Catalog |
name |
Description |
price |
R-L-149 |
Recombinant Human Fibroblast Growth Factor |
Fibroblast growth factor-basic (bFGF), also known as FGF-2, is a heparin-binding member of the FGF superfamily. It plays an important role in cell proliferation and differentiation associated with embryogenesis, tissue regeneration, wound healing, CNS development, angiogenesis, and tumor progression. |
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R-L-151 |
Recombinant Human Manganese Superoxide Dismutase |
Superoxide dismutase 2 (SOD2)/manganese SOD (Mn-SOD) is an antioxidant enzyme that protects cells from oxidative stress by scavenging superoxide anions.It exists as a homotetramer where each monomer is composed of an N-terminal α-hairpin domain and a C-terminal α/β domain that contain Mn-binding catalytic active sites. |
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R-L-155 |
Streptavidin-HRP |
Streptavidin-HRP conjugate is typically used in the immunodetection of biotinylated proteins. This conjugate is suitable for use in immunoblotting, ELISA, immunomicroscopy. The amount of conjugate provided is sufficient for 25 western blots using 10 ml of working solution per reaction or 25 immunostaining reactions using 1 ml of working solution per reaction as appropriate. |
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R-L-156 |
Recombinant Bovine(rb-EK) |
Enterokinase is a serine proteolytic enzyme, which can recognize the sequence of ASP ASP Lys (ddddk) in the protein efficiently and specifically, hydrolyze the peptide bond at the C-terminal of lysine (Lys , K), produce cleavage, hydrolyze trypsinogen to trypsin in the organism. Because enterokinase has high specificity and efficient enzymatic cleavage, it is widely used in genetic engineering.
Activity definition: 25 ℃, reaction buffer 50 mM Tris-HCl (pH 8.0), substrate 50 μ G 1 mg/ml of fusion protein containing restriction site, the amount of enzyme required to cut 95% of fusion protein within 16 hours is 1 enzyme activity unit (1 U). |
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R-L-157 |
Recombinant Bovine,rbEK-His |
Enterokinase (EC 3.4.21.9) is a serine proteolytic enzyme, which can recognize the sequence of ASP ASP Lys (DDDDK) in protein efficiently and specifically, hydrolyzed peptide binding at the c-terminal of lysine (Lys, K), producing cleavage, hydrolyzes trypsinogen into trypsin in the body. Because enterokinase has high specificity and efficient enzymatic cleavage, it is widely used in genetic engineering. Product development. Natural enterokinase consists of a heavy chain of 115kda and a light chain of 35kDa. The heavy chain anchors the cell membrane, and the light chain has full enzymatic catalytic activity. The central region of light chain activity (235A. A., 26.2kda) secreted and expressed by E. coli is more active than that of bovine enterokinase, which is particularly suitable for the enzymatic digestion of the fusion protein of genetic engineering.
Activity definition: 25 ℃, reaction buffer 50 mM Tris-HCl (pH 8.0), substrate 50 μ G 1 mg/ml of fusion protein containing restriction site, the amount of enzyme required to cut 95% of fusion protein within 16 hours is 1 enzyme activity unit (1 U). |
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R-L-158 |
Recombinant Core Streptavidin,r-cSA |
Compared to native streptavidin, rc-SA is improved in stability and solubility by removing the sequence unrelated to activity. In addition, a cysteine residue is inserted at the C-terminus of rc-SA for covalent conjugation to the resin. |
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R-L-159 |
Recombinant Core Streptavidin 2,r-csa2 |
Compared to native streptavidin, r-cSA2 is improved in stability and solubility by removal of the activity-unrelated sequence. Compared to r-csa, the amino acid sequence of this product does not contain cysteine, so it does not need reduction therapy. |
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R-L-160 |
Recombinant Streptavidin 2,r-SA2 |
Recombinant streptavidin 2 (r-SA2) is modified from native streptavidin at the molecular level by removing the binding force to form tetramers. r-SA2 is an active monomer, but its affinity for biotin is strongly weakened (Kd≈10-7M), achieving reversible binding and dissociation. Thus, it can be used for the gentle separation and purification of proteins, antibodies, nucleic acids and other biotinylated materials. |
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R-L-161 |
Recombinant Core Streptavidin 3,r-cSA3 |
Recombinant central streptavidin 3 (r-cSA3) is modified from native streptavidin at the molecular level by removing the binding force to form tetramers. r-cSA3 is an active monomer, but its affinity for biotin is strongly weakened (Kd≈10-7M), achieving reversible binding and dissociation. It can be used for gentle separation and purification of proteins, antibodies, nucleic acids and other biotinylated materials. |
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R-L-162 |
Recombinant Core Streptavidin 4,r-cSA4 |
In theory, an SA can bind four biotinylated macromolecules, but due to the spatial barrier in biotinylated macromolecules, SA generally cannot bind 1-2 biotinylated macromolecules. We have optimized the spatial structure of streptavidin 4 at the molecular level, which leads to advantages in binding with biotinylated macromolecules. Our designed product can bind 2-4 biotinylated macromolecules, and its stability is also higher than common SA or SA core. It is suitable for scientific research, diagnostic testing and other fields. |
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