| Description | Source: Microorganism Isoelectric point: 5.1 Michaelis constant: 5.5×10-5 M (Choline) Optimum pH: 7.0~8.5 Fig. 1Optimum temperature: 55℃ Fig. 3pH Stability: 5.0~9.0 (25℃, 20hr) Fig. 2Thermal stability: <55℃ (pH 8.0, 15min) Fig. 4Inhibitors: Co2+, Source: Microorganism Isoelectric point: 5.1 Michaelis constant: 5.5×10-5 M (Choline) Optimum pH: 7.0~8.5 Fig. 1Optimum temperature: 55℃ Fig. 3pH Stability: 5.0~9.0 (25℃, 20hr) Fig. 2Thermal stability: <55℃ (pH 8.0, 15min) Fig. 4Inhibitors: Co2+, Cu2+, Fe3+, Mn2+, Ni2+, Zn2+, BME, NEM, Proclin, SDS, Triton X-100 Effect of various chemicals: Table 1Reaction:... Read More | Collagenase NB 1 is chromatographically highly purified; therefore it contains a very high collagenolytic activity. It is largely free from additional enzymatic activities like clostripain, trypsin-like activity and neutral protease, as well as endotoxins.SpecificationsContains chromatographically Collagenase NB 1 is chromatographically highly purified; therefore it contains a very high collagenolytic activity. It is largely free from additional enzymatic activities like clostripain, trypsin-like activity and neutral protease, as well as endotoxins.SpecificationsContains chromatographically highly purified class I and class II collagenase (1).Largely free from clostripain, trypsin-like protease and neutral protease.Vial contains not less than 2000 PZ U collagenase.Activity (Wünsch): ≥ 3.00 U/mgEndotoxin: ≤ 10.0 EU/mg (Ph. Eur.)(Clostridiopeptidase A)EC 3.4.24.3 • Mr ca. 70 000 - 120 000 (collagenases) • CAS [9001-12-1]ApplicationCollagenase NB 1 is, mostly in combination with Neutral Protease NB, suitable for cell isolation from several tissue types.References and DefinitionsUnit definition: Collagenase: 1 U according to Wünsch (2) catalyzes the hydrolysis of 1 µmole 4-phenylazobenzyloxycarbonyl-L-prolyl-L-leucylglycyl-L-prolyl-D-arginine per minute at 25 °C, pH 7.1.Endotoxin: Ph. Eur. (1 Endotoxin Unit is equal to 1 International Unit of a WHO approved reference standard endotoxin (RSE)).References1. Bond, M.D. & van Wart, H.E. (1984) Biochemistry 23, 3077-30912. Wünsch, E. & Heidrich, H.G. (1963) Hoppe-Seyler's Z. Physiol. Chem. 333, 149-51... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:Bcl-2 family proteins contribute to programmed cell death or apoptosis. It is a large protein family and all members contain at least one of four Bcl-2 homology domains. Certain members (Bcl-2, Bcl-XL and Mcl-1) arePurity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:Bcl-2 family proteins contribute to programmed cell death or apoptosis. It is a large protein family and all members contain at least one of four Bcl-2 homology domains. Certain members (Bcl-2, Bcl-XL and Mcl-1) are antiapoptotic, whilst others (Bax, Bak, Bok) are proapoptotic... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:MCP-2 and CCL7 are two monocyte chemotactic proteins produced by human MG-63 osteosarcoma cells. Both MCP-2 and CCL7 are members of the C-C family of chemokines and share 62% and 71% amino acid sequence identity, Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:MCP-2 and CCL7 are two monocyte chemotactic proteins produced by human MG-63 osteosarcoma cells. Both MCP-2 and CCL7 are members of the C-C family of chemokines and share 62% and 71% amino acid sequence identity, respectively, with MCP-1. CCL7 also shares 58% amino acid identity with MCP-2. CCL7 cDNA encodes a 99 amino acid residue precursor protein from which the N-terminal 23 amino acid residues are cleaved to generate the 76 amino acid residue mature CCL7. Mature CCL7 contains a potential N-linked and several possible O-linked glycosylation sites. Similarly to other C-C chemokines, all three MCP proteins are monocyte chemoattractants. In addition, the three MCPs can chemoattract activated NK cells as well as CD4+ and CD8+ T lymphocytes. All three cytokines have also been shown to attract eosinophils and induce histamine secretion from basophils... Read More | Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining. Function：Actin cross-linking/gelling protein (By similarity). Involved in calcium interactions and contractile properties of the cell that may contribute to replicative senescence |