Product: JNK1/2/3 Antibody
Catalog: AF6318
Description: Rabbit polyclonal antibody to JNK1/2/3
Application: WB IF/ICC
Reactivity: Human, Mouse, Rat, Pig
Prediction: Pig, Bovine, Horse, Sheep, Rabbit, Dog, Chicken, Xenopus
Mol.Wt.: 46kDa,54kDa; 48kD,53kD(Calculated).
Uniprot: P45983 | P45984 | P53779
RRID: AB_2835177

View similar products>>

   Size Price Inventory
 100ul $280 In stock
 200ul $350 In stock

Lead Time: Same day delivery

For pricing and ordering contact:
Local distributors

Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat,Pig
Prediction:
Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(100%), Xenopus(100%)
Clonality:
Polyclonal
Specificity:
JNK1/2/3 Antibody detects endogenous levels of total JNK1/2/3.
RRID:
AB_2835177
Cite Format: Affinity Biosciences Cat# AF6318, RRID:AB_2835177.
Conjugate:
Unconjugated.
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

C Jun kinase 2; c Jun N terminal kinase 1; c Jun N terminal kinase 2; c Jun N terminal kinase 3; c-Jun N-terminal kinase 1; JNK 46; JNK 55; JNK; JNK-46; JNK1; JNK1A2; JNK2; JNK21B1/2; JNK2A; JNK2ALPHA; JNK2B; JNK2BETA; JNK3 alpha protein kinase; JNK3; JNK3A; Jun kinase; JUN N terminal kinase; MAP kinase 10; MAP kinase 8; MAP kinase 9; MAP kinase p49 3F12; MAPK 10; MAPK 8; MAPK 9; MAPK10; mapk8; MAPK9; Mitogen activated protein kinase 10; Mitogen activated protein kinase 8; Mitogen activated protein kinase 8 isoform JNK1 alpha1; Mitogen activated protein kinase 8 isoform JNK1 beta2; Mitogen activated protein kinase 9; Mitogen-activated protein kinase 8; MK08_HUMAN; p493F12; p54a; p54aSAPK; p54bSAPK; PRKM10; PRKM8; PRKM9; SAPK; SAPK(beta); SAPK1; SAPK1a; SAPK1b; SAPK1c; Stress activated protein kinase 1; Stress activated protein kinase 1a; Stress activated protein kinase 1b; Stress activated protein kinase 1c; Stress activated protein kinase beta; Stress activated protein kinase JNK1; Stress activated protein kinase JNK2; Stress activated protein kinase JNK3; Stress-activated protein kinase 1c; Stress-activated protein kinase JNK1; c Jun kinase 2; C Jun N terminal kinase 2; c-Jun N-terminal kinase 2; JNK 55; JNK-55; JNK2 alpha; JNK2; JNK2 beta; JNK2A; JNK2alpha; JNK2B; JNK2BETA; Jun kinase; MAP kinase 9; MAPK 9; Mapk9; Mitogen activated protein kinase 9; Mitogen-activated protein kinase 9; MK09_HUMAN; P54a; p54aSAPK; PRKM9; Protein kinase, mitogen-activated, 9; SAPK alpha; SAPK; SAPK1a; Stress activated protein kinase 1a; Stress-activated protein kinase JNK2; c Jun kinase 3; c-Jun N-terminal kinase 3; cJun N terminal kinase 3; FLJ12099; FLJ33785; JNK3 alpha protein kinase; JNK3; JNK3A; MAP kinase 10; MAP kinase; MAP kinase p49 3F12; MAPK 10; Mapk10; MGC50974; mitogen activated protein kinase 10; Mitogen-activated protein kinase 10; MK10_HUMAN; p493F12; p54bSAPK; PRKM10; protein kinase mitogen activated 10; SAPK1b; Stress activated protein kinase 1b; stress activated protein kinase beta; Stress activated protein kinase JNK3; Stress-activated protein kinase JNK3;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Expression:
P53779 MK10_HUMAN:

Specific to a subset of neurons in the nervous system. Present in the hippocampus and areas, cerebellum, striatum, brain stem, and weakly in the spinal cord. Very weak expression in testis and kidney.

Description:
JNK3 a protein kinase of the MAPK family that is potently activated by a variety of environmental stress and pro-inflammatory cytokines. Brain-selective JNK isoform.
Sequence:
MSRSKRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDLWSVGCIMGEMVCHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVIDASKRISVDEALQHPYINVWYDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKEVMDLEERTKNGVIRGQPSPLGAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR

MSDSKCDSQFYSVQVADSTFTVLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGCVIFQGTDHIDQWNKVIEQLGTPSAEFMKKLQPTVRNYVENRPKYPGIKFEELFPDWIFPSESERDKIKTSQARDLLSKMLVIDPDKRISVDEALRHPYITVWYDPAEAEAPPPQIYDAQLEEREHAIEEWKELIYKEVMDWEERSKNGVVKDQPSDAAVSSNATPSQSSSINDISSMSTEQTLASDTDSSLDASTGPLEGCR

