Recombinant Mouse Ankyrin-2 (Ank2), partial

Code
MSDS	MSDS Datasheet
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Source
Conjugate
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Target Background

Product Details

Abbreviation

Ank2

Purity

>85% (SDS-PAGE)

Target Names

Ank2

Uniprot NO.

Q8C8R3

Species

Mus musculus (Mouse)

Source

Yeast

Expression Region

1-3898

Target Protein Sequence

MMNEDAAQKS DSGEKFNGSS QRRKRPKKSD SNASFLRAAR AGNLDKVVEY LKGGIDINTC NQNGLNALHL AAKEGHVGLV QELLGRGSSV DSATKKGNTA LHIASLAGQA EVVKVLVKEG ANINAQSQNG FTPLYMAAQE NHIDVVKYLL ENGANQSTAT EDGFTPLAVA LQQGHNQAVA ILLENDTKGK VRLPALHIAA RKDDTKSAAL LLQNDHNADV QSKMMVNRTT ESGFTPLHIA AHYGNVNVAT LLLNRGAAVD FTARNGITPL HVASKRGNTN MVKLLLDRGG QIDAKTRDGL TPLHCAARSG HDQVVELLLE RKAPLLARTK NGLSPLHMAA QGDHVECVKH LLQYKAPVDD VTLDYLTALH VAAHCGHYRV TKLLLDKRAN PNARALNGFT PLHIACKKNR IKVMELLVKY GASIQAITES GLTPIHVAAF MGHLNIVLLL LQNGASPDVT NIRGETALHM AARAGQVEVV RCLLRNGALV DARAREEQTP LHIASRLGKT EIVQLLLQHM AHPDAATTNG YTPLHISARE GQVDVASVLL EAGAAHSLAT KKGFTPLHVA AKYGSLDVAK LLLQRRAAAD SAGKNGLTPL HVAAHYDNQK VALLLLEKGA SPHATAKNGY TPLHIAAKKN QMQIASTLLN YGAETNTVTK QGVTPLHLAS QEGHTDMVTL LLDKGANIHM STKSGLTSLH LAAQEDKVNV ADILTKHGAD RDAYTKLGYT PLIVACHYGN VKMVNFLLKQ GANVNAKTKN GYTPLHQAAQ QGHTHIINVL LQHGAKPNAT TANGNTALAI AKRLGYISVV DTLKVVTEEV TTTTTTITEK HKLNVPETMT EVLDVSDEEG DDTVTGDGGE YLRPEDLKEL GDDSLPSSQF LDGMNYLRYS LEGGRSDSLR SFSSDRSHTL SHASYLRDSA MIDDTVVIPS HQVSALAKEA ERNSYRLSWG TENLDNVALS SSPIHSGFLV SFMVDARGGA MRGCRHNGLR IIIPPRKCTA PTRVTCRLVK RHRLATMPPM VEGEGLASRL IEVGPSGAQF LGPVIVEIPH FAALRGKERE LVVLRSENGD SWKEHFCDYT EDELNEILNG MDEVLDSPED LEKKRICRII TRDFPQYFAV VSRIKQDSNL IGPEGGVLSS TVVSQVQAVF PEGALTKRIR VGLQAQPMHS ELVKKILGNK ATFSPIVTLE PRRRKFHKPI TMTIPVPKAS SDVMLNGFGG DAPTLRLLCS ITGGTTPAQW EDITGTTPLT FVNECVSFTT NVSARFWLID CRQIQESVAF ASQVYREIIC VPYMAKFVVF AKSHDPIEAR LRCFCMTDDK VDKTLEQQEN FSEVARSRDV EVLEGKPIYV DCFGNLVPLT KSGQHHIFSF FAFKENRLPL FVKVRDTTQE PCGRLSFMKE PKSTRGLVHQ AICNLNITLP IYAKESESDQ EPEEEIGMTS EKNDETESTE TSVLKSHLVN EVPVLASPDL LSEVSEMKQD LIKMTAILTT DVSDKAGSLK VKELAKAGEE EPGEPFEIVE RVKEDLEKVN AILRSGTCMR DEGRARSSQS ERELEEEWVI VSDEEIQEAK QHAPVEIDEH PCIEVRVDRE TKAKVEKDST GLVNYLTDDL NSYTSPHEKK PHTAPEKSGE TSQASAVGKS SESNKGKATS AEEKQSAQKQ LKPGLAIKKP VRRKLKEKQK QKEESSQSSE EKTELKKGSS EESVDEDRGL VPEPLPTAKA TSPLIEETPI GSIKDKVKAL QKRVEDEQKG RSKLPVRVKG KEDVPKRTTP RTHPAVSPSS KSSTSSKAER HSSLSSSAKP ERHTPVSPSS KNEKLSPVSP SAKTERHSPV