Product: CaMKII Antibody
Catalog: DF2907
Source: Rabbit
Application: WB, IHC, IF/ICC, ELISA(peptide)
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Horse, Sheep, Rabbit, Xenopus
Mol.Wt.: 50kD(α+δ), 60kD(β+γ); 54kD,73kD,63kD,56kD(Calculated).
Uniprot: Q9UQM7 | Q13554 | Q13555 | Q13557
RRID: AB_2840896

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 100ul $280 In stock
 200ul $350 In stock

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Product Info

Source:
Rabbit
Application:
WB 1:1000-3000, IHC 1:200, IF/ICC, ELISA(peptide) 1:20000-1:40000
*The optimal dilutions should be determined by the end user.
Reactivity:
Human,Mouse,Rat
Prediction:
Pig(100%), Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Xenopus(100%)
Clonality:
Polyclonal
Specificity:
CaMKII Antibody detects endogenous levels of total CaMKII.
RRID:
AB_2840896
Cite Format: Affinity Biosciences Cat# DF2907, RRID:AB_2840896.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

Alpha CaMKII; Calcium calmodulin dependent protein kinase II; Calcium/calmodulin dependent protein kinase II alpha B subunit; Calcium/calmodulin dependent protein kinase type II alpha chain; Calcium/calmodulin-dependent protein kinase (CaM kinase) II alpha; Calcium/calmodulin-dependent protein kinase II alpha; Calcium/calmodulin-dependent protein kinase II-alpha; Calcium/calmodulin-dependent protein kinase type II subunit alpha; Calcium/calmodulin-dependent protein kinase type IIA; CaM kinase II alpha chain; CaM kinase II alpha subunit; CaM kinase II subunit alpha; CaMK II alpha subunit; CaMK-II subunit alpha; Camk2a; CAMKA; CaMKII; CaMKIINalpha; EC 2.7.11.17; KCC2A_HUMAN; KIAA0968; MGC123320; MGC139375; MGC155201; mKIAA0968; PK2CDD; PKCCD; R74975; zgc:112538; zgc:123320; Calcium/calmodulin-dependent protein kinase type II subunit alpha; Calcium/calmodulin-dependent protein kinase type II subunit delta; CaM kinase II subunit alpha; CaM kinase II subunit delta; CAM2; CaMK-II subunit alpha; CaMK-II subunit delta; CAMK2A; CAMK2B; CAMKA; CAMKB; CAMKD; CAMKG; CaMKII alpha; KIAA0968; Calcium / calmodulin dependent protein kinase 2 delta; Calcium / calmodulin dependent protein kinase II delta; calcium/calmodulin-dependent protein kinase (CaM kinase) II delta; calcium/calmodulin-dependent protein kinase type II delta chain; Calcium/calmodulin-dependent protein kinase type II subunit delta; CAM kinase 2 delta; CAM kinase II delta; CaM kinase II delta subunit; CaM kinase II subunit delta; CaM-kinase II delta chain; CAMK 2d; CaMK-II delta subunit; CaMK-II subunit delta; CAMK2D; CAMKD; CAMKI; KCC2D_HUMAN; RATCAMKI;CAMK gamma;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Expression:
Q13554 KCC2B_HUMAN:

Widely expressed. Expressed in adult and fetal brain. Expression is slightly lower in fetal brain. Expressed in skeletal muscle.

Q13555 KCC2G_HUMAN:

Expressed in skeletal muscle.

Q13557 KCC2D_HUMAN:

Expressed in cardiac muscle and skeletal muscle. Isoform Delta 3, isoform Delta 2, isoform Delta 8 and isoform Delta 9 are expressed in cardiac muscle. Isoform Delta 11 is expressed in skeletal muscle.

