| Description | Human IgG2-kappa, Recombinant (IB2), Isotype Control, could be used for Flow Cytometry | Protein kinase inhibitor 1 hydrochloride is a potent HIPK2 inhibitor, with IC 50 s of 136 and 74 nM for HIPK1 and HIPK2, and a K d of 9.5 nM for HIPK2.In VitroProtein kinase inhibitor 1 hydrochloride is a potent HIPK2 inhibitor, with IC 50 s of 136 and 74 nM for HIPK1 and HIPK2, and a K d of 9.5 nM Protein kinase inhibitor 1 hydrochloride is a potent HIPK2 inhibitor, with IC 50 s of 136 and 74 nM for HIPK1 and HIPK2, and a K d of 9.5 nM for HIPK2.In VitroProtein kinase inhibitor 1 hydrochloride is a potent HIPK2 inhibitor, with IC 50 s of 136 and 74 nM for HIPK1 and HIPK2, and a K d of 9.5 nM for HIPK2. Protein kinase inhibitor 1 (Compound A64) is not an effective Cdk1 inhibitor (IC 50 > 10 µM). A64 is moderately selective across a panel of kinases, with K d s of 3.7 nM (PIM3), 6.1 nM (CSNK2A2), 6.1 nM (CSNK2A2), 8.8 nM (DYRK1A), 9.5 nM (DAPK1), 31 nM (CSNK2A1), 37 nM (PIM1), 130 nM (DRAK2), 150 nM (CLK2), 190 nM (DRAK1), 220 nM (ULK2), 240 nM (CLK1), 250 nM (DYRK2), and 390 nM (ERK8) and IC 50 s of 19 nM (DYRK1A), 62 nM (DYRK1B), and 74 nM (HIPK2). MCE has not independently confirmed the accuracy of these methods. They are for reference only.IC50& Target:DYRK1 DYRK2... Read More | Product IntroduceProteinase K, originally isolated from the mold Tritirachium album, is a serine protease with broad substrate specificity and relatively high proteolytic activity. It preferentially cleaves ester and peptide bonds adjacent to the C-termini of hydrophobic, aliphatic, or aromatic Product IntroduceProteinase K, originally isolated from the mold Tritirachium album, is a serine protease with broad substrate specificity and relatively high proteolytic activity. It preferentially cleaves ester and peptide bonds adjacent to the C-termini of hydrophobic, aliphatic, or aromatic amino acids. aladdin's proteinase K is characterized by high purity, sterility, no bio-burden, and no presence of DNAse, RNAse, DNA, and RNA contaminants. It is a good partner in DNA and RNA extraction for you.Features1、According to the SDS-PAGE image,the purity of Proteinase K is more than 95% and the molecular weight is 28.9 kDa.2、Detect DNase residue by agarose gel electrophores.3、Detect Nucleic acid residue by agarose gel electrophores.4、Detect RNase residue by agarose gel electrophores.5、Using the absorbance A275 as the vertical axis and different concentrations of tyrosine as the horizontal axis, a standard curve was drawn, and the enzyme activity was calculated>30U/mg... Read More | Purity>98% by SDS-PAGE and HPLC analyses.FunctionChemoattractant for blood monocytes, memory T-helper cells and eosinophils. Causes the release of histamine from basophils and activates eosinophils. Binds to CCR1, CCR3, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-Purity>98% by SDS-PAGE and HPLC analyses.FunctionChemoattractant for blood monocytes, memory T-helper cells and eosinophils. Causes the release of histamine from basophils and activates eosinophils. Binds to CCR1, CCR3, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant RANTES protein induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). The processed form RANTES(3-68) acts as a natural chemotaxis inhibitor and is a more potent inhibitor of HIV-1-infection. The second processed form RANTES(4-68) exhibits reduced chemotactic and HIV-suppressive activity compared with RANTES(1-68) and RANTES(3-68) and is generated by an unidentified enzyme associated with monocytes and neutrophils... Read More | Inquire |