| Description | Reconstitution: After centrifugation, we suggest addition of 50 mM Na Acetate, pH 5.5, with 150 mM NaCl to the original volume, followed by gentle mixing to ensure adequate homogenization.This enzyme degrades elastin, collagen, and proteoglycan and has been implicated in the development of pulmonaryReconstitution: After centrifugation, we suggest addition of 50 mM Na Acetate, pH 5.5, with 150 mM NaCl to the original volume, followed by gentle mixing to ensure adequate homogenization.This enzyme degrades elastin, collagen, and proteoglycan and has been implicated in the development of pulmonary emphesema and rheumatoid arthritis.Activity: 20-22 units per mg protein. One unit is defined as the amount of enzyme that hydrolyzes one umole of MeO-Suc-Ala-Ala-Pro-Val-pNA per minute at 25℃, pH 7.5. Product Citations:Mittendorf, Elizabeth A., Gheath Alatrash, Na Qiao, Yun Wu, Pariya Sukhumalchandra, Lisa S. St John, Anne V. Philips et al. "Breast cancer cell uptake of the inflammatory mediator neutrophil elastase triggers an anticancer adaptive immune response." Cancer research 72, no. 13 (2012): 3153-3162van den Berg, Carmen W., et al. "Mechanism of Neutrophil Dysfunction: Neutrophil Serine Proteases Cleave and Inactivate the C5a Receptor." The Journal of Immunology 192.4 (2014): 1787-1795.Edwards, J. Vincent, Nicolette Prevost, Kandan Sethumadhavan, Abul Ullah, and Brian Condon. "Peptide conjugated cellulose nanocrystals with sensitive human neutrophil elastase sensor activity." Cellulose (2013): 1-13.Valdez C, Wong YC, Schwake M, Bu G, Wszolek ZK, Krainc D.Progranulin-mediated deficiency of cathepsin D results in FTD and NCL-like phenotypes in neurons derived from FTD patients.Hum Mol Gen. 2017. 2017 Sep 25. doi:10.1093/hmg/ddx364Kerros C, et al.Neuropilin-1 mediates neutrophil elastase uptake and cross-presentation in breast cancer cells.J Biol Chem. 2017 Jun 16;292(24):10295-10305. doi: 10.1074/jbc.M116.773051. Epub 2017 May 3.Martin KR, Kantari-Mimoun C, Yin M, Pederzoli-Ribeil M, et al.Proteinase 3 Is a Phosphatidylserine-binding Protein That Affects the Production and Function of Microvesicles.J Biol Chem. 2016 May 13;291(20):10476-89. doi: 10.1074/jbc.M115.698639. Epub 2016 Mar 9.Edwards JV, Fontenot KR, Prevost NT, Pircher N, Liebner F, Condon BD.Preparation, Characterization and Activity of a Peptide-Cellulosic Aerogel Protease Sensor from Cotton.Sensors (Basel). 2016 Oct 26;16(11). pii: E1789.Chawla A, Alatrash G, Philips AV, Qiao N, et al.Neutrophil elastase enhances antigen presentation by upregulating human leukocyte antigen class I expression on tumor cells.Cancer Immunol Immunother. 2016 Jun;65(6):741-51. doi: 10.1007/s00262-016-1841-6. Epub 2016 Apr 29.Sinden NJ, et al.α-1-Antitrypsin variants and the proteinase/antiproteinase imbalance in chronic obstructive pulmonary disease.Am J Physiol Lung Cell Mol Physiol. 2015 Jan 15;308(2):L179-90.Ksiazek M, et al.Miropin, a Novel Bacterial Serpin from the Periodontopathogen Tannerella forsythia, Inhibits a Broad Range of Proteases by Using Different Peptide Bonds within the Reactive Center Loop.J Biol Chem. 2015 Jan 2;290(1):658-70. doi: 10.1074/jbc.M114.601716. Epub 2014 Nov 11.Ramadass M, Ghebrehiwet B, Kew RR.Enhanced recognition of plasma proteins in a non-native state by complement C3b. A possible clearance mechanism for damaged proteins in blood.Mol Immunol. 2015 Mar;64(1):55-62. doi: 10.1016/j.molimm.2014.10.022. Epub 2014 Nov 15.Thomas MP, et al.Leukocyte Protease Binding to Nucleic Acids Promotes Nuclear Localization and Cleavage of Nucleic Acid Binding Proteins.J Immunol. 2014 Jun 1;192(11):5390-7. doi: 10.4049/jimmunol.1303296. Epub 2014 Apr 25.Ungurs MJ, Sinden NJ, Stockley RA.Progranulin is a substrate for neutrophil-elastase and proteinase-3 in the airway and its concentration correlates with mediators of airway inflammation in COPDAm J Physiol Lung Cell Mol Physiol. 2014 Jan 1;306(1):L80-7. doi: 10.1152/ajplung.00221.2013. Epub 2013 Nov 1.Sinden NJ, Koura F, Stockley RA.The significance of the F variant of alpha-1-antitrypsin and unique case report of a PiFF homozygote.BMC Pulm Med. 2014 Aug 7;14:132. doi: 10.1186/1471-2466-14-132.Kenninston JA, et al.Inhibition of Plasma Kallikrein by a Highly Specific Active Site Blocking Antibody.J Biol Chem. 2014 Aug 22;289(34):23596-608. doi: 10.1074/jbc.M114.569061. Epub 2014 Jun 26.Tejera P, et al.Functional Characterization of Polymorphisms in the Peptidase Inhibitor 3 (Elafin) Gene and Validation of Their Contribution to Risk of Acute Respiratory Distress Syndrome.Am J Respir Cell Mol Biol. 2014 Aug;51(2):262-72. doi: 10.1165/rcmb.2013-0238OC.Zheng K, et al.Influence of glycosylation pattern on the molecular properties of monoclonal antibodies.MAbs. 2014 May-Jun;6(3):649-58. doi: 10.4161/mabs.28588. Epub 2014 Mar 24... 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 | H-7 dihydrochloride blocks human immunodeficiency virus (HIV-1) replication in MOLT-4 (clone No. 8) cell line. It increases the secretion of interleukin 1β (IL-1β).Application：H-7 dihydrochloride has been used to study H-7-induced inhibition of contractility in rat embryo H-7 dihydrochloride blocks human immunodeficiency virus (HIV-1) replication in MOLT-4 (clone No. 8) cell line. It increases the secretion of interleukin 1β (IL-1β).Application：H-7 dihydrochloride has been used to study H-7-induced inhibition of contractility in rat embryo fibroblasts (REF52) cells and acts as a kinase inhibitor... Read More | Purity> 97 % by SDS-PAGE and HPLC analyses.Additional sequence informationMature protein.FunctionPromotes neurite outgrowth and especially branching of neuritic processes in primary hippocampal and cortical cells | Purity:>85%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：mCherry is a bright red monomeric fluorescent protein created by rounds of directed evolution of DsRed. mCherry matures rapidly, making it possible to see results very soon after transfection or activation Purity:>85%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：mCherry is a bright red monomeric fluorescent protein created by rounds of directed evolution of DsRed. mCherry matures rapidly, making it possible to see results very soon after transfection or activation of transcription. It is highly photostable and resistant to photobleaching (Shaner et al. 2004). As a result, mCherry is now the most widely used and cited red fluorescent protein. mCherry is bright although tdTomato is the brightest commercially available red fluorescent protein... Read More |