Sequence:
MATITCTRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNARRKLKGAILTTMLATRNFSGGKSGGNKKSDGVKESSESTNTTIEDEDTKVRKQEIIKVTEQLIEAISNGDFESYTKMCDPGMTAFEPEALGNLVEGLDFHRFYFENLWSRNSKPVHTTILNPHIHLMGDESACIAYIRITQYLDAGGIPRTAQSEETRVWHRRDGKWQIVHFHRSGAPSVLPH

MATTVTCTRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWVCQRSTVASMMHRQETVECLKKFNARRKLKGAILTTMLATRNFSVGRQTTAPATMSTAASGTTMGLVEQAKSLLNKKADGVKPQTNSTKNSAAATSPKGTLPPAALEPQTTVIHNPVDGIKESSDSANTTIEDEDAKAPRVPDILSSVRRGSGAPEAEGPLPCPSPAPFSPLPAPSPRISDILNSVRRGSGTPEAEGPLSAGPPPCLSPALLGPLSSPSPRISDILNSVRRGSGTPEAEGPSPVGPPPCPSPTIPGPLPTPSRKQEIIKTTEQLIEAVNNGDFEAYAKICDPGLTSFEPEALGNLVEGMDFHRFYFENLLAKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQYIDGQGRPRTSQSEETRVWHRRDGKWQNVHFHCSGAPVAPLQ

MATTATCTRFTDDYQLFEELGKGAFSVVRRCVKKTSTQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIHQILESVNHIHQHDIVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITADQALKHPWVCQRSTVASMMHRQETVECLRKFNARRKLKGAILTTMLVSRNFSAAKSLLNKKSDGGVKKRKSSSSVHLMPQSNNKNSLVSPAQEPAPLQTAMEPQTTVVHNATDGIKGSTESCNTTTEDEDLKGRVPEGRSSRDRTAPSAGMQPQPSLCSSAMRKQEIIKITEQLIEAINNGDFEAYTKICDPGLTSFEPEALGNLVEGMDFHKFYFENLLSKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQYIDGQGRPRTSQSEETRVWHRRDGKWLNVHYHCSGAPAAPLQ

MASTTTCTRFTDEYQLFEELGKGAFSVVRRCMKIPTGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILESVNHCHLNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDMWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPAKRITASEALKHPWICQRSTVASMMHRQETVDCLKKFNARRKLKGAILTTMLATRNFSAAKSLLKKPDGVKESTESSNTTIEDEDVKARKQEIIKVTEQLIEAINNGDFEAYTKICDPGLTAFEPEALGNLVEGMDFHRFYFENALSKSNKPIHTIILNPHVHLVGDDAACIAYIRLTQYMDGSGMPKTMQSEETRVWHRRDGKWQNVHFHRSGSPTVPIKPPCIPNGKENFSGGTSLWQNI

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Pig
100
Horse
100
Bovine
100
Sheep
100
Xenopus
100
Rabbit
100
Dog
0
Zebrafish
0
Chicken
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - Q9UQM7/Q13554/Q13555/Q13557 As Substrate

