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Calmodulin (CaM)

 CALM_BOVIN              Reviewed;         149 AA.
P62157; P02593; P70667; P99014; Q08D84; Q2KJE6; Q61379; Q61380;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
27-SEP-2017, entry version 153.
RecName: Full=Calmodulin;
Short=CaM;
Name=CALM; Synonyms=CAM;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12658628; DOI=10.1002/mrd.10292;
Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H.,
Takahashi T., Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y.,
Tsujimoto G., Izaike Y., Todoroki J., Hashizume K.;
"Characterization of gene expression profiles in early bovine
pregnancy using a custom cDNA microarray.";
Mol. Reprod. Dev. 65:9-18(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus, and Hereford;
TISSUE=Fetal pons, Ileum, and Uterus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 2-149.
TISSUE=Uterus;
Grand R.J.A., Perry S.V.;
"The amino acid sequence of the troponin C-like protein (modulator
protein) from bovine uterus.";
FEBS Lett. 92:137-142(1978).
[4]
PROTEIN SEQUENCE OF 2-149.
TISSUE=Brain;
Kasai H., Kato Y., Isobe T., Kawasaki H., Okuyama T.;
"Determination of the complete amino acid sequence of calmodulin
(phenylalanine-rich acidic protein II) from bovine brain.";
Biomed. Res. 1:248-264(1980).
[5]
PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, AND METHYLATION AT
LYS-116.
TISSUE=Brain;
PubMed=7356670;
Watterson D.M., Sharief F., Vanaman T.C.;
"The complete amino acid sequence of the Ca2+-dependent modulator
protein (calmodulin) of bovine brain.";
J. Biol. Chem. 255:962-975(1980).
[6]
PROTEIN SEQUENCE OF 2-28, AND UBIQUITINATION AT LYS-22.
PubMed=9716384; DOI=10.1046/j.1432-1327.1998.2550422.x;
Laub M., Steppuhn J.A., Blueggel M., Immler D., Meyer H.E.,
Jennissen H.P.;
"Modulation of calmodulin function by ubiquitin-calmodulin ligase and
identification of the responsible ubiquitylation site in vertebrate
calmodulin.";
Eur. J. Biochem. 255:422-431(1998).
[7]
PROTEIN SEQUENCE OF 39-61.
PubMed=3058479; DOI=10.1111/j.1432-1033.1988.tb14420.x;
Pribilla I., Krueger H., Buchner K., Otto H., Schiebler W.,
Tripier D., Hucho F.;
"Heat-resistant inhibitors of protein kinase C from bovine brain.";
Eur. J. Biochem. 177:657-664(1988).
[8]
METHYLATION AT LYS-116.
Weise C.;
Unpublished observations (OCT-2002).
[9]
INTERACTION WITH MYO1C.
PubMed=8022785; DOI=10.1073/pnas.91.14.6349;
Reizes O., Barylko B., Li C., Suedhof T.C., Albenisi J.P.;
"Domain Structure of a mammalian myosin I-beta.";
Proc. Natl. Acad. Sci. U.S.A. 91:6349-6353(1994).
[10]
INTERACTION WITH MYO10.
PubMed=11457842; DOI=10.1074/jbc.M104785200;
Homma K., Saito J., Ikebe R., Ikebe M.;
"Motor function and regulation of myosin X.";
J. Biol. Chem. 276:34348-34354(2001).
[11]
3D-STRUCTURE MODELING OF TRIMETHYLATED CALMODULIN.
PubMed=3375233; DOI=10.1002/prot.340030102;
Strynadka N.C.J., James M.N.G.;
"Two trifluoperazine-binding sites on calmodulin predicted from
comparative molecular modeling with troponin-C.";
Proteins 3:1-17(1988).
[12]
STRUCTURE BY NMR OF 1-75.
PubMed=9305950; DOI=10.1021/bi971022+;
Bentrop D., Bertini I., Cremonini M.A., Forsen S., Luchinat C.,
Malmendal A.;
"Solution structure of the paramagnetic complex of the N-terminal
domain of calmodulin with two Ce3+ ions by 1H NMR.";
Biochemistry 36:11605-11618(1997).
