| Description | DNAJB8 Human Pre-designed siRNA Set A contains three designed siRNAs for DNAJB8 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components DNAJB8 siRNA-1: 5 nmol (HPLC) DNAJB8 siRNA-2: 5 nmol (HPLC) DNAJB8 siRNA-3: 5 nmol (HPLC) siRNA Negative DNAJB8 Human Pre-designed siRNA Set A contains three designed siRNAs for DNAJB8 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components DNAJB8 siRNA-1: 5 nmol (HPLC) DNAJB8 siRNA-2: 5 nmol (HPLC) DNAJB8 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 = 0.974 at 1.0 mg/ml for pure C3bMolecular Weight185,000 Da (2 chains)General DescriptionCynomolgus monkey C3 (cyno C3) is purified from pooled normal cynomolgus monkey serum. C3 is central to the activation of all three pathways of Protein Purity≥85% by SDS PAGEExtinction CoeffA280 nm = 0.974 at 1.0 mg/ml for pure C3bMolecular Weight185,000 Da (2 chains)General DescriptionCynomolgus monkey C3 (cyno C3) is purified from pooled normal cynomolgus monkey 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 & StructureCynomolgus monkey C3 is an uncharacterized protein. The calculated molecular weight based on its amino acid sequence is 184,926 daltons similar to that of human C3 (185,000 daltons). Like human C3, cyno C3 is composed of two disulfide-linked chains. Analysis of purified cyno C3 by SDS/polyacrylamide gel electrophoresis under non-reduced conditions shows the mobility of cyno C3 to be similar to that of human C3. Under reduced conditions, the migration of the alpha chain of cyno C3 is comparable to that of human C3 alpha chain (110,000 daltons) while the beta chain migrates slightly ahead of the human C3 beta chain (75,000daltons).The extinction coefficient of cyno C3 is calculated from its amino acid sequence using ProtParam and assumes all pairs of Cys residues form cystines (i.e. a pair of cystine molecules are joined by a disulfide bond). The theoretical pI value for cyno monkey C3 is 6.03. Employing immunoturbidimetric method the serum concentration of cyno C3 has been reported to be 1.27 mg/ml in males and 1.1 mg/ml in female monkeys (Park H-K et al., (2016)). FunctionThe biological functions of C3 are described above in the General Description and Physical Characteristics sections.GeneticsCynomolgus monkey C3 chromosome location 19. The NCBI Gene ID number for Cynomolgus monkey C3 is 102131458 and UniProt accession number is A0A2K5VPN1.Precautions/Toxicity/HazardsThis protein is purified from animal 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.Park H-K, Cho J-W, Lee B-S, Park H, Han J-S, Yang M-J, Im W-J, Park D-Y, Kim W-J, Han SC, Kim Y-B. (2016) Reference values of clinical pathology parameters in cynomolgus monkeys (Macaca fascicularis) used in preclinical studies. Lab Anim Res. 32(2):79-86... Read More | TEV Protease is the 241 amino acid (aa), 27 kDa catalytic domain of the nuclear inclusion a (NIa) protein encoded by the potyvirus, tobacco etch virus (TEV). It may be used in biotechnology to cleave affinity tags from recombinant proteins, either co-translationally orin vitrofollowing purification.TEV Protease is the 241 amino acid (aa), 27 kDa catalytic domain of the nuclear inclusion a (NIa) protein encoded by the potyvirus, tobacco etch virus (TEV). It may be used in biotechnology to cleave affinity tags from recombinant proteins, either co-translationally orin vitrofollowing purification. Its high specificity and activity at a wide range of pH and ionic strength make TEV Protease more versatile than many other proteases used for the same purpose. Unlike factor Xa, enteropeptidase or thrombin, TEV Protease has not been found to cleave at unintended sites, even when present at a high concentration. TEV Protease is a 3C-type protease that cleaves substrates with a consensus sequence of ENLYFQG. Cleavage occurs between Q and G. Since the final aa remains on the cleaved protein where it could