Site PTM Type Enzyme
K57 Ubiquitination
S79 Phosphorylation
K138 Ubiquitination
S146 Phosphorylation
K227 Acetylation
K227 Ubiquitination
Y231 Phosphorylation
S235 Phosphorylation
K246 Ubiquitination
T254 Phosphorylation
K259 Ubiquitination
K268 Ubiquitination
S276 Phosphorylation
S280 Phosphorylation
T287 Phosphorylation Q13554 (CAMK2B)
K299 Methylation
K301 Methylation
T306 Phosphorylation
T307 Phosphorylation
T311 Phosphorylation
S315 Phosphorylation
T328 Phosphorylation
K342 Acetylation
S394 Phosphorylation
S395 Phosphorylation
S397 Phosphorylation
T400 Phosphorylation
T401 Phosphorylation
S423 Phosphorylation
S436 Phosphorylation
S441 Phosphorylation
S456 Phosphorylation
S461 Phosphorylation
T463 Phosphorylation
S471 Phosphorylation
S479 Phosphorylation
S499 Phosphorylation
S504 Phosphorylation
T506 Phosphorylation
S522 Phosphorylation
Site PTM Type Enzyme
Y14 Phosphorylation
K22 Ubiquitination
S26 Phosphorylation
K34 Ubiquitination
T35 Phosphorylation
K43 Ubiquitination
K57 Ubiquitination
K69 Ubiquitination
S79 Phosphorylation
S114 Phosphorylation
K138 Ubiquitination
S146 Phosphorylation
K227 Acetylation
K227 Ubiquitination
Y231 Phosphorylation
S235 Phosphorylation
K246 Ubiquitination
T254 Phosphorylation
K259 Ubiquitination
K268 Ubiquitination
C273 S-Nitrosylation
S276 Phosphorylation
S280 Phosphorylation Q13555 (CAMK2G)
T287 Phosphorylation Q13555 (CAMK2G)
K299 Methylation
K301 Methylation
T306 Phosphorylation
T307 Phosphorylation
S311 Phosphorylation
S315 Phosphorylation
S319 Phosphorylation Q13555 (CAMK2G)
S325 Phosphorylation
S334 Phosphorylation
S336 Phosphorylation
S349 Phosphorylation
S352 Phosphorylation
T382 Phosphorylation
S384 Phosphorylation
T388 Phosphorylation
S419 Phosphorylation
S484 Phosphorylation
Site PTM Type Enzyme
A2 Acetylation
S3 Phosphorylation
K43 Ubiquitination
K57 Ubiquitination
K69 Ubiquitination
S79 Phosphorylation
K138 Ubiquitination
S146 Phosphorylation
K227 Acetylation
K227 Ubiquitination
Y231 Phosphorylation
S235 Phosphorylation
K246 Ubiquitination
K251 Ubiquitination
T254 Phosphorylation
S264 Phosphorylation
S276 Phosphorylation
S280 Phosphorylation
T287 Phosphorylation Q13557 (CAMK2D)
K299 Methylation
K301 Methylation
T306 Phosphorylation
T307 Phosphorylation
T311 Phosphorylation
S315 Phosphorylation
K318 Acetylation
K318 Ubiquitination
S319 Phosphorylation
S330 Phosphorylation
T331 Phosphorylation
S333 Phosphorylation
S334 Phosphorylation
T336 Phosphorylation
T337 Phosphorylation
C373 S-Nitrosylation
S404 Phosphorylation
S441 Phosphorylation
S472 Phosphorylation
T474 Phosphorylation
S490 Phosphorylation
Site PTM Type Enzyme
C6 S-Nitrosylation
Y13 Phosphorylation
K56 Ubiquitination
K68 Ubiquitination
S78 Phosphorylation
K137 Ubiquitination
S145 Phosphorylation
K226 Acetylation
K226 Ubiquitination
Y230 Phosphorylation
S234 Phosphorylation
K245 Ubiquitination
T253 Phosphorylation
K258 Methylation
C280 S-Nitrosylation
T286 Phosphorylation Q9UQM7 (CAMK2A)
K298 Methylation
K300 Methylation
T305 Phosphorylation Q9UQM7 (CAMK2A)
T306 Phosphorylation Q9UQM7 (CAMK2A)
T310 Phosphorylation
S314 Phosphorylation Q9UQM7 (CAMK2A)
S318 Phosphorylation
S331 Phosphorylation
S333 Phosphorylation
T334 Phosphorylation
T336 Phosphorylation
T337 Phosphorylation