[13]
STRUCTURE BY NMR OF 77-149.
PubMed=8262263; DOI=10.1016/0014-5793(93)80839-M;
Finn B.E., Drakenberg T., Forsen S.;
"The structure of apo-calmodulin. A 1H NMR examination of the carboxy-
terminal domain.";
FEBS Lett. 336:368-374(1993).
[14]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=1519061; DOI=10.1126/science.1519061;
Meador W.E., Means A.R., Quiocho F.A.;
"Target enzyme recognition by calmodulin: 2.4 A structure of a
calmodulin-peptide complex.";
Science 257:1251-1255(1992).
[15]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-148.
PubMed=8259515; DOI=10.1126/science.8259515;
Meador W.E., Means A.R., Quiocho F.A.;
"Modulation of calmodulin plasticity in molecular recognition on the
basis of X-ray structures.";
Science 262:1718-1721(1993).
[16]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 6-148 GLU-85 DEL.
PubMed=8341712; DOI=10.1073/pnas.90.14.6869;
Raghunathan S., Chandross R.J., Cheng B.P., Persechini A.,
Sobottka S.E., Kretsinger R.H.;
"The linker of des-Glu84-calmodulin is bent.";
Proc. Natl. Acad. Sci. U.S.A. 90:6869-6873(1993).
[17]
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
PubMed=7803388; DOI=10.1021/bi00255a006;
Cook W.J., Walter L.J., Walter M.R.;
"Drug binding by calmodulin: crystal structure of a calmodulin-
trifluoperazine complex.";
Biochemistry 33:15259-15265(1994).
[18]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 4-149.
PubMed=7634090; DOI=10.1038/nsb1194-795;
Vandonselaar M., Hickie R.A., Quail J.W., Delbaere L.T.;
"Trifluoperazine-induced conformational change in Ca(2+)-calmodulin.";
Nat. Struct. Biol. 1:795-801(1994).
[19]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-147.
PubMed=9438860; DOI=10.1016/S0969-2126(97)00308-0;
Wall M.E., Clarage J.B., Phillips G.N.;
"Motions of calmodulin characterized using both Bragg and diffuse X-
ray scattering.";
Structure 5:1599-1612(1997).
[20]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 79-149.
PubMed=11320306; DOI=10.1107/S090744490100347X;
Olsson L.L., Sjolin L.;
"Structure of Escherichia coli fragment TR2C from calmodulin to 1.7 A
resolution.";
Acta Crystallogr. D 57:664-669(2001).
-!- FUNCTION: Calmodulin mediates the control of a large number of
enzymes, ion channels, aquaporins and other proteins by Ca(2+).
Among the enzymes to be stimulated by the calmodulin-Ca(2+)
complex are a number of protein kinases and phosphatases. Together
with CCP110 and centrin, is involved in a genetic pathway that
regulates the centrosome cycle and progression through cytokinesis
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with CEP97, CCP110, TTN/titin and SRY.
Interacts with MYO5A and RRAD (By similarity). Interacts with
USP6; the interaction is calcium dependent (By similarity).
Interacts with CDK5RAP2. Interacts with SCN5A. Interacts with RYR1
and RYR2 (By similarity). Interacts with FCHO1. Interacts with MIP
in a 1:2 stoichiometry; the interaction with the cytoplasmic
domains from two MIP subunits promotes MIP water channel closure.
Interacts with ORAI1; this may play a role in the regulation of
ORAI1-mediated calcium transport. Interacts with SYT7 (By
similarity). Interacts with MYO10 and MYO1C (PubMed:11457842,
PubMed:8022785). {ECO:0000250|UniProtKB:P62158,
ECO:0000250|UniProtKB:P62204, ECO:0000269|PubMed:11457842,
ECO:0000269|PubMed:8022785}.
