Kininogen, HMW, Human Plasma Plasma Human HMW, Kininogen, Gel Glycine 12% Tris Standard 1

BioVision 1/14 For research use only Kininogen, HMW, Human Plasma CATALOG #: 7300-100 100 µg ALTERNATE NAMES: Alpha-2-thiol proteinase inhibitor, Fitzgerald factor, High molecular weight Kininogen, Williams- Fitzgerald-Flaujeac factor, BDK, KNG, Kininogen-1 heavy chain, Tkinin, Bradykinin, Lysyl-bradykinin, Kininogen-1 light chain, Low molecular weight growth-promoting factor SOURCE: Human Plasma. Shown to be non-reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti- HIV 1 & 2 by FDA approved tests. PURITY: ≥ 95% by SDS-PAGE Kininogen, HMW, Human Plasma 12% Tris Glycine gel MOL. WEIGHT: 120 kDa 1. LMW Standard 2. Kininogen, HMW - 10 µg (reduced / heated) EXTINCTION COEFFICIENT: 0.7 3. Kininogen, HMW - 20 µg (reduced / heated) FORM: Frozen FORMULATION: Frozen in 10 mM Na acetate, pH 5.5 with 250 mM RELATED PRODUCTS: • Kininogen, LMW, Human Plasma (Cat. No. 7301-100) NaCI. • Kallikrein 12 (KLK 12) Antibody (Cat. No. 3720-100) • Kallikrein, Human Plasma (Cat. No. 4093-50) STORAGE CONDITIONS: Store at -70°C or lower. Avoid repeated freezing and • KLK3 (Kallikrein-3), human plasma (Cat. No. 4727-20, -100, -1000) thawing cycles. • Trypsin Activity Colorimetric Assay Kit (Cat. No. K771-100) • Trypsin, Human pancreas (Cat. No. 7292-50) DESCRIPTION : HMW kininogen, synthesized by hepatocytes, is a multifunctional protein. It is • Alpha 1 Antichymotrypsin, Human Plasma (Cat. No. 7293-100) the precursor protein of bradykinin. In addition it is a cofactor in the activation of factor XI, XII, • Serpin E1/PAI-1, human recombinant, (Cat. No. 4731-10, -100, -1000) and prekallikrein and a major extra-cellular cysteine proteinase inhibitor. Kininogens inhibit • Human CellExp™ SERPINA1 /A1AT, human recombinant, (Cat. No. 7235-10) systemic proteases which are thought to have a part in various diseases such as cancer, • Serpin A6 Antibody (Cat. No. 3906-100) muscular dystrophy and joint disease. • Serpin A6 Blocking Peptide (Cat. No. 3906BP-100) • Neuroserpin, human recombinant, (Cat. No. 7181-10, -50) FOR RESEARCH USE ONLY! Not to be used in humans. BioVision Incorporated Tel: 408-493-1800 | Fax: 408-493-1801 155 S. Milpitas Boulevard, Milpitas, CA 95035 USA www.biovision.com | [email protected] .

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Plasma Kallikrein Activation and Inhibition During Typhoid Fever
Plasma Kallikrein Activation and Inhibition during Typhoid Fever Robert W. Colman, … , Cheryl F. Scott, Robert H. Gilman J Clin Invest. 1978;61(2):287-296. https://doi.org/10.1172/JCI108938. Research Article As an ancillary part of a typhoid fever vaccine study, 10 healthy adult male volunteers (nonimmunized controls) were serially bled 6 days before to 30 days after ingesting 105Salmonella typhi organisms. Five persons developed typhoid fever 6-10 days after challenge, while five remained well. During the febrile illness, significant changes (P < 0.05) in the following hematological parameters were measured: a rise in α1-antitrypsin antigen concentration and high molecular weight kininogen clotting activity; a progressive decrease of platelet count (to 60% of the predisease state), functional prekallikrein (55%) and kallikrein inhibitor (47%) with a nadir reached on day 5 of the fever and a subsequent overshoot during convalescence. Despite the drop in functional prekallikrein and kallikrein inhibitor, there was no change in factor XII clotting activity or antigenic concentrations of prekallikrein and the kallikrein inhibitors, C1 esterase inhibitor (C1-̄ INH) and α2-macroglobulin. Plasma from febrile patients subjected to immunoelectrophoresis and crossed immunoelectrophoresis contained a new complex displaying antigenic characteristics of both prekallikrein and C1-̄ INH; the α2-macroglobulin, antithrombin III, and α1-antitrypsin immunoprecipitates were unchanged. Plasma drawn from infected-well subjects showed no significant change in these components of the kinin generating system. The finding of a reduction in functional prekallikrein and kallikrein inhibitor (C1-̄ INH) and the formation of a kallikrein C1-̄ INH complex is consistent with prekallikrein activation in typhoid fever.