PTMs - Q9UQM7/Q13554/Q13555/Q13557 As Enzyme

Substrate Site Source
O14490-2 (DLGAP1) S349 Uniprot
O14490-2 (DLGAP1) S393 Uniprot
P14921-1 (ETS1) S251 Uniprot
P14921-1 (ETS1) S257 Uniprot
P14921-1 (ETS1) S282 Uniprot
P14921-1 (ETS1) S285 Uniprot
P16949 (STMN1) S16 Uniprot
P26678 (PLN) T17 Uniprot
P35222 (CTNNB1) T332 Uniprot
P35222 (CTNNB1) T472 Uniprot
P35222 (CTNNB1) S552 Uniprot
P42224 (STAT1) S727 Uniprot
P49840 (GSK3A) S21 Uniprot
Q01970-1 (PLCB3) S537 Uniprot
Q12879-1 (GRIN2A) S1291 Uniprot
Q13131 (PRKAA1) T183 Uniprot
Q13224 (GRIN2B) S383 Uniprot
Q13224 (GRIN2B) S1303 Uniprot
Q13554-1 (CAMK2B) T287 Uniprot
Q9NQC7 (CYLD) S362 Uniprot
Q9NQC7 (CYLD) S418 Uniprot
Q9NQC7 (CYLD) S772 Uniprot
Substrate Site Source
O60266-1 (ADCY3) S1076 Uniprot
P00533-1 (EGFR) S1070 Uniprot
P00533-1 (EGFR) S1071 Uniprot
P07101-1 (TH) S19 Uniprot
P10276 (RARA) T210 Uniprot
P17600-2 (SYN1) S568 Uniprot
P17600-2 (SYN1) S605 Uniprot
P18846-1 (ATF1) S63 Uniprot
P21333-2 (FLNA) S2515 Uniprot
P21817-1 (RYR1) S2843 Uniprot
P28329 (CHAT) T574 Uniprot
P35270 (SPR) S213 Uniprot
P40763 (STAT3) S727 Uniprot
P42224-1 (STAT1) S727 Uniprot
P42261-1 (GRIA1) S645 Uniprot
P42261-1 (GRIA1) S849 Uniprot
P48058 (GRIA4) S862 Uniprot
P55042 (RRAD) S273 Uniprot
Q01970-1 (PLCB3) S537 Uniprot
Q03060-16 (CREM) S87 Uniprot
Q13555 (CAMK2G) S280 Uniprot
Q13555 (CAMK2G) T287 Uniprot
Q13555 (CAMK2G) S319 Uniprot
Q15121-1 (PEA15) S116 Uniprot
Q15746-1 (MYLK) S1760 Uniprot
Q92934 (BAD) S134 Uniprot
Q9UQL6 (HDAC5) S259 Uniprot
Q9UQL6 (HDAC5) S498 Uniprot
Substrate Site Source
O15084 (ANKRD28) S1011 Uniprot
P08670 (VIM) S83 Uniprot
P13688-8 (CEACAM1) T457 Uniprot
P13688-8 (CEACAM1) S459 Uniprot
P16220 (CREB1) S133 Uniprot
P16220 (CREB1) S142 Uniprot
P26678 (PLN) T17 Uniprot
P55327 (TPD52) S176 Uniprot
P56524 (HDAC4) S210 Uniprot
P56524 (HDAC4) S632 Uniprot
Q00613 (HSF1) S230 Uniprot
Q03060-16 (CREM) S87 Uniprot
Q08289-2 (CACNB2) T499 Uniprot
Q08289 (CACNB2) T554 Uniprot
Q13557 (CAMK2D) T287 Uniprot
Q13557-1 (CAMK2D) S315 Uniprot
Q13557-8 (CAMK2D) S319 Uniprot
Q13557-1 (CAMK2D) T331 Uniprot
Q13557-1 (CAMK2D) S333 Uniprot
Q13557-1 (CAMK2D) S334 Uniprot
Q13557-8 (CAMK2D) T337 Uniprot
Q14524 (SCN5A) S516 Uniprot
Q14524 (SCN5A) T594 Uniprot
Q14571 (ITPR2) S150 Uniprot
Q14654 (KCNJ11) T224 Uniprot
Q16695 (HIST3H3) S11 Uniprot
Q8WYL5 (SSH1) S937 Uniprot
Q8WYL5 (SSH1) S978 Uniprot
Q8WZ42 (TTN) S4062 Uniprot
Q8WZ42 (TTN) S11878 Uniprot
Q8WZ42 (TTN) S12022 Uniprot
Q92736 (RYR2) S2814 Uniprot
Q9UQL6 (HDAC5) S498 Uniprot
Substrate Site Source
A8K161 (CAMK2A) T286 Uniprot
A8K161 (CAMK2A) T305 Uniprot
O00631 (SLN) T5 Uniprot
O14490-2 (DLGAP1) S44 Uniprot
O14713-2 (ITGB1BP1) T38 Uniprot
O15273 (TCAP) S157 Uniprot
O15273 (TCAP) S161 Uniprot
O95999 (BCL10) S138 Uniprot
P00533 (EGFR) S768 Uniprot
P00533-1 (EGFR) S1064 Uniprot
P00533 (EGFR) S1070 Uniprot
P00533 (EGFR) S1071 Uniprot
P00533-1 (EGFR) S1081 Uniprot
P00533-1 (EGFR) S1120 Uniprot
P00533 (EGFR) S1166 Uniprot
P04626 (ERBB2) T1172 Uniprot
P05556 (ITGB1) T788 Uniprot
P05556 (ITGB1) T789 Uniprot
P05783 (KRT18) S53 Uniprot
P07101 (TH) S19 Uniprot
P07101-4 (TH) S35 Uniprot
P07101-3 (TH) S40 Uniprot