FSGKPEKHSP GSPSTKNERH SPVSSLKTER HTPGSPSGKT DKRPPVPSSG RTEKHPPVSP GKTEKHLPGS PSIRTPEKPA PGSATGKHEK HLPVSPGKTE KQPPISPTSK TERIEETMSV RELMKAFQSG QDPSKHKTGL FEHKSAKQKQ PQDKSKSRVE KEKGHTVTQR EVTQRETQRI ESQTAKRGQR FQVSAATESR RFRSTTITVG LRMEDPVRER FERTPIIKTP EVVPSVAAEE SHRGSEKIVD EQGDMDFQIS PDRKTSTDFS EVIKQELEDN DKYQQFRLTE DTEKAQVHLD QVITSPFNTA FPLDYMKDEF LPALSLQSGA LGGSSESLKQ EVIAGSPCSS LMEGTPQISS EESYKHEGLA ETPETSPESL SFSPKKSEEQ IGEAKETTKV GTPTDIHSEK ELPITNDITD SSQKQGAGVT RGSEPSTEHS QKEVTQDPHK DVCSKQDGCP ESQSVSLASE VFTEKGSCGE SQLPLVSSAF KTQSESETQE SLTPSEVTKP FPPSDASVKT AEGTEPKPQG AIRSPQGLEL PLPNRDSEVL SPMADESLAV SHKDSLEASP VLEDNSSHKT PDSLEPSPLK ESPCRDSLES SPVEPKMKAG ILPSHFPLPA AIAKTDLVAE VASMRSRLLR DPDGSAEDDS LEQTSLMESS GKSPLSPDTP SSEEVSYEVT PKPSDSSTPK PAVIHECAEE DDSENGEKKR FTPEEEMFKM VTKIKTFDEL EQEAKQKRDY KKEPRQDGSS SASDPDADYS AEVNDEKQMA GTEGEGEVPV LVTSENRKVS SSSSESEPEL TQLSKGADSG LLTEPVIRVQ PPSPLPSSID SNSSPEEATQ FQPIVPKQYT FKMNEEIQEE PATSEDKDCK SHLAEDSQTH SADAADGSDG DLNRETTQPE TCDGHGCETV SPSNSATPVS LGVQSPEHKD VDKPLAIDKD SLAHQDTCEN DREEREFDPS GVESTQADLP NESSSLSSRC AIPEGNESAK EIASPSSPVK VEVTITDQAL ESMPEDCPIQ DSSTTMQTER FAMDVPVSEL AETDENSDPQ IISPYENVPS SSFFSAEPSK IQTDTCHSTV VHSPEVYSVI IRSSPEDVVV TNSSNRTVSG EESHCESHDL ETESEQKSAL WAAQSDAPPL AVAPTASDAA SVTGEQASKV IITKTDADAD SWSEIREDDA AFEARVKEEE QKIFGLMVDR QSQGTTPDTT PARTPTEEGT PTSEQNPFLF QEGKLFEMTR SGAIDMTKRP YADESLHFFQ IGQESNEEAI SEDLKEGATG AEPPQTETTS ESLELSEPKE AMDDEGELLP DDVSEEIEDL PASDANIDSQ VIISASTETP TKEAVSTAVE EPPTTQRSDS LSTVKQTPRP AVPGPVGQLD FSPVTRSVYS GQDDESPESS PEEQKSVIEI PTAPVDNVPS AESKPQIPIR TLPTLVPAPP SAEDESAFSD DFPSSLDEDS KEGGAKPKSK IPVKAPTQRT EWQPSPTDIP LQKTAVPQGQ ETLSRAPDGR SKSESDASSL DAKTKCPVKA RSYIETETES RERAEGFESE SEDGATKPKL FASRLPVKSR STSSSGRPGT SPTRESREHF FDLYRNSIEF FEEISDEASK LVDRLTQSER EQEPPSDDES SSALEVSVIE SLPPVDIEHS APEDIFDTRP IWDESIETMI ERIPDENGHD RAEDPQDEQE RMEERLAYIA DHLGFSWTEL ARELDFTEEQ IHQIRIENPN SLQDQSHALL KYWLERDGKH ATDTILIECL TKINRMDIVH LLETNTEPLQ ERMGRSYAEI EQTITLDHSE GFSVLPDELC AAKEKKEQEA SKESESSDHP PMVSEEDISV GYSTFQDCLP KTEGDSPAAA LSPQMHQEPV QQDFSGKTQD QQEYYVTTPG AEVEDPQKAT AVPDSLCKTP EDISTPPEGT KPCLQTPVTS ERGSPIVQEP EEASEPKEES SPRKTSLVIV ESTDDQSQVF ERLDGDAAFQ KGDDMPDIPP ETVTEEEYVD ENGHTVVKKV TRKIIRRYVS SDGTEKEEVT MQGMPQEPVN IEDGDNYSKV IKRVVLKSDT QQSEDNNE
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

N-terminal His-tagged/Tag-Free
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.

