Recombinant Human Ankyrin-2 (ANK2), partial

Code
MSDS
Size Pls inquire
Source
Conjugate
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
ANK2
Uniprot NO.
Alternative Names
Ankyrin-2; ANK-2; Ankyrin-B; Brain ankyrin; Non-erythroid ankyrin; ANK2 ANKB
Species
Homo sapiens (Human)
Source
Yeast
Expression Region
968-1156
Target Protein Sequence
FLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGKLHLPTAPPPLNEGESLVSRILQLGPPGTKFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSR
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Storage
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Customer Reviews and Q&A

 Customer Reviews

Target Background

Function(From Uniprot)
Plays an essential role in the localization and membrane stabilization of ion transporters and ion channels in several cell types, including cardiomyocytes, as well as in striated muscle cells. In skeletal muscle, required for proper localization of DMD and DCTN4 and for the formation and/or stability of a special subset of microtubules associated with costameres and neuromuscular junctions. In cardiomyocytes, required for coordinate assembly of Na/Ca exchanger, SLC8A1/NCX1, Na/K ATPases ATP1A1 and ATP1A2 and inositol 1,4,5-trisphosphate (InsP3) receptors at sarcoplasmic reticulum/sarcolemma sites. Required for expression and targeting of SPTBN1 in neonatal cardiomyocytes and for the regulation of neonatal cardiomyocyte contraction rate. In the inner segment of rod photoreceptors, required for the coordinated expression of the Na/K ATPase, Na/Ca exchanger and beta-2-spectrin (SPTBN1). Plays a role in endocytosis and intracellular protein transport. Associates with phosphatidylinositol 3-phosphate (PI3P)-positive organelles and binds dynactin to promote long-range motility of cells. Recruits RABGAP1L to (PI3P)-positive early endosomes, where RABGAP1L inactivates RAB22A, and promotes polarized trafficking to the leading edge of the migrating cells. Part of the ANK2/RABGAP1L complex which is required for the polarized recycling of fibronectin receptor ITGA5 ITGB1 to the plasma membrane that enables continuous directional cell migration.
Gene References into Functions
  1. Cell-autonomous adiposity results from increased cell surface GLUT4 due to ankyrin-B deficiency in humans and mice. PMID:29133412
  2. The authors discovered that the entire 24 ankyrin repeats are inhibited by combinatorial and quasi-independent bindings of multiple disordered segments located in the ankyrin-B/G linkers and tails, suggesting a mechanistic basis for differential regulations of membrane target bindings by ankyrins. PMID:28841137
  3. we support classification of Ankyrin-B p.L1622I as a "mild" loss-of-function variant that may confer arrhythmia susceptibility in the context of secondary risk factors including environment, medication, and/or additional genetic variation. PMID:27298202
  4. Clinical manifestations of ANK2 variants may include QT prolongation and torsades de pointes, often precipitated by strenuous exercise or stress. PMID:27005929
  5. Disruption of Ankyrin B and Caveolin-1 Interaction Sites Alters Na(+),K(+)-ATPase Membrane Diffusion PMID:28988699
  6. Report disease-causing ANK2 variant localized to the membrane-binding domain resulting in reduced ankyrin-B expression and abnormal localization in a First Nations population with a high rate of long QT syndrome. PMID:28196901
  7. VariousANK2mutations are associated with a wide range of phenotypes, including aLQTS, especially with ventricular fibrillation, representing "ankyrin-B" syndrome. PMID:27784853
  8. Rare Variants in ANK2 Associated With Various Inherited Arrhythmia Syndromes. PMID:27818464
  9. The identification and characterization of two functionally distinct ankyrin-B isoforms in heart provide compelling evidence that alternative splicing of the ANK2 gene regulates the fidelity of ankyrin-B interactions with proteins PMID:26109584
  10. the structures of ANK repeats in complex with an inhibitory segment from the C-terminal regulatory domain and with a sodium channel Nav1.2 peptide, are reported. PMID:25383926
  11. Gankyrin plays an essential role in estrogen-driven and GPR30-mediated endometrial carcinoma cell proliferation via the PTEN/PI3K/AKT signaling pathway. PMID:23142288