P07101-4 (TH) S44 Uniprot
P07101 (TH) S71 Uniprot
P08670 (VIM) S83 Uniprot
P09917 (ALOX5) S272 Uniprot
P10636-6 (MAPT) S204 Uniprot
P10636-8 (MAPT) S262 Uniprot
P10636-2 (MAPT) S267 Uniprot
P10636-6 (MAPT) S298 Uniprot
P10636-8 (MAPT) S356 Uniprot
P10636-8 (MAPT) S416 Uniprot
P10636 (MAPT) T548 Uniprot
P10636 (MAPT) S552 Uniprot
P10636 (MAPT) S579 Uniprot
P11831 (SRF) S103 Uniprot
P11831 (SRF) T160 Uniprot
P14136-1 (GFAP) S13 Uniprot
P14136-1 (GFAP) S17 Uniprot
P14136-1 (GFAP) S38 Uniprot
P14136-1 (GFAP) S393 Uniprot
P14921 (ETS1) S251 Uniprot
P14921 (ETS1) S257 Uniprot
P14921-1 (ETS1) S282 Uniprot
P14921 (ETS1) S285 Uniprot
P15036 (ETS2) S246 Uniprot
P15036 (ETS2) S310 Uniprot
P15036 (ETS2) S313 Uniprot
P16070 (CD44) S706 Uniprot
P16220 (CREB1) S142 Uniprot
P16615-2 (ATP2A2) S38 Uniprot
P16949 (STMN1) S16 Uniprot
P17676-1 (CEBPB) S325 Uniprot
P18433 (PTPRA) S204 Uniprot
P20941-2 (PDC) S2 Uniprot
P20941-2 (PDC) S21 Uniprot
P20941-1 (PDC) S54 Uniprot
P20941-1 (PDC) S73 Uniprot
P21333 (FLNA) S2523 Uniprot
P23677 (ITPKA) T311 Uniprot
P26678 (PLN) T17 Uniprot
P28329-3 (CHAT) T456 Uniprot
P28329 (CHAT) T574 Uniprot
P29475 (NOS1) S852 Uniprot
P31645 (SLC6A4) S13 Uniprot
P35222 (CTNNB1) T332 Uniprot
P35222 (CTNNB1) T472 Uniprot
P35222 (CTNNB1) S552 Uniprot
P35270 (SPR) S213 Uniprot
P35367 (HRH1) T140 Uniprot
P35367 (HRH1) T142 Uniprot
P35367 (HRH1) S396 Uniprot
P35367 (HRH1) S398 Uniprot
P35372 (OPRM1) S268 Uniprot
P35372 (OPRM1) S270 Uniprot
P35372 (OPRM1) T372 Uniprot
P35462 (DRD3) S229 Uniprot
P37840 (SNCA) S129 Uniprot
P42261 (GRIA1) S567 Uniprot
P42261 (GRIA1) S832 Uniprot
P46527 (CDKN1B) S10 Uniprot
P48058 (GRIA4) S862 Uniprot
P51790 (CLCN3) S109 Uniprot
P55042 (RRAD) S273 Uniprot
P55055 (NR1H2) S426 Uniprot
Q00613-1 (HSF1) S230 Uniprot
Q00975 (CACNA1B) S2120 Uniprot
Q01970 (PLCB3) S537 Uniprot
Q04760 (GLO1) T107 Uniprot
Q05397 (PTK2) S843 Uniprot
Q05469 (LIPE) S855 Uniprot
Q05682 (CALD1) S643 Uniprot
Q05682 (CALD1) S656 Uniprot
Q06210 (GFPT1) S261 Uniprot
Q12879-1 (GRIN2A) S1291 Uniprot
Q12959 (DLG1) S232 Uniprot
Q13224 (GRIN2B) S383 Uniprot
Q13224 (GRIN2B) S1303 Uniprot
Q14653 (IRF3) S386 Uniprot
Q14654 (KCNJ11) T180 Uniprot
Q14654 (KCNJ11) T224 Uniprot
Q14674 (ESPL1) S1501 Uniprot
Q15121 (PEA15) S116 Uniprot
Q15796 (SMAD2) S110 Uniprot
Q15796-1 (SMAD2) S240 Uniprot
Q15796-1 (SMAD2) S260 Uniprot
Q4G163 (FBXO43) T234 Uniprot
Q86UR5 (RIMS1) S242 Uniprot
Q86UR5 (RIMS1) S288 Uniprot
Q8IZP0 (ABI1) S88 Uniprot
Q92736 (RYR2) S2808 Uniprot
Q92736 (RYR2) S2814 Uniprot
Q96A00 (PPP1R14A) S130 Uniprot
Q96NW7 (LRRC7) S1439 Uniprot
Q96PH1-4 (NOX5) S475 Uniprot
Q96PM5 (RCHY1) T154 Uniprot
Q96PM5 (RCHY1) S155 Uniprot
Q96PV0-1 (SYNGAP1) S1073 Uniprot
Q96PV0-1 (SYNGAP1) T1077 Uniprot
Q96PV0-1 (SYNGAP1) S1138 Uniprot
Q9BXL7 (CARD11) S116 Uniprot
Q9NSC5 (HOMER3) S120 Uniprot
Q9NSC5 (HOMER3) S159 Uniprot
Q9NSC5 (HOMER3) S176 Uniprot
Q9UBS5 (GABBR1) S868 Uniprot
Q9UQL6 (HDAC5) S259 Uniprot
Q9UQL6 (HDAC5) S498 Uniprot
Q9UQM7-1 (CAMK2A) T286 Uniprot
Q9UQM7-1 (CAMK2A) T305 Uniprot
Q9UQM7 (CAMK2A) T306 Uniprot
Q9UQM7 (CAMK2A) S314 Uniprot
Q9Y496 (KIF3A) S687 Uniprot
Q9Y4D2 (DAGLA) S782 Uniprot
Q9Y4D2 (DAGLA) S808 Uniprot