-!- INTERACTION:
Q9LF79:ACA8 (xeno); NbExp=14; IntAct=EBI-397403, EBI-980643;
Q8L517:At4g30490 (xeno); NbExp=4; IntAct=EBI-397403, EBI-4439046;
Q14451:GRB7 (xeno); NbExp=2; IntAct=EBI-397403, EBI-970191;
P23711:Hmox2 (xeno); NbExp=3; IntAct=EBI-397403, EBI-2910092;
P02788:LTF (xeno); NbExp=2; IntAct=EBI-397403, EBI-1058602;
P29476:Nos1 (xeno); NbExp=2; IntAct=EBI-397403, EBI-349460;
Q62600:Nos3 (xeno); NbExp=2; IntAct=EBI-397403, EBI-7052018;
Q96PH1-4:NOX5 (xeno); NbExp=3; IntAct=EBI-397403, EBI-7305642;
Q13586:STIM1 (xeno); NbExp=2; IntAct=EBI-397403, EBI-448878;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, spindle.
Cytoplasm, cytoskeleton, spindle pole. Note=Distributed throughout
the cell during interphase, but during mitosis becomes
dramatically localized to the spindle poles and the spindle
microtubules. {ECO:0000250}.
-!- PTM: Ubiquitination results in a strongly decreased activity.
{ECO:0000269|PubMed:9716384}.
-!- PTM: Phosphorylation results in a decreased activity.
{ECO:0000250}.
-!- MISCELLANEOUS: This protein has four functional calcium-binding
sites.
-!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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EMBL; AB099053; BAC56543.1; -; mRNA.
EMBL; BC105380; AAI05381.1; -; mRNA.
EMBL; BC120080; AAI20081.1; -; mRNA.
EMBL; BC123890; AAI23891.1; -; mRNA.
PIR; A90719; MCBO.
RefSeq; NP_001039714.1; NM_001046249.2.
RefSeq; NP_001229501.1; NM_001242572.1.
RefSeq; NP_001229516.1; NM_001242587.1.
UniGene; Bt.12896; -.
UniGene; Bt.53264; -.
UniGene; Bt.61778; -.
UniGene; Bt.63542; -.
PDB; 1A29; X-ray; 2.74 A; A=2-149.
PDB; 1AK8; NMR; -; A=1-76.
PDB; 1CDM; X-ray; 2.00 A; A=5-148.
PDB; 1CM1; X-ray; 2.00 A; A=2-149.
PDB; 1CM4; X-ray; 2.00 A; A=2-149.
PDB; 1CMF; NMR; -; A=77-149.
PDB; 1CMG; NMR; -; A=77-149.
PDB; 1DEG; X-ray; 2.90 A; A=6-148.
PDB; 1FW4; X-ray; 1.70 A; A=79-149.
PDB; 1LIN; X-ray; 2.00 A; A=2-149.
PDB; 1PRW; X-ray; 1.70 A; A=2-149.
PDB; 1QIV; X-ray; 2.64 A; A=2-149.
PDB; 1QIW; X-ray; 2.30 A; A/B=2-149.
PDB; 1XA5; X-ray; 2.12 A; A=2-149.
PDB; 2CLN; Model; -; A=1-149.
PDB; 2F2O; X-ray; 2.17 A; A/B=1-149.
PDB; 2F2P; X-ray; 2.60 A; A/B=1-149.
PDB; 2FOT; X-ray; 2.45 A; A=2-149.
PDB; 3IF7; X-ray; 1.60 A; A=2-149.
PDBsum; 1A29; -.
PDBsum; 1AK8; -.
PDBsum; 1CDM; -.
PDBsum; 1CM1; -.
PDBsum; 1CM4; -.
PDBsum; 1CMF; -.
PDBsum; 1CMG; -.
PDBsum; 1DEG; -.
PDBsum; 1FW4; -.
PDBsum; 1LIN; -.
PDBsum; 1PRW; -.
PDBsum; 1QIV; -.
PDBsum; 1QIW; -.
PDBsum; 1XA5; -.
PDBsum; 2CLN; -.
PDBsum; 2F2O; -.
PDBsum; 2F2P; -.
PDBsum; 2FOT; -.
PDBsum; 3IF7; -.
ProteinModelPortal; P62157; -.
SMR; P62157; -.
BioGrid; 176895; 1.
BioGrid; 544691; 5.
DIP; DIP-36674N; -.
ELM; P62157; -.
