| Description | DNAJC6 Human Pre-designed siRNA Set A contains three designed siRNAs for DNAJC6 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components DNAJC6 siRNA-1: 5 nmol (HPLC) DNAJC6 siRNA-2: 5 nmol (HPLC) DNAJC6 siRNA-3: 5 nmol (HPLC) siRNA Negative DNAJC6 Human Pre-designed siRNA Set A contains three designed siRNAs for DNAJC6 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components DNAJC6 siRNA-1: 5 nmol (HPLC) DNAJC6 siRNA-2: 5 nmol (HPLC) DNAJC6 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 | Protein Purity≥85% by SDS PAGEExtinction CoeffA280 nm = 10.16 at 1.0 mg/ml for pure C3Molecular Weight187,000 Da (2 chains)General DescriptionRat C3 is purified from pooled normal rat serum. C3 is central to the activation of all three pathways of complement activation (Law, S.K.A. and Reid, KProtein Purity≥85% by SDS PAGEExtinction CoeffA280 nm = 10.16 at 1.0 mg/ml for pure C3Molecular Weight187,000 Da (2 chains)General DescriptionRat C3 is purified from pooled normal rat serum. C3 is central to the activation of all three pathways of complement activation (Law, S.K.A. and Reid, K.B.M. (1995)). Initiation of each pathway generates proteolytic enzyme complexes (C3 convertases) which are bound to the target surface. These enzymes cleave a peptide bond in C3 releasing the anaphylatoxin C3a and activating C3b. For a brief time (~60 µs) this nascent C3b is capable of reacting with and covalently coupling to hydroxyl groups on the target surface. Carbohydrates are the favored target, but protein hydroxyls and amino groups also react. This process of tagging the target surface with C3b is called opsonization. The reactive site in nascent C3b is a thioester (Tack B.J., et al. (1980); Pangburn M.K. and MüllerEberhard H.J. (1980)) and C3b is linked to the target through a covalent ester bond (an amide bond is formed if C3b is attached to amino groups). Most of the C3 activated during complement activation never attaches to the surface because its thioester reacts with water forming fluid phase C3b which is rapidly inactivated by factors H and I forming iC3b. Surface-bound C3b is necessary in all three pathways for efficient activation of C5 and formation of C5b-9 complexes that lyse the target cell membrane. Surface-bound C3b and its breakdown products iC3b and C3d are recognized by numerous receptors on lymphoid and phagocytic cells which use the C3b ligand to stimulate antigen presentation to cells of the adaptive immune system. The end result is an expansion of target-specific B-cell and T-cell populations.Physical Characteristics & StructureThe calculated molecular weight of rat C3 based on its amino acid sequence is 184,111daltons (without the signal peptide) and is similar to that of human C3 (185,000 daltons).The molecular weight of rat C3 as determined by SDS/polyacrylamide gel electrophoresis has been reported by Daha, M.R. et al., (1979) to be 187,000 daltons composed of two disulfide linked chains, alpha chain (123,000 daltons) and beta chain (76,000 daltons). The extinction coefficient of rat C3 (E1%/280nm = 10.16) is calculated based on its amino acid sequence using ProtParam and assumes all pairs of Cys residues form cystines (i.e. a pair of cysteine molecules are joined by a disulfide bond). The theoretical pI of rat C3 is 6.12. The normal plasma concentration of C3 inWistar rats has been reported to be 0.581mg/ml (Daha, M.R. et al., (1979)).FunctionThe biological functions of C3 are described above in the General Description section.GeneticsRat C3 chromosome location 9. The NCBI Gene ID number for rat C3 is 24232 and UniProt accession number is P01026.Precautions/Toxicity/HazardsThis protein is purified from animal plasma/serum and therefore precautions appropriate for handling any animal blood-derived product must be used.ReferencesLaw, S.K.A. and Reid, K.B.M. (1995) Complement 2nd Edition (ISBN 0199633568) Oxford University Press, Oxford.Tack BF, Harrison RA, Janatova J, Thomas ML, Prahl JW. (1980) Evidence for presence of an internal thiolester bond in third component of human complement. Proc Natl Acad Sci U S A. 77:5764-8.Pangburn M.K. and Müller-Eberhard H.J. (1980) Relation of putative thioester bond in C3 to activation of the alternative pathway and the binding of C3b to biological targets of complement. J Exp Med. 152:1102-14.Daha MR, Stuffers-Heiman M, Kijlstra A and Van ES LA. (1979) Isolation and characterization of the third component of rat complement. Immunology 36:63-70... Read More | 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 | H-7 is an inhibitor of the cyclic nucleotide dependent protein kinases PKA and PKC.Protein kinase inhibitor H-7 is a potent inhibitor of protein kinase C (PKC) and cyclic nucleotide dependent protein kinase, with a Ki of 6 µM for PKC | 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 |