Research Backgrounds

Function:

Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in synaptic plasticity, neurotransmitter release and long-term potentiation. Member of the NMDAR signaling complex in excitatory synapses, it regulates NMDAR-dependent potentiation of the AMPAR and therefore excitatory synaptic transmission (By similarity). Regulates dendritic spine development. Also regulates the migration of developing neurons. Phosphorylates the transcription factor FOXO3 to activate its transcriptional activity.

PTMs:

Autophosphorylation of Thr-286 following activation by Ca(2+)/calmodulin. Phosphorylation of Thr-286 locks the kinase into an activated state.

Subcellular Location:

Cell junction>Synapse. Cell junction>Synapse>Postsynaptic density. Cell projection>Dendritic spine. Cell projection>Dendrite.
Note: Postsynaptic lipid rafts.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

There are 4 genes encoding calcium/calmodulin-dependent protein kinase type II chains: CAMK2A, CAMK2B, CAMK2G and CAMK2D. The corresponding proteins assemble into homo- or heteromultimeric holoenzymes composed of 12 subunits with two hexameric rings stacked one on top of the other. Interacts with BAALC. Interacts with MPDZ. Interacts with SYN1. Interacts with CAMK2N2. Interacts with SYNGAP1. Interacts with SYNPO2 (By similarity). Interacts with SHANK3. Interacts with GRIN2B. Interacts with CACNB2. Interacts with LRRC7. Interacts with GRM5.

Family&Domains:

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.

Function:

Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in dendritic spine and synapse formation, neuronal plasticity and regulation of sarcoplasmic reticulum Ca(2+) transport in skeletal muscle. In neurons, plays an essential structural role in the reorganization of the actin cytoskeleton during plasticity by binding and bundling actin filaments in a kinase-independent manner. This structural function is required for correct targeting of CaMK2A, which acts downstream of NMDAR to promote dendritic spine and synapse formation and maintain synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning. In developing hippocampal neurons, promotes arborization of the dendritic tree and in mature neurons, promotes dendritic remodeling. Also regulates the migration of developing neurons. Participates in the modulation of skeletal muscle function in response to exercise. In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of triadin, a ryanodine receptor-coupling factor, and phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2.

PTMs:

Autophosphorylation of Thr-287 following activation by Ca(2+)/calmodulin. Phosphorylation of Thr-287 locks the kinase into an activated state.

Subcellular Location:

Cytoplasm>Cytoskeleton. Cytoplasm>Cytoskeleton>Microtubule organizing center>Centrosome. Sarcoplasmic reticulum membrane>Peripheral membrane protein>Cytoplasmic side. Cell junction>Synapse.
Note: In slow-twitch muscle, evenly distributed between longitudinal SR and junctional SR.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Widely expressed. Expressed in adult and fetal brain. Expression is slightly lower in fetal brain. Expressed in skeletal muscle.

