ANKMY1 Polyklonale Antilichaam, PE-Cy5 Vervoeging

Ankyrins are membrane adaptor molecules that play important roles in coupling integral membrane proteins to the spectrin-based cytoskeleton network. Mutations of ankyrin genes lead to severe genetic diseases such as fatal cardiac arrhythmias and hereditary spherocytosis. ANKMY1 (ankyrin repeat and MYND domain containing 1), also known as ZMYND13 or TSAL1, is a 941 amino acid protein that contains seven ANK repeats, three MORN repeats and one MYND-type zinc finger. MORN repeats were first identified in junctophilins, cytoplasmic proteins involved in junctions between the plasma membrane and the ER/SR membrane. The presence of MORN repeats suggests that ANKMY1 may interact with the plasma membrane. The MYND domain consists of a cluster of cysteine and histidine residues, arranged with an invariant spacing to form a potential zinc-binding motif which may be involved in protein-protein interactions. Three isoforms of ANKMY1 exists due to alternative splicing events.

Ankyrin repeat and MYND domain containing 1; Testis specic ankyrin like protein 1; TSAL1; Zinc finger MYND domain containing protein 13; ZMYND13; ANKY1_HUMAN.

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Human

814-941/941

ANKMY1

PE-Cy5

KLH conjugated synthetic peptide derived from human ANKMY1

WB

Purified by Protein A.

488nm/670nm

1µg/µl

WB (1:300-5000)

Aqueous buffered solution containing 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Unmodified

Store at -20°C. Aliquot into multiple vials to avoid repeated freeze-thaw cycles.

51281