potentially affect structure or function, substitution of a variety of aa have been tested. In order of efficiency, S, A, M, Y, D, N, E, K or L may be effectively used in place of G. Several of the remaining aa may also vary, giving a final consensus sequence of ExxYF(M)Q(E)/G(S, A or others) where aa in parenthesis are alternatives and x is any aa. The autocatalytic site of NIa at S2256 has been mutated to an N for improved stability of the protease.Tobacco Etch Virus Protease is a highly site-specific cysteine protease that is found in the tags from fusion proteins. The optimal temperature for cleavage is 30°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of recombinant viral TEV protease, reaction time, or incubation temperature. It can be removed by Ni2+ affinity resin... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： 100B, previously called S100 beta, belongs to the S100 family within the EF-hand superfamily of Ca2+ binding proteins. S100 proteins contain two EF-hand motifs that differ in affinity, separated by a hingePurity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： 100B, previously called S100 beta, belongs to the S100 family within the EF-hand superfamily of Ca2+ binding proteins. S100 proteins contain two EF-hand motifs that differ in affinity, separated by a hinge region with a hydrophobic cleft that is exposed upon Ca2+ binding. S100B is a 91 amino acid (aa) protein, after removal of the initial methionine, and is found as homodimers of 10.4 kDa monomers. Human S100B shares 99%, 98%, 100%, 99% and 97% aa sequence identity with mouse, rat, rabbit, equine and bovine S100B, respectively. Within the S100 family, human S100B shows the highest aa identity (59%) with S100A1. S100B is expressed primarily by astrocytes and oligodendrocytes in the central nervous system, and by Schwann cells in the peripheral nervous system. Ca2+-bound S100B interacts in vitro with at least 20 cytoplasmic proteins, including several structural molecules such as tubulin and GFAP. It can inhibit the phosphorylation of these kinase substrates and others such as tau and neuromodulin. Astrocytes can secrete S100B, which then acts in a cytokine-like manner. Nanomolar concentrations of S100B are secreted constitutively, promote proliferation, and are neurotrophic and anti-apoptotic. Blood levels of S100B reflect extracellular concentrations within the nervous system, and are elevated in Down’s syndrome, Alzheimer’s disease and Tourette’s syndrome, metabolic stress, acute brain injury and brain tumors. Micromolar concentrations of S100B can be destructive and pro-apoptotic; they induce the expression of iNOS, COX-2, IL-1, IL‑6 and TNF-alpha by microglia, astrocytes or neurons. Most extracellular actions of S100B can be mediated by RAGE (receptor for advanced glycation end products), which is also a receptor for other S100 proteins... Read More | Tankyrase-IN-2 (compound 5k) is a potent, selective, and orally active tankyrase inhibitor ( IC 50 s of 10, 7, and 710 nM for TNKS1, TNKS2 as well as PARP1, respectively). Tankyrase-IN-2 has favorable physicochemical profile and pharmacokinetic properties modulating Wnt pathway activity in a Tankyrase-IN-2 (compound 5k) is a potent, selective, and orally active tankyrase inhibitor ( IC 50 s of 10, 7, and 710 nM for TNKS1, TNKS2 as well as PARP1, respectively). Tankyrase-IN-2 has favorable physicochemical profile and pharmacokinetic properties modulating Wnt pathway activity in a colorectal xenograft modelIn VitroTankyrase-IN-2 (1-10000 nM; 24 hours) leads to a dose-dependent increase of tankyrase protein abundance with an EC 50 of 320 nM in DLD1 cells. This is in the same potency range as the value for axin2 increase (EC 50 =319 nM). MCE has not independently confirmed the accuracy of these methods. They are for reference only.IC50& Target:IC50: 10 nM (TNKS1), 7 nM (TNKS2), 710 nM (PARP1)... Read More |