Subunit Structure:

CAMK2 is composed of 4 different chains: alpha (CAMK2A), beta (CAMK2B), gamma (CAMK2G), and delta (CAMK2D). The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 12 subunits with two hexameric rings stacked one on top of the other Ref.19). Interacts with SYNGAP1 and CAMK2N2 (By similarity). Interacts with MPDZ. Interacts with FOXO3 (By similarity). Interacts (when in a kinase inactive state not associated with calmodulin) with ARC; leading to target ARC to inactive synapses (By similarity).

Family&Domains:

The CAMK2 protein kinases contain a unique C-terminal subunit association domain responsible for oligomerization.

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.

Function:

Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in sarcoplasmic reticulum Ca(2+) transport in skeletal muscle and may function in dendritic spine and synapse formation and neuronal plasticity. In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of the ryanodine receptor-coupling factor triadin. In the central nervous system, it is involved in the regulation of neurite formation and arborization. It may participate in the promotion of dendritic spine and synapse formation and maintenance of synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning.

PTMs:

Autophosphorylation of Thr-287 following activation by Ca(2+)/calmodulin. Phosphorylation of Thr-287 locks the kinase into an activated state.

Subcellular Location:

Sarcoplasmic reticulum membrane>Peripheral membrane protein>Cytoplasmic side.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Expressed in skeletal muscle.

Subunit Structure:

CAMK2 is composed of 4 different chains: alpha (CAMK2A), beta (CAMK2B), gamma (CAMK2G), and delta (CAMK2D). The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 12 subunits with two hexameric rings stacked one on top of the other.

Family&Domains:

The CAMK2 protein kinases contain a unique C-terminal subunit association domain responsible for oligomerization.

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.

Function:

Calcium/calmodulin-dependent protein kinase involved in the regulation of Ca(2+) homeostatis and excitation-contraction coupling (ECC) in heart by targeting ion channels, transporters and accessory proteins involved in Ca(2+) influx into the myocyte, Ca(2+) release from the sarcoplasmic reticulum (SR), SR Ca(2+) uptake and Na(+) and K(+) channel transport. Targets also transcription factors and signaling molecules to regulate heart function. In its activated form, is involved in the pathogenesis of dilated cardiomyopathy and heart failure. Contributes to cardiac decompensation and heart failure by regulating SR Ca(2+) release via direct phosphorylation of RYR2 Ca(2+) channel on 'Ser-2808'. In the nucleus, phosphorylates the MEF2 repressor HDAC4, promoting its nuclear export and binding to 14-3-3 protein, and expression of MEF2 and genes involved in the hypertrophic program. Is essential for left ventricular remodeling responses to myocardial infarction. In pathological myocardial remodeling acts downstream of the beta adrenergic receptor signaling cascade to regulate key proteins involved in ECC. Regulates Ca(2+) influx to myocytes by binding and phosphorylating the L-type Ca(2+) channel subunit beta-2 CACNB2. In addition to Ca(2+) channels, can target and regulate the cardiac sarcolemmal Na(+) channel Nav1.5/SCN5A and the K+ channel Kv4.3/KCND3, which contribute to arrhythmogenesis in heart failure. Phosphorylates phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2, contributing to the enhancement of SR Ca(2+) uptake that may be important in frequency-dependent acceleration of relaxation (FDAR) and maintenance of contractile function during acidosis. May participate in the modulation of skeletal muscle function in response to exercise, by regulating SR Ca(2+) transport through phosphorylation of PLN/PLB and triadin, a ryanodine receptor-coupling factor.

PTMs:

Autophosphorylation of Thr-287 following activation by Ca(2+)/calmodulin. Phosphorylation of Thr-287 locks the kinase into an activated state.

Subcellular Location:

Cell membrane>Sarcolemma>Peripheral membrane protein>Cytoplasmic side. Sarcoplasmic reticulum membrane>Peripheral membrane protein>Cytoplasmic side.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Expressed in cardiac muscle and skeletal muscle. Isoform Delta 3, isoform Delta 2, isoform Delta 8 and isoform Delta 9 are expressed in cardiac muscle. Isoform Delta 11 is expressed in skeletal muscle.

Subunit Structure:

CAMK2 is composed of 4 different chains: alpha (CAMK2A), beta (CAMK2B), gamma (CAMK2G), and delta (CAMK2D). The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 12 subunits with two hexameric rings stacked one on top of the other. Interacts with RRAD and CACNB2 (By similarity).