IntAct; P62157; 101.
MINT; MINT-1347941; -.
STRING; 9913.ENSBTAP00000036057; -.
BindingDB; P62157; -.
ChEMBL; CHEMBL6092; -.
iPTMnet; P62157; -.
PaxDb; P62157; -.
PeptideAtlas; P62157; -.
PRIDE; P62157; -.
Ensembl; ENSBTAT00000019411; ENSBTAP00000019411; ENSBTAG00000014583.
Ensembl; ENSBTAT00000036194; ENSBTAP00000036057; ENSBTAG00000025644.
GeneID; 100297344; -.
GeneID; 520277; -.
GeneID; 617095; -.
KEGG; bta:100297344; -.
KEGG; bta:520277; -.
KEGG; bta:617095; -.
CTD; 801; -.
CTD; 805; -.
CTD; 808; -.
eggNOG; KOG0027; Eukaryota.
eggNOG; COG5126; LUCA.
GeneTree; ENSGT00760000118901; -.
HOVERGEN; HBG012180; -.
InParanoid; P62157; -.
KO; K02183; -.
OMA; NEVDEMI; -.
OrthoDB; EOG091G0V73; -.
TreeFam; TF300912; -.
Reactome; R-BTA-111932; CaMK IV-mediated phosphorylation of CREB.
Reactome; R-BTA-111933; Calmodulin induced events.
Reactome; R-BTA-111957; Cam-PDE 1 activation.
Reactome; R-BTA-111997; CaM pathway.
Reactome; R-BTA-114608; Platelet degranulation.
Reactome; R-BTA-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
Reactome; R-BTA-163615; PKA activation.
Reactome; R-BTA-180024; DARPP-32 events.
Reactome; R-BTA-1855204; Synthesis of IP3 and IP4 in the cytosol.
Reactome; R-BTA-203615; eNOS activation.
Reactome; R-BTA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
Reactome; R-BTA-2672351; Stimuli-sensing channels.
Reactome; R-BTA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-BTA-4086398; Ca2+ pathway.
Reactome; R-BTA-418359; Reduction of cytosolic Ca++ levels.
Reactome; R-BTA-425561; Sodium/Calcium exchangers.
Reactome; R-BTA-442717; CREB phosphorylation through the activation of CaMKK.
Reactome; R-BTA-442729; CREB phosphorylation through the activation of CaMKII.
Reactome; R-BTA-442745; Activation of CaMK IV.
Reactome; R-BTA-442982; Ras activation uopn Ca2+ infux through NMDA receptor.
Reactome; R-BTA-445355; Smooth Muscle Contraction.
Reactome; R-BTA-451308; Activation of Ca-permeable Kainate Receptor.
Reactome; R-BTA-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-BTA-5218921; VEGFR2 mediated cell proliferation.
Reactome; R-BTA-5576892; Phase 0 - rapid depolarisation.
Reactome; R-BTA-5578775; Ion homeostasis.
Reactome; R-BTA-5607763; CLEC7A (Dectin-1) induces NFAT activation.
Reactome; R-BTA-5626467; RHO GTPases activate IQGAPs.
Reactome; R-BTA-5627123; RHO GTPases activate PAKs.
Reactome; R-BTA-5673001; RAF/MAP kinase cascade.
Reactome; R-BTA-70221; Glycogen breakdown (glycogenolysis).
Reactome; R-BTA-8876725; Protein methylation.
Reactome; R-BTA-936837; Ion transport by P-type ATPases.
Reactome; R-BTA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
EvolutionaryTrace; P62157; -.
PRO; PR:P62157; -.
Proteomes; UP000009136; Chromosome 10.
Proteomes; UP000009136; Chromosome 18.
Bgee; ENSBTAG00000014583; -.
GO; GO:0005737; C:cytoplasm; IDA:CAFA.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0043234; C:protein complex; IDA:CAFA.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; IDA:CAFA.
GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0006936; P:muscle contraction; TAS:Reactome.
GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; TAS:Reactome.
CDD; cd00051; EFh; 2.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF13499; EF-hand_7; 2.
SMART; SM00054; EFh; 4.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 4.
