| Description | GPR101 Human Pre-designed siRNA Set A contains three designed siRNAs for GPR101 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components GPR101 siRNA-1: 5 nmol (HPLC) GPR101 siRNA-2: 5 nmol (HPLC) GPR101 siRNA-3: 5 nmol (HPLC) siRNA Negative GPR101 Human Pre-designed siRNA Set A contains three designed siRNAs for GPR101 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components GPR101 siRNA-1: 5 nmol (HPLC) GPR101 siRNA-2: 5 nmol (HPLC) GPR101 siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 nmol (HPLC) FAM-labeled siRNA Negative Control: 5 nmol (HPLC) GAPDH siRNA Positive Control:5 nmol (HPLC)... Read More | DescriptionApolipoprotein E (ApoE) is present in the brain and is mainly produced by astrocytes. It is a 299 amino acid glycoprotein of 34kDa. It is present in all classes of lipoproteins except LDL (low-density lipoprotein). APOE gene has three alleles, such as APOE ε3, APOE ε4and APOE &#DescriptionApolipoprotein E (ApoE) is present in the brain and is mainly produced by astrocytes. It is a 299 amino acid glycoprotein of 34kDa. It is present in all classes of lipoproteins except LDL (low-density lipoprotein). APOE gene has three alleles, such as APOE ε3, APOE ε4and APOE ε2. It is located on human chromosome 19q13.Preparation instructionsFormLyophillized from a 0.2 µm filtered solution in 20 mM sodium phosphate, pH 7.8.Principle... 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 | Aprotinin is a competitive serine protease inhibitor that inhibits trypsin,chymotrypsin,kallikrein and plasmin.Aprotinin forms stable complexes with and blocks the active sites of enzymes. Binding is reversible with most aprotinin,protease complexes and dissociating at pH >10 or <3. Effective Aprotinin is a competitive serine protease inhibitor that inhibits trypsin,chymotrypsin,kallikrein and plasmin.Aprotinin forms stable complexes with and blocks the active sites of enzymes. Binding is reversible with most aprotinin,protease complexes and dissociating at pH >10 or <3. Effective concentration is equimolar with protease.Recombinant aprotinin is expressed in E. Coli, and purified with HPLC. It contains no animal-derived components. This is a recombinant form of bovine lung aprotinin, which is traditionally isolated from bovine lung by methods involving fractional precipitation, gel filtration, and ion exchange chromatography. UNIT DEFINITION:A conversion factor for Aprotinin is: 1 EPU = 1 USP Aprotinin Unit = 1800 KIU... Read More | Purity>97% by SDS-PAGE and HPLC analyses.FunctionMay be involved in macrophage-mediated cellular proliferation. It is mitogenic for fibroblasts and smooth muscle but not endothelial cells. It is able to bind EGF receptors with higher affinity than EGF itself and is a far more potent mitogen for Purity>97% by SDS-PAGE and HPLC analyses.FunctionMay be involved in macrophage-mediated cellular proliferation. It is mitogenic for fibroblasts and smooth muscle but not endothelial cells. It is able to bind EGF receptors with higher affinity than EGF itself and is a far more potent mitogen for smooth muscle cells than EGF. Also acts as a diphtheria toxin receptor.Background:Human HB-EGF (Heparin-Binding EGF-like growth factor) is a 12-16 kDa member of the EGF family of peptide growth factors (1-3). Also known as the DTR (diphtheria toxin receptor), it is further classified as a group 2 ErbB ligand based on its ability to activate both the EGF/ErbB1 and ErbB4 receptors (4, 5). HB-EGF is synthesized as a 208 amino acid (aa) type I transmembrane preproprecursor (1, 6). It contains a 19 aa signal sequence, a 43 aa prosegment, an 86 aa mature region (aa 63-148), an 11 aa juxtamembrane cleavage peptide, a 24 aa transmembrane segment, and a 25 aa cytoplasmic tail (aa 184-208). As an integral membrane protein, HB-EGF is expressed as a 19-27 kDa protein in mammalian cells (7-9). The variability in molecular weight (MW) is attributed to heterogeneity in glycosylation and/or the utilization of multiple proteolytic cleavage sites during maturation. Mature HB-EGF is a soluble peptide that arises from proteolytic processing of the transmembrane form. It possesses an EGF-like domain between aa 104-144, and a heparin-binding motif between aa 93‑113. Although the aa range for "mature" HB-EGF is typically stated to be Asp63-Leu148, potential N-terminal start (cleavage) sites also exist at Gly32, Arg73, Val74, Ser77 and Ala82 (8, 10-12). Thus, differential processing (in part) likely accounts for the 16-23 kDa range in MW noted for mammalian-derived mature HB-EGF. Proteases suggested to contribute to HB-EGF processing include TACE, MMP-3 and -7, ADAM-17 and ADAM-12 (11, 13-16). When expressed recombinantly in E.coli, HB-EGF (aa 73-148) runs at 14 kDa in SDS-PAGE; when expressed in Baculovirus, HB-EGF (aa 63-148, 77-148 and 32-148) runs at 18 kDa, 15 kDa, and 19 kDa respectively (8, 12, 17). Over aa 63-148, human HB-EGF- shares 76% and 73% aa sequence identity with rat and mouse HB-EGF, respectively (1, 18). Cells known to express HB-EGF include bronchial epithelium (19), visceral and vascular smooth muscle (20, 21), CD4+ T cells (22), cardiac muscle (23), glomerular podocytes (24), keratinocytes (13) and IL-10-secreting regulatory macrophages (25). As noted earlier, HB-EGF is known to bind to both 170 kDa EGFR and 180 kDa ErbB4, and through heterodimerization, ErbB2 (13, 26). Activity associated with ErbB4 binding appears to be limited to non-mitogenic actions, while EGFR binding induces both mitogenic and non-mitogenic activity... Read More |