Family&Domains:

The CAMK2 protein kinases contain a unique C-terminal subunit association domain responsible for oligomerization.

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.

Research Fields

· Cellular Processes > Cell growth and death > Oocyte meiosis.   (View pathway)

· Cellular Processes > Cell growth and death > Necroptosis.   (View pathway)

· Environmental Information Processing > Signal transduction > ErbB signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Calcium signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > cAMP signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > HIF-1 signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Wnt signaling pathway.   (View pathway)

· Human Diseases > Substance dependence > Amphetamine addiction.

· Human Diseases > Infectious diseases: Bacterial > Tuberculosis.

· Human Diseases > Cancers: Overview > Pathways in cancer.   (View pathway)

· Human Diseases > Cancers: Overview > Proteoglycans in cancer.

· Human Diseases > Cancers: Specific types > Glioma.   (View pathway)

· Organismal Systems > Circulatory system > Adrenergic signaling in cardiomyocytes.   (View pathway)

· Organismal Systems > Development > Axon guidance.   (View pathway)

· Organismal Systems > Environmental adaptation > Circadian entrainment.

· Organismal Systems > Nervous system > Long-term potentiation.

· Organismal Systems > Nervous system > Neurotrophin signaling pathway.   (View pathway)

· Organismal Systems > Nervous system > Cholinergic synapse.

· Organismal Systems > Nervous system > Dopaminergic synapse.

· Organismal Systems > Sensory system > Olfactory transduction.

· Organismal Systems > Sensory system > Inflammatory mediator regulation of TRP channels.   (View pathway)

· Organismal Systems > Endocrine system > Insulin secretion.   (View pathway)

· Organismal Systems > Endocrine system > Melanogenesis.

· Organismal Systems > Endocrine system > Oxytocin signaling pathway.

· Organismal Systems > Endocrine system > Glucagon signaling pathway.

· Organismal Systems > Endocrine system > Aldosterone synthesis and secretion.

· Organismal Systems > Digestive system > Gastric acid secretion.

References

1). Sun F et al. Epac1 signaling pathway mediates the damage and apoptosis of inner ear hair cells after noise exposure in a rat model. Neuroscience 2021 Apr 7;S0306-4522(21)00168-8. (PubMed: 33838290) [IF=3.708]

Application: WB    Species: rat    Sample: HEI-OC1 cells

Fig. 7. Effects of Epac regulators on intracellular Ca2+ in HEI-OC1 cells. Epac1 activation induces OHC death through CaMKII. (A) Representative images of Ca2+ in HEI-OC1 cells 12 h after oligomycin exposure; green: fura-2 AM; scale bar = 100 mm, n = 3. (B) The intracellular Ca2+ concentration was determined by confocal Ca2+ measurements; time courses of changes in calcium fluorescence are shown; n = 3. (C) A summary of data showing [Ca2+]i alterations induced by Epac regulators. (D) Western blot analysis of CaMKII expression in cochlear tissue after noise exposure; n = 3. (E) Western blot analysis of CaMKII expression in oligomycin-treated HEI-OC1 cells; b-actin was used as the loading control. The data represent the mean ± SEM, n = 3; *P < 0.05 vs. Control group, #P < 0.05 vs. OA.

2). Tong L et al. TRPM2 mediates CaMKⅡ-Beclin-1 signaling in early cortical injury after induced subarachnoid hemorrhage in mice. J Chem Neuroanat 2022 Aug 18;125:102144. (PubMed: 35988814) [IF=3.097]

3). Zhang BB et al. Neuroprotective Effects of Dammarane-Type Saponins from Panax notoginseng on Glutamate-Induced Cell Damage in PC12 Cells. Planta Med 2019 Feb 21 (PubMed: 30791058) [IF=3.007]

Application: WB    Species: rat    Sample: PC12 cells

Fig. 6 | Effects of compound 4 on the protein expression levels in glutamate-treated PC12 cells. A Western blot analysis of compound 4 and MK801 (a standard NMDAR antagonist) for the expression of p-NMDAR1/NMDAR1. B Western blot analysis of compound 4 and KN93 (a standard inhibitor of CaMKII) for the expression of p-CaMKII/CaMKII. Results were obtained from three independent experiments and are expressed as the mean ± SEM (##p < 0.01 vs. control group, **p < 0.01 vs. glutamate-induced cells, *p < 0.05 vs. glutamate-induced cells).

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