PROSITE; PS50222; EF_HAND_2; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Calcium; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Isopeptide bond;
Metal-binding; Methylation; Phosphoprotein; Reference proteome;
Repeat; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7356670,
ECO:0000269|PubMed:9716384,
ECO:0000269|Ref.3, ECO:0000269|Ref.4}.
CHAIN 2 149 Calmodulin.
/FTId=PRO_0000198222.
DOMAIN 8 43 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 44 79 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 81 116 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 117 149 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 21 32 1.
CA_BIND 57 68 2.
CA_BIND 94 105 3.
CA_BIND 130 141 4.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:7356670}.
MOD_RES 22 22 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P0DP23}.
MOD_RES 45 45 Phosphothreonine; by CaMK4.
{ECO:0000250|UniProtKB:P0DP29}.
MOD_RES 82 82 Phosphoserine.
{ECO:0000250|UniProtKB:P0DP23}.
MOD_RES 95 95 N6-acetyllysine.
{ECO:0000250|UniProtKB:P0DP23}.
MOD_RES 100 100 Phosphotyrosine.
{ECO:0000250|UniProtKB:P0DP23}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000250|UniProtKB:P0DP23}.
MOD_RES 111 111 Phosphothreonine.
{ECO:0000250|UniProtKB:P0DP23}.
MOD_RES 116 116 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:7356670,
ECO:0000269|Ref.8}.
MOD_RES 116 116 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:P0DP23}.
MOD_RES 139 139 Phosphotyrosine.
{ECO:0000250|UniProtKB:P0DP23}.
CROSSLNK 22 22 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P0DP23}.
CROSSLNK 22 22 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:9716384}.
HELIX 7 20 {ECO:0000244|PDB:3IF7}.
TURN 21 23 {ECO:0000244|PDB:1CM4}.
STRAND 25 28 {ECO:0000244|PDB:3IF7}.
HELIX 30 39 {ECO:0000244|PDB:3IF7}.
HELIX 46 56 {ECO:0000244|PDB:3IF7}.
STRAND 61 65 {ECO:0000244|PDB:3IF7}.
HELIX 66 75 {ECO:0000244|PDB:3IF7}.
STRAND 79 82 {ECO:0000244|PDB:1QIW}.
HELIX 83 93 {ECO:0000244|PDB:3IF7}.
STRAND 98 101 {ECO:0000244|PDB:3IF7}.
HELIX 103 112 {ECO:0000244|PDB:3IF7}.
HELIX 119 129 {ECO:0000244|PDB:3IF7}.
STRAND 131 138 {ECO:0000244|PDB:3IF7}.
HELIX 139 146 {ECO:0000244|PDB:3IF7}.
SEQUENCE 149 AA; 16838 MW; 6B4BC3FCDE10727B CRC64;
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE
EVDEMIREAD IDGDGQVNYE EFVQMMTAK


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MCA5125Z MOUSE ANTI HUMAN CALMODULIN Azide free, Product Type Monoclonal Antibody, Specificity CALMODULIN, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG1, Applications IF, Clone 3F4 0.1 mg
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EIAAB05236 Calmodulin-regulated spectrin-associated protein 1-like protein 1,Calmodulin-regulated spectrin-associated protein 2,Camsap1l1,Camsap2,Kiaa1078,Mouse,Mus musculus
orb70537 Calmodulin Dependent Protein Kinase 2-g (345-358) peptide This is Calmodulin Dependent Protein Kinase 2-g (345-358) peptide. For research use only. 1 mg
orb71484 Calmodulin-Dependent Protein Kinase 2 (281-309) peptide This is Calmodulin-Dependent Protein Kinase 2 (281-309) peptide. For research use only. 1 mg
orb70539 Calmodulin-Dependent Protein Kinase 2 (281-289) peptide This is Calmodulin-Dependent Protein Kinase 2 (281-289) peptide. For research use only. 1 mg
orb71485 Calmodulin-Dependent Protein Kinase 2 (290-309) peptide This is Calmodulin-Dependent Protein Kinase 2 (290-309) peptide. For research use only. 1 mg


 

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