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

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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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

These findings reveal spectrin (alpha/beta) / ankyrin B cytoskeletal and signaling proteins as key regulators of T-type calcium channels expressed in the nervous system. PMID:29720258
Cell-autonomous adiposity results from increased cell surface GLUT4 due to ankyrin-B deficiency in humans and mice. PMID:29133412
We demonstrate that AnkB binds to Rab GTPase Activating Protein 1-Like (RabGAP1L) and recruits it to PI3P-positive organelles, where RabGAP1L inactivates Rab22A, and promotes polarized trafficking to the leading edge of migrating fibroblasts. We further determine that a5b1-integrin depends on an AnkB/RabGAP1L complex for polarized recycling PMID:27718357
The increased incidence of pro-arrhythmogenic Ca(2+) sparks and waves in AnkB(+/-) hearts is due to enhanced CaMKII-mediated RyR phosphorylation, which is caused by higher junctional [Ca(2+)] and consequent local CaMKII activation. PMID:27131508
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
Taken together, these observations reveal that AnkB is required for Prx membrane anchoring and for maintenance of lens fiber cell hexagonal geometry, membrane skeleton organization, and biomechanics. PMID:26538089
that ankyrin-B deficiency results in a metabolic syndrome that combines primary pancreatic beta cell insufficiency with peripheral insulin resistance PMID:26168218
Functional relationships between PIK3C3, dynactin, and AnkB promote axonal transport of organelles and are required for normal axon length. PMID:25533844
These findings identify an interaction between ankyrin-B and both Cav2.1 and Cav2.2 at the amino acid level that is necessary for proper Cav2.1 and Cav2.2 targeting in vivo. PMID:24394417
Ankyrin-B protein in heart failure: identification of a new component of metazoan cardioprotection. PMID:22778271
AnkB reduction alters cardiac Na and Ca transport and enhances the coupled RyR openings, resulting in more frequent Ca sparks and waves although the total SR Ca leak is unaffected. PMID:22406428
Ankyrin-B then interacts with dynactin-4 and dystrophin, whereas dynactin-4 collaborates with dystrophin in coordinating costamere-aligned microtubules PMID:21186323
Ankyrin-B regulates Kir6.2 membrane expression and function in heart. PMID:20610380
Findings highlight the importance of the functional anatomy of the entire atrial distributed pacemaker complex and clearly demonstrate the role of AnkB in cardiac automaticity. PMID:20525877
Defective glycemic regulation through loss of ankyrin-B-dependent stabilization of IP3R is a potential risk factor for type 2 diabetes. PMID:20234002
The ankyrin-B C-terminal domain determines activity of ankyrin-B/G chimeras PMID:11781319
Mice heterozygous for a null mutation in ankyrin-B are haploinsufficient and display arrhythmia similar to humans PMID:12571597
ankyrin-B has a role in Inositol 1,4,5-trisphosphate receptor localization and stability in neonatal cardiomyocytes PMID:14722080
We propose that the ankyrin-B-based complex is a specialized adaptation of cardiomyocytes with a role for cytosolic Ca2+ modulation PMID:16292983
Ankyrin-B has a role in cardiac function, cardiac death and premature senescence PMID:17940615
ANK2 is subject to alternative splicing that gives rise to unique polypeptides with diverse roles in cardiac function. PMID:18782775
aNK2-deficient mice displayed abnormal membrane expression of NCX1, Na+/K+ ATPase, IP3R and Ca(V)1.3. Loss of ank2 promoted slow and irregular Ca2+ release, as well as afterdepolarizations in isolated sinoatrial node cardiomyocytes PMID:19098452
Ankyrin-B thus is an adaptor required for sarcolemmal localization of dystrophin, as well as dynactin-4. PMID:19109891
The results of this study indicate that ankyrin(B) regulates axon guidance via cyclic AMP. PMID:19110015

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Subcellular Location

Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, M line. 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

Detected in eye lens fiber cells (at protein level). In the retina, expressed in the inner segments of rod photoreceptors. Expressed in cardiomyocytes, as well as in skeletal muscles. Also detected in brain and pancreas, as well as in kidney and spleen (a

Database Links

UNIGENE: Mm.220242

KEGG: mmu:109676

STRING: 10090.ENSMUSP00000043765

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