| Description | ACAT1 Human Pre-designed siRNA Set A contains three designed siRNAs for ACAT1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ACAT1 siRNA-1: 5 nmol (HPLC) ACAT1 siRNA-2: 5 nmol (HPLC) ACAT1 siRNA-3: 5 nmol (HPLC) siRNA Negative Control:ACAT1 Human Pre-designed siRNA Set A contains three designed siRNAs for ACAT1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ACAT1 siRNA-1: 5 nmol (HPLC) ACAT1 siRNA-2: 5 nmol (HPLC) ACAT1 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 = 0.631 at 1.0 mg/ml for pure C1qMolecular Weight400,000 Da (18 chains)General DescriptionRat C1q is purified from pooled normal rat serum. C1q is part of the C1 complex, which is the first complement component in the classical pathway of Protein Purity≥85% by SDS PAGEExtinction CoeffA280 nm = 0.631 at 1.0 mg/ml for pure C1qMolecular Weight400,000 Da (18 chains)General DescriptionRat C1q is purified from pooled normal rat serum. C1q is part of the C1 complex, which is the first complement component in the classical pathway of complement. The C1 complex is a non-covalent assembly of three different proteins (C1q, C1r, and C1s) bound together in a calcium-dependent complex. C1q has six extended arms with domains at the end of each arm that bind to the Fc domains of immunoglobulins such as IgG or IgM. When antibodies bind toantigens, forming immune complexes, they cluster allowing two or more of the six C1q arms to bind to the Fc domains of antibodies. Rat IgG2 is very efficient when compared to IgG1 in activating complement (Medgyesi, G.A et., al., 1981). This is in contrast to the human system in which IgG1 activates complement but not IgG2 (Redpath, S. et. al., 1998). The binding of multiple arms of C1q to immune complexes causes the two C1r proteins in the complex (protease zymogens) to auto-activate. The activated C1r proteases cleave and activate the two C1s protease zymogens in the complex. The activated C1s cleaves complement component C4 releasing C4a and initiating covalent attachment of C4b to the activating surface. Activated C1s also cleaves C2 and the larger fragment of C2 binds to the surface-attached C4b forming C4b,C2a, the C3/C5 convertase of the classical pathway.Rat IgG1 cannot activate complement whereas rat IgG2 does.Physical Characteristics & StructureThe apparent molecular weight of rat C1q as determined by gel filtration has been reported to be 400,000 by Veerhuis, R. et al., (1985) and is calculated to be 420,000 based on its amino acid sequence. Rat C1q is a high molecular weight complex of 18 polypeptide chains. Each of the six arms of rat C1q contains three chains, an A chain (~30,000 daltons), a B chain (~28,000 daltons) and a C chain (~26,000 daltons) as determined by SDS/polyacrylamide gel electrophoresis (Wing, M.G. et al., (1993)).FunctionThe biological functions of C1q are described above in the General Description and Physical Characteristics sections.ApplicationsRat C1q can be used to coat ELISA plates to capture and quantitate immune complexes in samples from rat models used for studying immune complex related diseases and conditions.GeneticsNCBI Gene ID numbers for rat C1q are: C1q A chain (298566), C1q B chain (29687), and C1q C chain (362634). The genes for C1q chains A, B and C are all located on chromosome 5. The UniprotKB primary accession numbers for rat C1q are: C1q A chain (P31720), C1q B chain (P31721), and C1q C chain (P31722).Precautions/Toxicity/HazardsThis protein is purified from animal plasma/serum and therefore precautions appropriate for handling any animal blood-derived product must be used.ReferencesMedgyesi, G.A et., Miklos, K., Kulics, J., Fust, G., and Gergely, J. Bazin, H. (1981). Classes and subclasses of rat antibodies: reaction with the antigen and interaction of the complex with the complement system. Immunology 43, 171-176.Redpath, S., Michaelsen, T., Sandlie, I. and Clark, M. R. (1998). Activation of complement by human IgG1 and human IgG3 antibodies against the human leucocyte antigen CD52. Immunology 93, 595–600.Veerhuis, R., Van Es, L.A. and Daha, M.R. (1985). In vivo degradation of rat C1q induced by intravenous injection of soluble IgG aggregates. Immunology 54, 801-810.Wing, M.G., Seilly, D. J., Bridgman, D.J. and Harrison, R.A. (1993). Rapid isolation and biochemical characterization of rat C1 and C1q. Molecular Immunology 30, 433-440... 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 | Lipase PS is generally used in the enantioselective transesterification and hydrolysis. Applications include: 1.Lipase catalyzed transesterification of prochiral pyrimidine acyclonucleoside. 2.Lipase catalyzed hydrolysis of diacetylated pyrimidine acyclonucleosides. 3. Enantiomer selective acylationLipase PS is generally used in the enantioselective transesterification and hydrolysis. Applications include: 1.Lipase catalyzed transesterification of prochiral pyrimidine acyclonucleoside. 2.Lipase catalyzed hydrolysis of diacetylated pyrimidine acyclonucleosides. 3. Enantiomer selective acylation of racemic alcohols in continuous-flow bioreactors... Read More | Ribonuclease T1 is an endoribonuclease, highly specific for the cleavage of RNA or deaminated RNA between guanosine 3'-phosphate residues (or inosine 3'-phosphate) and the 5'-OH residues of adjacent nucleotides with the formation of the corresponding intermediate 2', 3'-cyclic phosphates. It cleavesRibonuclease T1 is an endoribonuclease, highly specific for the cleavage of RNA or deaminated RNA between guanosine 3'-phosphate residues (or inosine 3'-phosphate) and the 5'-OH residues of adjacent nucleotides with the formation of the corresponding intermediate 2', 3'-cyclic phosphates. It cleaves single-stranded RNA releasing oligonucleotides from the guanosine 3'-phosphate termini. The enzyme has a molecular weight of 11 kDa. The optimum pH is 7.5. RNase T1 is inhibited by Ag+, Zn2+, Cu2+, and Hg2+ at 1 X 10-3 M. The stimulatory effects of both histidine and EDTA are attributed to chelation of contaminating inhibitor cations. The enzyme assay is essentially the method of Egami et al., Prog. in Nucleic Acid Res. and Molec. Biol., III, 59 (1964) based upon the release of acid soluble oligonucleotides following the digestion of yeast RNA.Ribonuclease T1 (RNase T1) from Aspergillus oryzae is used to digest denatured RNA prior to sequencing and is used for protein folding studies. ApplicationRibonuclease T1 has extensive applications in molecular cloning and DNA sequencing. Because of its specificity it has been a commonly used cleavage enzyme for the determination of structure, nearest neighbor frequencies, and RNA sequencing. The enzyme has further application in the preparation of nucleoside 2',3'-cyclic phosphates, the synthesis of oligonucleotides, and the removal of RNA from DNA preparations. The enzyme is also used as a non-mammalian source of RNase in various applications... Read More |