| Description | CYP3A43 Human Pre-designed siRNA Set A contains three designed siRNAs for CYP3A43 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components CYP3A43 siRNA-1: 5 nmol (HPLC) CYP3A43 siRNA-2: 5 nmol (HPLC) CYP3A43 siRNA-3: 5 nmol (HPLC) siRNA CYP3A43 Human Pre-designed siRNA Set A contains three designed siRNAs for CYP3A43 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components CYP3A43 siRNA-1: 5 nmol (HPLC) CYP3A43 siRNA-2: 5 nmol (HPLC) CYP3A43 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 | C1q separated from C1r and C1s and from other stabilizing proteins tends to aggregate easily. Because it was isolated and studied in numerous research laboratories, many buffers have been used to stabilize concentrated C1q and prevent aggregation. About half of the scientists prefer high salt and C1q separated from C1r and C1s and from other stabilizing proteins tends to aggregate easily. Because it was isolated and studied in numerous research laboratories, many buffers have been used to stabilize concentrated C1q and prevent aggregation. About half of the scientists prefer high salt and the other prefer 40% glycerol in the storage buffer.C1q is purified from pooled normal human plasma. C1q is part of the C1 complex and this complex is the first complement component in the cascade referred to as the classical pathway of complement. C1 is actually 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. When antibodies bind to antigens forming immune complexes they cluster allowing two or more of its six arms of C1q to bind to the Fc domains of antibodies such as IgG or IgM. The binding of multiple arms to immune complexes causes the two C1r proteins in the complex (protease zymogens) to auto-activate producing two C1r proteases that cleave and activate the two C1s protease zymogens in the complex. 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 which is the C3/C5 convertase of the classical pathway.Extinction Coeff.A₂₈₀ nm = 0.68 at 1.0 mg/ml for pure C1q Molecular weight:410,000 Da (18 chains)Preservative:None, 0.22 µm filtered.Source:Normal human serum (shown by certified tests to be negative for HBsAg, HTLV-I/II, STS, and for antibodies to HCV, HIV-1 and HIV-II).Physical Characteristics & StructureC1q is a high molecular weight complex of 18 polypeptide chains. Each of the six arms of C1q contains three chains, an A chain (26,000 daltons), a B chain (25,000 daltons) and a C chain (24,000 daltons). The three chains are coiled into a collagen-like triple helix over approximately half their length. Half of this collagen region forms a central core where all 18 chains come together. The chains are joined in this core by disulfides in the pattern A-B and C-C. There is a bend in the center of the collagen region allowing the arms to extend away from each other. Globular heads at the far ends of the collagen arms possess binding sites for Fc domains of immunoglobulins. C1 complex is composed of one C1q molecule (410,000 daltons), two C1r molecules (92,000 daltons) and two C1s molecules (86,000 daltons). The complex is stable in the presence of calcium, but easily dissociates if calcium is removed. When C1 is activated the C1r and C1s subunits are each cleaved into two chain molecules due to proteolytic activation. Thus, the SDS gel pattern of C1 is very complex. Function The biological functions of C1q are described above in the General Description and Physical Characteristics sections. C1q functional activity may be assayed using C1q-depleted serum and EA cells. These assays are extremely sensitive to C1q typically yielding 50% lysis with less than 2 ng C1q in assays measuring the lysis of EA cells. AssaysThe unit of classical pathway activity is the CH50. A similar unit, the C1qH50, is used to quantitate the activity of C1q. A C1qH50 unit is the amount of functional C1q needed to lyse 50% of 3×10^7 EA cells (antibody-sensitized sheep erythrocytes) when that amount of C1q is incubated with 5-20 µL of C1q-Dpl in GVB++ in a total volume of 500 µL for 30 min at 37℃. This amount of C1q indicates the sensitivity of the assay for C1q which is typically about 1 ng C1q with 10 µL C1q-Dpl. See the Certificate of Analysis for lot specific values.ApplicationsC1q is used to coat ELISA plates to capture and quantitate immune complexes in clinical samples. A number of commercial companies sell diagnostic kits for immune complex detection and quantitation. These kits are based on the ability of C1q to bind well to immune complexes, but to not bind significantly to monomeric immunoglobulins. GeneticsThe EMBL/Genbank cDNA accession numbers are: C1q A chain (P02745), C1q B chain (P02746), and C1q C chain (P02747). The genes for C1q chains A, B and C are all located on chromosome 1p in the order A-C-B. DeficienciesDeficiencies of each of the three components of C1 have been found. Patients lacking C1q generally have immune-complex-mediated renal disease and skin lesions. Like all patients lacking early classical pathway components C1q deficient individuals are prone to systemic lupus erythrematosis (SLE) and recurrent pyogenic infections. They lack classical pathway function and