Dieses Kaninchen Polyklonal-Antikörper erkennt spezifisch Erythrocyte Ankyrin in WB, IHC und ELISA. Er zeigt eine Reaktivität gegenüber Human, Maus, Ratte und Hund.
ANK1
Reaktivität: Human
WB, IHC, ICC, IF
Wirt: Maus
Monoclonal
S388A-10
Atto 390
Applikationshinweise
ANK1 antibody can be used for detection of ANK1 by ELISA at 1:312500. ANK1 antibody can be used for detection of ANK1 by western blot at 1.25 μg/mL, and HRP conjugated secondary antibody should be diluted 1:50,000 - 100,000.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Lyophilized
Rekonstitution
Add 100 ?L of distilled water. Final antibody concentration is 1 mg/mL.
Konzentration
1 mg/mL
Buffer
Antibody is lyophilized in PBS buffer with 2 % sucrose.
Handhabung
As with any antibody avoid repeat freeze-thaw cycles.
Lagerung
4 °C/-20 °C
Informationen zur Lagerung
For short periods of storage (days) store at 4 °C. For longer periods of storage, store ANK1 antibody at -20 °C.
Ankyrins are a family of proteins that are believed to link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of ankyrin 1 have been described, however, the precise functions of the various isoforms are not known.Ankyrins are a family of proteins that are believed to link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple ankyrin repeats, a central region with a highly conserved spectrin binding domain, and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of ankyrin 1 have been described, however, the precise functions of the various isoforms are not known. Alternative polyadenylation accounting for the different sized erythrocytic ankyrin 1 mRNAs, has also been reported. Truncated muscle-specific isoforms of ankyrin 1 resulting from usage of an alternate promoter have also been identified.