Anti-Ankyrin erytroid/ANK/ANK1 Antibody Picoband® fluoro550 Vervoeging

Ankyrin 1, erythrocytic, also known as ANK1, is a protein that in humans is encoded by the ANK1 gene. Ankyrins are a family of proteins that 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. Truncated muscle-specific isoforms of ankyrin 1 resulting from usage of an alternate promoter have also been identified.

Short transient receptor potential channel 5; TrpC5; Transient receptor protein 5; TRP-5; hTRP-5; hTRP5; TRPC5; TRP5

ANK1

286

P16157

Human, Mouse, Rat

No cross-reactivity with other proteins.

E.coli-derived human Ankyrin erythroid/ANK/ANK1 recombinant protein (Position: N1300-Q1844) .

Expressed in brain with higher levels in fetal brain. Found in cerebellum and occipital pole.

Flow Cytometry

Calcium Channels, Calcium Signaling, Metabolism, Neuroscience, Neurotransmission, Plasma Membrane, Signal Transduction, Signaling Pathway

Immunogen affinity purified.

Liquid

Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Has also been shown to be calcium-selective. May also be activated by intracellular calcium store depletion.

1. Davies, K. A., Lux, S. E. Hereditary disorders of the red cell membrane skeleton. Trends Genet. 5: 222-227, 1989. 2. Duru, F., Gurgey, A., Ozturk, G., Yorukan, S., Altay, C. Homozygosity for dominant form of hereditary spherocytosis. Brit. J. Haemat. 82: 596-600, 1992. 3. Eber, S. W., Gonzalez, J. M., Lux, M. L., Scarpa, A. L., Tse, W. T., Dornwell, M., Herbers, J., Kugler, W., Ozcan, R., Pekrun, A., Gallagher, P. G., Schroter, W., Forget, B. G., Lux, S. E. Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis. Nature Genet. 13: 214-218, 1996.

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

91791 MW

6

Transient receptor potential cation channel subfamily C member 5

Cell membrane. Multi-pass membrane protein.

Rabbit IgG

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.