  12. ankyrin-B linker suppresses activity of the ANK repeat domain through an intramolecular interaction, likely with a groove on the surface of the ANK repeat solenoid, thereby regulating the affinities between ankyrin-B and its binding partners PMID:23569209
  13. Residues 63-73 of cdB3 is also essential for ankyrin binding. PMID:22861190
  14. Ankyrin-B protein in heart failure: identification of a new component of metazoan cardioprotection. PMID:22778271
  15. Reduced ankyrin-B expression or mutations in ankyrin 2 are associated with atrial fibrillation. PMID:21859974
  16. Data show that DAnk2-binding is critical for beta spectrin function in vivo. PMID:20573981
  17. The common genetic variation in the ANK2 gene is modified the physiological variability of the QT interval in the general population. PMID:20031550
  18. The ankyrin-B C-terminal domain determines activity of ankyrin-B/G chimeras PMID:11781319
  19. Loss-of-function (E1425G) mutation in ankyrin-B (also known as ankyrin 2), a member of a family of versatile membrane adapters, causes dominantly inherited type 4 long-QT cardiac arrhythmia in humans PMID:12571597
  20. Data show that L1-cell adhesion molecule interactions with ankyrinB (but not with ankyrinG) are involved in the initial formation of neurites. PMID:14657231
  21. An amphipathic alpha-helix in the divergent regulatory domain of ankyrin-b interacts with the molecular co-chaperone Hdj1/Hsp40. PMID:15075330
  22. interaction between members of the ankyrin and beta-spectrin families previously established in erythrocytes and axon initial segments also occurs in neonatal cardiomyocytes with ankyrin-B and beta(2)-spectrin PMID:15262991
  23. Quantitative analysis of erythrocyte membrane proteins revealed increase in ankyrin from patients with homozygous and heterozygous forms of beta-thalassemia. PMID:15310273
  24. Genotype-negative LQTS patients with a single ANK2 variant displayed nonexertional syncope, U waves, sinus bradycardia, and extracardiac findings. PMID:16253912
  25. study identified T to A transition mutation at position 4,603 in exon 40 resulting in substitution of arginine for tryptophan at amino acid residue 1,535 in regulatory domain of ankyrin-B; this novel mutation may be a cause of type 4 long QT syndrome PMID:16864073
  26. Six novel mutations--4 in ANK2, 1 in KCNQ1, and 1 in SCN5A--were found in the patients with torsades de pointes. PMID:17161064
  27. role of ankyrin-B-dependent protein interactions in regulating cardiac electrogenesis PMID:17242276
  28. Ankyrin-B has a role in cardiac function, cardiac death and premature senescence PMID:17940615
  29. ANK2 mutations were not found to directly cause long QT syndrome. PMID:18052691
  30. the ankyrin-binding site is located on the cytoplasmic face of the InsP(3) receptor, thus validating the feasibility of in vivo ankyrin-InsP(3) receptor interactions. PMID:18275062
  31. Ankyrin B modulates the function of Na,K-ATPase/inositol 1,4,5-trisphosphate receptor signaling microdomain PMID:18303017
  32. ANK2 is subject to alternative splicing that gives rise to unique polypeptides with diverse roles in cardiac function. PMID:18782775
  33. Exon organization and novel alternative splicing of the human ANK2 gene: implications for cardiac function and human cardiac disease PMID:18790697
  34. dysfunction in AnkB-based trafficking pathways causes abnormal sinoatrial node (SAN) electrical activity and sinus node dysfunction. PMID:18832177

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Subcellular Location
Cytoplasm, cytoskeleton. Membrane. Cytoplasm, myofibril, sarcomere, M line. Apical cell membrane. Cell membrane. Cell junction, synapse, postsynaptic cell membrane. Early endosome. Recycling endosome. Lysosome. Mitochondrion. Cytoplasm, myofibril, sarcomere, Z line. Cell membrane, sarcolemma, T-tubule.
Tissue Specificity
Present in plasma membrane of neurons as well as glial cells throughout the brain. Expressed in fetal brain and in temporal cortex of adult brain. Also expressed in the inner segments of rod photoreceptors in retina.
Database Links

HGNC: 493

UNIGENE: Hs.620557

KEGG: hsa:287

STRING: 9606.ENSP00000349588

OMIM: 106410

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