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Protection by Recombinant Alpha 1-Antitrypsin Ala357 Arg358 Against Arterial Hypotension Induced by Factor XII Fragment
Protection by recombinant alpha 1-antitrypsin Ala357 Arg358 against arterial hypotension induced by factor XII fragment. M Schapira, … , C Roitsch, M Courtney J Clin Invest. 1987;80(2):582-585. https://doi.org/10.1172/JCI113108. Research Article The specificity of serpin superfamily protease inhibitors such as alpha 1-antitrypsin or C1 inhibitor is determined by the amino acid residues of the inhibitor reactive center. To obtain an inhibitor that would be specific for the plasma kallikrein- kinin system enzymes, we have constructed an antitrypsin mutant having Arg at the reactive center P1 residue (position 358) and Ala at residue P2 (position 357). These modifications were made because C1 inhibitor, the major natural inhibitor of kallikrein and Factor XIIa, contains Arg at P1 and Ala at P2. In vitro, the novel inhibitor, alpha 1-antitrypsin Ala357 Arg358, was more efficient than C1 inhibitor for inhibiting kallikrein. Furthermore, Wistar rats pretreated with alpha 1-antitrypsin Ala357 Arg358 were partially protected from the circulatory collapse caused by the administration of beta- Factor XIIa. Find the latest version: https://jci.me/113108/pdf Rapid Publication Protection by Recombinant a1-Antitrypsin Ala357 Arg358 against Arterial Hypotension Induced by Factor XII Fragment Marc Schapira, Marie-Andree Ramus, Bernard Waeber, Hans R. Brunner, Sophie Jallat, Dorothee Carvallo, Carolyn Roitsch, and Michael Courtney Departments ofPathology and Medicine, Vanderbilt University, Nashville, Tennessee 37232; Division de Rhumatologie, Hbpital Cantonal Universitaire, 1211 Geneve 4, Switzerland; Division d'Hypertension, Centre Hospitalier Universitaire Vaudois, 1011 Lausanne, Switzerland; and Transgene SA, 67000 Strasbourg, France Abstract is not known whether this mechanism induces the symptoms observed in these disease states or whether activation of this The specificity of serpin superfamily protease inhibitors such as pathway merely represents an accompanying phenomenon.
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Confirmation of Pathogenic Mechanisms by SARS-Cov-2–Host
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Recombinant Human Kininogen-1 Protein
Leader in Biomolecular Solutions for Life Science Recombinant Human Kininogen-1 Protein Catalog No.: RP01026 Recombinant Sequence Information Background Species Gene ID Swiss Prot Kininogen-1 (KNG1) is also known as high molecular weight kininogen, Alpha-2- Human 3827 P01042-2 thiol proteinase inhibitor, Fitzgerald factor, Williams-Fitzgerald-Flaujeac factor, which can be cleaved into the following 6 chains:Kininogen-1 heavy chain, T- Tags kinin, Bradykinin, Lysyl-bradykinin, Kininogen-1 light chain, Low molecular weight C-6×His growth-promoting factor. Kininogen-1 is a secreted protein which contains three cystatin domains. HMW-kininogen plays an important role in blood coagulation by Synonyms helping to position optimally prekallikrein and factor XI next to factor XII. As with BDK; BK; KNG many other coagulation proteins, the protein was initially named after the patients in whom deficiency was first observed.Patients with HWMK deficiency do not have a hemorrhagic tendency, but they exhibit abnormal surface-mediated activation of fibrinolysis. Product Information Basic Information Source Purification HEK293 cells > 97% by SDS- Description PAGE. Recombinant Human Kininogen-1 Protein is produced by HEK293 cells expression system. The target protein is expressed with sequence (Gln 19 - Ser 427 ) of human Endotoxin Kininogen-1 (Accession #NP_000884) fused with a 6×His tag at the C-terminus. < 0.1 EU/μg of the protein by LAL method. Bio-Activity Formulation Storage Lyophilized from a 0.22 μm filtered Store the lyophilized protein at -20°C to -80 °C for long term. solution of PBS, pH 7.4.Contact us for After reconstitution, the protein solution is stable at -20 °C for 3 months, at 2-8 °C customized product form or for up to 1 week.
