For Western blotting and immunofluorescence dilutions to be used depend on detection system applied. It is recommended that users test the reagent and determine their own optimal dilutions. The typical starting working dilution is 1:50.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Buffer
PBS, containing 0.1 % bovine serum albumin and 0.02 % sodium azide.
Konservierungsmittel
Sodium azide
Vorsichtsmaßnahmen
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Lagerung
4 °C
Informationen zur Lagerung
Product should be stored at 4 °C. Under recommended storage conditions, product is stable for one year.
Haltbarkeit
12 months
Target
ADAMTS13
(ADAM Metallopeptidase with Thrombospondin Type 1 Motif, 13 (ADAMTS13))
ADAMTS13 antikoerper, ADAM-TS13 antikoerper, ADAMTS-13 antikoerper, C9orf8 antikoerper, VWFCP antikoerper, vWF-CP antikoerper, Gm710 antikoerper, ADAM metallopeptidase with thrombospondin type 1 motif 13 antikoerper, a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 13 antikoerper, ADAM metallopeptidase with thrombospondin type 1 motif, 13 antikoerper, ADAMTS13 antikoerper, Adamts13 antikoerper, adamts13 antikoerper
Hintergrund
The monoclonal antibody 20A5 recognizes human ADAMTS-13, A Disintegrin And Metalloprotease with ThromboSpondin type 1 domain 13. ADAMTS-13 is produced by hepatic stellate cells and in smaller amounts by human endothelial cells, and is present in plasma at a concentration of approximately 1 μg/mL. ADAMTS-13 is a zinc-containing metalloprotease belonging to the ADAMTS family characterized by a protease domain, an adjacent disintegrin-like domain, one or more thrombospondin type 1 repeats, a cystein-rich domain and a typical spacer region. ADAMTS-13 is composed of a series of domains (amino to carboxy terminal): metalloprotease, disintegrin-like, central thrombospondin-1 (TSP-1), cysteine-rich, spacer, seven additional TSP-1 domains and two unique CUB domains. ADAMTS-13 has no hydrophobic transmembrane domain, and hence it is not anchored in the cell membrane. The apparent molecular weight is 170 or 190 kDa on non-reducing or reducing SDS-PAGE, respectively. ADAMTS-13 has an important function in haemostasis, where it catalyzes the cleavage of the peptide bond between tyrosine-1605 and methionine-1606 in the A2 domain of von Willebrand Factor (VWF), resulting in 2 electrophoretic reduced fragments of 176 and 140 kDa, respectively. This process renders large multimers less adhesive and hence less reactive in the setting of thrombus formation. ADAMTS-13 is therefore said to be a natural anti-thrombotic agent. Severe ADAMTS-13 deficiency is associated with systemic microvascular thrombosis in familial or acquired thrombotic thrombocytopenic purpura (TTP). The accumulation of non-cleaved large VWF multimers causes spontaneous systemic platelet aggregation blocking oxygen supply to vital organs. This life-threatening disorder can lead to ischemic disease with (multiple) organ failure. The monoclonal antibody 20A5 recognizes the central to C-terminal TSP-1 repeats 2 to 5 of ADAMTS- 13 (amino acid 686-894). Aliases Von Willebrand Factor-Cleaving Protease (VWFCP)