may or may not exhibit C1q antigen in blood.DiseasesSee section titled Deficiencies above. Precautions/Toxicity/HazardsThis protein is purified from human serum and therefore precautions appropriate for handling any blood-derived product must be used even though the source was shown by certified tests to be negative for HBsAg, HTLV-I/II, STS, and for antibodies to HCV, HIV-1 and HIV-II... Read More | Product DescriptionEndo F1 cleaves Asparagine-linked high mannose and some hybrid oligosaccharides. Core fucosylation reduces the activity by 50 fold. Endoglycosidase F1 will hydrolyze sulfate containing high-mannose chains. It cleaves between the two N-acetylglucosamine residues in the Product DescriptionEndo F1 cleaves Asparagine-linked high mannose and some hybrid oligosaccharides. Core fucosylation reduces the activity by 50 fold. Endoglycosidase F1 will hydrolyze sulfate containing high-mannose chains. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide, generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. In contrast, PNGase F removes the oligosaccharide intact.Molecular weight 32,000 daltonsContents60 µl aliquot of enzyme (1 U) in 20 mM Tris-HCl, pH 7.5Included with 20 µL and 60 µL pack sizes:5x Reaction Buffer – 250 mM sodium phosphate, pH 5.5Specific ActivityDefined as the amount of enzyme required to catalyze the release of N-linked oligosaccharides from 1 micromole of denatured Ribonuclease B (RNase B) in 1 minute at 37°C, pH 5.5. Cleavage is monitored by SDS-PAGE (cleaved RNase B migrates faster).FormulationThe enzyme is provided as a sterile-filtered solution in 20 mM Tris-HCl, pH 7.5StabilitySeveral days exposure to ambient temperatures will not reduce activity. Stable at least 12 months when stored properly. SpecificityEndo F1 cleaves Asparagine-linked high mannose or hybrid oligosaccharides. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide, generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. In contrast, PNGase F removes the oligosaccharide intact. Quality & PurityEndo F1 is tested for contaminating protease as follows: 10 µg of denatured BSA is incubated at 37°C for 24 hours with 2 µl of enzyme. SDS-PAGE analysis of the treated BSA shows no evidence of degradation. The production host strain has been extensively tested and does not produce any detectable glycosidases.Directions for use1. Add up to 200 µg of glycoprotein to an Eppendorf tube. Adjust to 38 µl final volume with de-ionized water.2. Add 10 µl 5x Reaction Buffer 5.53. Add 2.0 µl of Endo F1 to the reaction. Incubate 1 hour or more at 37°C.Monitor cleavage by SDS-PAGE... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:Monkeypox is a zoonotic disease caused by monkeypox virus (MPXV), which is a member of orthopoxvirus genus. A35R gene is highly conserved among poxviruses and encodes a previously uncharacterized hydrophobic acidicPurity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:Monkeypox is a zoonotic disease caused by monkeypox virus (MPXV), which is a member of orthopoxvirus genus. A35R gene is highly conserved among poxviruses and encodes a previously uncharacterized hydrophobic acidic protein. The A35R has little homology to any protein outside of poxviruses, suggesting a novel virulence Monkeypox is a zoonotic disease caused by monkeypox virus (MPXV), which is a member of orthopoxvirus genus. A35R gene is highly conserved among poxviruses and encodes a previously uncharacterized hydrophobic acidic protein. The A35R has little homology to any protein outside of poxviruses, suggesting a novel virulence mechanism.A35R could block some stage of antigen processing or presentation in infected cells or interfere with regulation of apoptosis. In addition, the A35R function may be required for growth in certain cell types, e.g., macrophage, in vivo. It localizes to factories where viral DNA is located and it was shown to be a constitutive transcriptional activator in a large-scale yeast two-hybrid study... Read More | This reagent kit is based on TRIzon's improved columnar total RNA extraction kit. This product can be extracted from animal groupsExtract total RNA from samples such as textiles, plant materials, various microorganisms, and cultured cells. Firstly, the cracking solution is fully cracked This reagent kit is based on TRIzon's improved columnar total RNA extraction kit. This product can be extracted from animal groupsExtract total RNA from samples such as textiles, plant materials, various microorganisms, and cultured cells. Firstly, the cracking solution is fully cracked andHomogenized samples, in their unique high salt state, RNA specifically binds to silicon matrix membranes, greatly reducingEffectively removing organic solvent contamination while removing protein contamination, resulting in higher purity and quality of RNA. bookThe product can quickly extract total RNA from various cells or tissues, and can process 30-50 mg of tissue or 5 × 10 ⁶ cells each time,Can handle multiple different samples simultaneously. If it is an RNA experiment that is very sensitive to trace amounts of DNA, the residual DNA can be utilizedUsing DNase without RNase for digestion