following: Abcam Restricted Use Statement
Omega Biotek Inc Proteinase K, 10 mL solution, 20 mg/mL concentration, non-specific serine protease, RNase/DNase free, high stability in SDS, EDTA, urea
Omega Bio-tek Proteinase K is a non-specific serine protease that is essential for various molecular biology applications. Supplied as a ready-to-use 10 mL solution, it effectively inactivates nucleases and promotes cell lysis, ensuring high-quality DNA and RNA isolation. This enzyme is stable across a broad pH range and maintains its activity even in the presence of protein-denaturing agents such as SDS, EDTA, and urea.
- Volume: 10 ml
- Formulation: Ready-to-use solution
- Concentration: 20 mg/ml
- Activity: >600 mAU/mg
- Enzyme type: Non-specific serine protease
- Source organism: Tritirachium album
- Stability: High stability in SDS, EDTA, urea
- pH range: Wide range
- Primary application: Inactivation of nucleases and lysis for DNA/RNA isolation
- Purity: RNase/DNase free
- Storage temperature: -20°C
- Shipping condition: Requires ice pack
- Country of origin: USA
Sigma Aldrich Fine Chemicals Biosciences Benzonase(R) endonuclease Safety Plus Emprove(R) Expert EMPROVE(R) Expert |
Benzonase(R) endonuclease Safety Plus Emprove(R) Expert EMPROVE(R) Expert |