MSLHFLYYCSEPTLDVKIAFCQGFDKQVDVSYIAKHYNMSKSKVDNQFYSVEVGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRNYVENRPKYAGLTFPKLFPDSLFPADSEHNKLKASQARDLLSKMLVIDPAKRISVDDALQHPYINVWYDPAEVEAPPPQIYDKQLDEREHTIEEWKELIYKEVMNSEEKTKNGVVKGQPSPSGAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAGPLGCCR

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
Dog
100
Xenopus
100
Chicken
100
Rabbit
100
Zebrafish
79
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P45983/P45984/P53779 As Substrate

Site PTM Type Enzyme
S2 Phosphorylation
K30 Ubiquitination
K56 Ubiquitination
K68 Ubiquitination
C116 S-Nitrosylation
S129 Phosphorylation Q05655 (PRKCD)
S144 Phosphorylation
K153 Ubiquitination
S155 Phosphorylation
K160 Ubiquitination
K166 Ubiquitination
T178 Phosphorylation
S179 Phosphorylation
T183 Phosphorylation P45985 (MAP2K4) , O14733 (MAP2K7) , Q99683 (MAP3K5) , O95382 (MAP3K6)
Y185 Phosphorylation P45985 (MAP2K4) , P07949 (RET) , Q99683 (MAP3K5) , O14733 (MAP2K7) , O95382 (MAP3K6)
T188 Phosphorylation
T243 Phosphorylation
K250 Ubiquitination
K251 Ubiquitination
T255 Phosphorylation
T258 Phosphorylation
Y259 Phosphorylation
K265 Ubiquitination
K273 Ubiquitination
K288 Ubiquitination
S292 Phosphorylation
K300 Ubiquitination
S307 Phosphorylation
K308 Acetylation
K308 Ubiquitination
K336 Ubiquitination
K353 Ubiquitination
Y357 Phosphorylation
T367 Phosphorylation
S377 Phosphorylation
Site PTM Type Enzyme
K56 Ubiquitination
K68 Ubiquitination
S144 Phosphorylation
K153 Ubiquitination
S155 Phosphorylation
K160 Ubiquitination
C163 S-Nitrosylation
K166 Ubiquitination
T178 Phosphorylation
T183 Phosphorylation O14733 (MAP2K7)
Y185 Phosphorylation P45985 (MAP2K4) , P07949 (RET) , O14733 (MAP2K7)
T188 Phosphorylation
K250 Acetylation
K250 Ubiquitination
K251 Ubiquitination
S292 Phosphorylation
K300 Ubiquitination
S311 Phosphorylation
K353 Ubiquitination
Y357 Phosphorylation
T386 Phosphorylation
T404 Phosphorylation O14733 (MAP2K7) , P68400 (CSNK2A1)
S407 Phosphorylation P68400 (CSNK2A1) , O14733 (MAP2K7)
Site PTM Type Enzyme
K94 Ubiquitination
K106 Ubiquitination
T131 Phosphorylation Q00535 (CDK5)
S182 Phosphorylation
K191 Ubiquitination
S193 Phosphorylation
K198 Ubiquitination
K204 Ubiquitination
T216 Phosphorylation
S217 Phosphorylation
T221 Phosphorylation O14733 (MAP2K7)
Y223 Phosphorylation P45985 (MAP2K4)
T226 Phosphorylation
T281 Phosphorylation
K288 Ubiquitination
K289 Ubiquitination
S330 Phosphorylation
K346 Acetylation
K391 Ubiquitination