and removal on the column, the extracted RNA can be directly applied to RT-PCR Experiments such as Northern Blot, Dot Blot, and in vitro translation. U665516 Component 50 T Storage U665516A DNase I 1000 U -20℃. Avoid freeze/thaw cycle. U665516B 10×Reaction Buffer 1000 µL -20℃. Avoid freeze/thaw cycle. U665516C TRIzon Reagent 60 mL 2-8℃. Protect from light. U665516D TRIzon PaI™ 10 mL 2-8℃. Protect from light. U665516E Buffer RW1 40 mL RT U665516F Buffer RW2 (concentrate) 11 mL RT U665516G RNase-Free Water 10 mL RT U665516H Spin Columns RM with Collection Tubes 50 sets RT U665516I RNase-Free Centrifuge Tubes (1.5 mL) 50 EA RTPreparation and important precautions before the experiment:1.To prevent RNase pollution, attention should be paid to the following aspects:1) RNase's plastic products and gun heads to avoid cross contamination.2) Prepare the solution using water without RNase.3) Operators should wear disposable masks and gloves, and change gloves frequently during the experiment.2. The sample should avoid repeated freezing and thawing, otherwise it will affect the yield and quality of RNA extraction.3. If TRIzon Reagent is found to have precipitates before use, it can be dissolved in a water bath at 56 ℃ for a few minutes.Before the first use, anhydrous ethanol should be added to Buffer RW2 according to the instructions on the reagent bottle label.5. All centrifugation steps should be carried out at room temperature unless otherwise specified, and all operation steps should be carried out quickly.Usage：1. Sample processing1a. Organization: 30-50 mg of tissue is thoroughly ground in liquid nitrogen and 1 mL of TRIzon Reagent is added, or 1 mL of TRIzon Reagent is added to the tissue sample and homogenized. Attention: The sample volume should not exceed 10% of the volume of TRIzon Reagent.2a. Single layer cell culture: Remove the culture medium and add an appropriate amount every 10 cm ² Add 1 mL of TRIzon Reagent.3a. Cell suspension: Collect cells by centrifugation. Add 1 mL of TRIzon Reagent to every 5 × 10 µ m cell.2. After adding TRIzon Reagent, repeatedly blow a few times to fully crack the sample. Leave at room temperature for 5 minutes to completely separate the protein nucleic acid complex.3. Add 200 to every 1 mL of TRIzon Reagent µ LTRIzon PaI ™， Cover the tube tightly, vigorously shake for 15 seconds, and let it sit at room temperature for 2 minutes.4. Centrifuge at 4 ℃ 12000 rpm (~13400 × g) for 10 minutes. At this time, the sample is divided into three layers: the red organic phase, the middle layer, and the upper colorless aqueous phase. RNA is mainly in the upper aqueous phase. Move the upper aqueous phase to a new RNase Free centrifuge tube (provided).5. Add an equal volume of 70% ethanol (prepared without RNase water) to the obtained aqueous solution, invert and mix well.6. Add all the solutions obtained in the previous step to the spin columns RM that have been loaded into the collection tube. If the solution cannot be added at once, it can be transferred in multiple batches. Centrifuge at 12000 rpm for 20 seconds, discard the waste liquid in the collection tube, and place the adsorption column back into the collection tube.7. Add 350 to the adsorption column µ L Buffer RW1, centrifuge at 12000 rpm for 20 seconds, discard the waste liquid in the collection tube, and place the adsorption column back into the collection tube.8. Preparation of DNase I mixture: Take 52 µ LRNase Free Water, add 8 to it µ L 10 x Reaction Buffer and 20 µ L DNase I (1 U/ µ L) Mix well and prepare to a final volume of 80 µ The reaction solution of L.9. Directly add 80 µ L DNase I mixture to the adsorption column and incubate at 20-30 ℃ for 15 minutes.10. Add 350 to the adsorption column µ L Buffer RW1, centrifuge at 12000 rpm for 1 minute, discard the waste liquid, and place the adsorption column back into the recovery manifold.11. Add 500 to the adsorption column µ L Buffer RW2 (check if anhydrous ethanol has been added before use), centrifuge at 12000 rpm for 20 seconds, discard the waste liquid in the collection tube, and place the adsorption column back into the collection tube.12. Repeat step 11.Centrifuge at 12000 rpm for 2 minutes and discard the waste liquid from the collection tube. Place the adsorption column at room temperature for a few minutes and thoroughly air dry. Attention: The purpose of this step is to remove residual ethanol from the adsorption column, which will affect subsequent enzymatic reactions (enzyme digestion,. )PCR, etc.14. Place the adsorption column in a new RNase free centrifuge tube and add 30-50 to the middle of the adsorption column µ Place RNase Free Water at room temperature for 1 minute, centrifuge at 12000 rpm for 1 minute, collect RNA solution, and store RNA at -70 ℃ to prevent degradation.Attention:1) The volume of RNase Free Water should not be less than 30 µ L. Small volume affects the recovery rate.2) If you want to increase RNA production, you can use 30-50 µ Repeat step 14 for the new RNase Free Water.3) If you want to increase the RNA concentration, you can add the obtained solution back to the adsorption column and repeat step 14... Read More |