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Position Paper from the Second Maastricht Consensus Conference on Thrombosis
Consensus Document 229 Atherothrombosis and Thromboembolism: Position Paper from the Second Maastricht Consensus Conference on Thrombosis H. M. H. Spronk1 T. Padro2 J. E. Siland3 J. H. Prochaska4 J. Winters5 A. C. van der Wal6 J. J. Posthuma1 G. Lowe7 E. d’Alessandro5,6 P. Wenzel8 D. M. Coenen9 P. H. Reitsma10 W. Ruf4 R. H. van Gorp9 R. R. Koenen9 T. Vajen9 N. A. Alshaikh9 A. S. Wolberg11 F. L. Macrae12 N. Asquith12 J. Heemskerk9 A. Heinzmann9 M. Moorlag13 N. Mackman14 P. van der Meijden9 J. C. M. Meijers15 M. Heestermans10 T. Renné16,17 S. Dólleman18 W. Chayouâ13 R. A. S. Ariëns12 C. C. Baaten9 M. Nagy9 A. Kuliopulos19 J. J. Posma1 P. Harrison20 M. J. Vries1 H. J. G. M. Crijns21 E. A. M. P. Dudink21 H. R. Buller22 Y. M.C. Henskens1 A. Själander23 S. Zwaveling1,13 O. Erküner21 J. W. Eikelboom24 A. Gulpen1 F. E. C. M. Peeters21 J. Douxﬁls25 R. H. Olie1 T. Baglin26 A. Leader1,27 U. Schotten4 B. Scaf1,5 H. M. M. van Beusekom28 L. O. Mosnier29 L. van der Vorm13 P. Declerck30 M. Visser31 D. W. J. Dippel32 V. J. Strijbis13 K. Pertiwi33 A. J. ten Cate-Hoek1 H. ten Cate1 1 Laboratory for Clinical Thrombosis and Haemostasis, 17Institute of Clinical Chemistry and Laboratory Medicine, University Cardiovascular Research Institute Maastricht (CARIM), Maastricht Medical Center Hamburg-Eppendorf, Hamburg, Germany University Medical Center, Maastricht, The Netherlands 18Department of Nephrology, Leiden University Medical Centre, 2 Cardiovascular Research Center (ICCC), Hospital Sant Pau, Leiden, The Netherlands Barcelona, Spain 19Tufts University School
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T-Kininogen 1/2 (F-12): Sc-103886
SANTA CRUZ BIOTECHNOLOGY, INC. T-kininogen 1/2 (F-12): sc-103886 The Power to Question BACKGROUND SOURCE In rats, four types of kininogens are produced, two of which are classical T-kininogen 1/2 (F-12) is an affinity purified goat polyclonal antibody raised high and low molecular weight kininogens and two of which are low molec- against a peptide mapping within an internal region of T-kininogen 2 of rat ular weight-like kininogens, designated T-kininogen 1 and T-kininogen 2. origin. T-kininogen 1 and T-kininogen 2 are 430 amino acid secreted rat proteins that each contain three cystatin domains and have nearly identical functions. PRODUCT Existing in plasma, both T-kininogen 1 and T-kininogen 2 are glycoproteins Each vial contains 200 µg IgG in 1.0 ml of PBS with < 0.1% sodium azide that act as thiol protease inhibitors and also play a role in blood coagulation, and 0.1% gelatin. specifically by helping to optimally position blood coagulation factors. Additionally, T-kininogen 1 and T-kininogen 2 act as precursors of the active Blocking peptide available for competition studies, sc-103886 P, (100 µg peptide Bradykinin and, as such, effect vascular permeability, hypotension peptide in 0.5 ml PBS containing < 0.1% sodium azide and 0.2% BSA). and smooth muscle contraction. APPLICATIONS REFERENCES T-kininogen 1/2 (F-12) is recommended for detection of full length and heavy 1. Furuto-Kato, S., Matsumoto, A., Kitamura, N. and Nakanishi, S. 1985. chain of T-kininogen 1 and 2 of rat origin by Western Blotting (starting dilu- Primary structures of the mRNAs encoding the rat precursors for tion 1:200, dilution range 1:100-1:1000), immunofluorescence (starting dilu- bradykinin and T-kinin.
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Identification of Physicochemical Properties That Modulate Nanoparticle Aggregation in Blood
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The Human in Vivo Biomolecule Corona Onto Pegylated Liposomes
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Ph-Responsive Magnetic Nanospheres for Reversibly Selective Capture and Release of Glycoproteins
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Aberrant Processing of Plasma Vitronectin and High
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