PTMs - P45983/P45984/P53779 As Enzyme

Substrate Site Source
O00418 (EEF2K) S396 Uniprot
O43521-2 (BCL2L11) S44 Uniprot
O43521-17 (BCL2L11) T56 Uniprot
O43521-2 (BCL2L11) S58 Uniprot
O43521-1 (BCL2L11) S59 Uniprot
O43521-1 (BCL2L11) S69 Uniprot
O43521-1 (BCL2L11) S77 Uniprot
O43521-1 (BCL2L11) S104 Uniprot
O43521 (BCL2L11) T116 Uniprot
O43521-1 (BCL2L11) S118 Uniprot
O43524 (FOXO3) S574 Uniprot
O43561-2 (LAT) T155 Uniprot
O43561 (LAT) T184 Uniprot
O95644 (NFATC1) S172 Uniprot
P01106 (MYC) T58 Uniprot
P01106 (MYC) S62 Uniprot
P01106 (MYC) S71 Uniprot
P01106-2 (MYC) S77 Uniprot
P01106-2 (MYC) S86 Uniprot
P04150 (NR3C1) S226 Uniprot
P04637 (TP53) S20 Uniprot
P04637 (TP53) S37 Uniprot
P04637-1 (TP53) T81 Uniprot
P05067-4 (APP) T668 Uniprot
P05067 (APP) T743 Uniprot
P05412 (JUN) S63 Uniprot
P05412 (JUN) S73 Uniprot
P05412 (JUN) T91 Uniprot
P05412 (JUN) T93 Uniprot
P05787 (KRT8) S74 Uniprot
P05787 (KRT8) S432 Uniprot
P08047 (SP1) T278 Uniprot
P08047 (SP1) T739 Uniprot
P10275 (AR) S651 Uniprot
P10276 (RARA) T181 Uniprot
P10276 (RARA) S445 Uniprot
P10276 (RARA) S461 Uniprot
P10415-1 (BCL2) T69 Uniprot
P10415 (BCL2) S70 Uniprot
P10415 (BCL2) S87 Uniprot
P10636-8 (MAPT) T181 Uniprot
P10636-8 (MAPT) S202 Uniprot
P10636-8 (MAPT) T231 Uniprot
P10636-8 (MAPT) S396 Uniprot
P10636 (MAPT) T498 Uniprot
P10636 (MAPT) S516 Uniprot
P10636 (MAPT) S519 Uniprot
P10636 (MAPT) T522 Uniprot
P10636 (MAPT) T529 Uniprot
P10636 (MAPT) T534 Uniprot
P10636 (MAPT) S713 Uniprot
P10636 (MAPT) S721 Uniprot
P10636 (MAPT) S739 Uniprot
P14618-2 (PKM) T365 Uniprot
P15336 (ATF2) T69 Uniprot
P15336 (ATF2) T71 Uniprot
P15336 (ATF2) S90 Uniprot
P16104 (H2AFX) S140 Uniprot
P16949 (STMN1) S25 Uniprot
P16949 (STMN1) S38 Uniprot
P17275 (JUNB) T102 Uniprot
P17275 (JUNB) T104 Uniprot
P17535 (JUND) S90 Uniprot
P17535 (JUND) S100 Uniprot
P17535 (JUND) T117 Uniprot
P19419 (ELK1) S383 Uniprot
P19419 (ELK1) S389 Uniprot
P19793 (RXRA) S56 Uniprot
P19793 (RXRA) S70 Uniprot
P19793 (RXRA) T82 Uniprot
P19793 (RXRA) S260 Uniprot
P22736 (NR4A1) S95 Uniprot
P23443 (RPS6KB1) S434 Uniprot
P29353 (SHC1) S36 Uniprot
P30305-2 (CDC25B) S101 Uniprot
P30305-2 (CDC25B) S103 Uniprot
P30305 (CDC25B) S115 Uniprot
P30305 (CDC25B) S117 Uniprot
P30307 (CDC25C) S168 Uniprot
P31946 (YWHAB) S186 Uniprot
P31947 (SFN) S186 Uniprot
P35222 (CTNNB1) S33 Uniprot
P35222 (CTNNB1) S37 Uniprot
P35222 (CTNNB1) T41 Uniprot
P35568 (IRS1) S307 Uniprot
P35568 (IRS1) S312 Uniprot
P35568 (IRS1) S315 Uniprot
P35568 (IRS1) S616 Uniprot
P35568 (IRS1) S636 Uniprot
P36956-3 (SREBF1) T81 Uniprot
P36956-3 (SREBF1) S93 Uniprot
P36956 (SREBF1) S117 Uniprot
P37231-2 (PPARG) S84 Uniprot
P37231 (PPARG) S112 Uniprot
P38936 (CDKN1A) T57 Uniprot
P38936 (CDKN1A) S98 Uniprot
P38936 (CDKN1A) S130 Uniprot
P40763-2 (STAT3) S726 Uniprot
P40763 (STAT3) S727 Uniprot
P41970 (ELK3) S357 Uniprot
P41970 (ELK3) S363 Uniprot
P41970 (ELK3) S396 Uniprot
P41970 (ELK3) S401 Uniprot
P42224 (STAT1) S727 Uniprot
P42226 (STAT6) S707 Uniprot
P49023 (PXN) S178 Uniprot
P54259 (ATN1) S739 Uniprot
P55957 (BID) T59 Uniprot
P61978 (HNRNPK) S216 Uniprot
P61978 (HNRNPK) S353 Uniprot
P63104-1 (YWHAZ) S184 Uniprot
P68431 (HIST1H3J) S29 Uniprot
P78352 (DLG4) S295 Uniprot
P84243 (H3F3B) S29 Uniprot
P98177 (FOXO4) T227 Uniprot
P98177 (FOXO4) S230 Uniprot
P98177 (FOXO4) T451 Uniprot
P98177 (FOXO4) T455 Uniprot
Q00613-1 (HSF1) S363 Uniprot
Q01844 (EWSR1) T79 Uniprot
Q05639 (EEF1A2) S205 Uniprot
Q05639 (EEF1A2) S358 Uniprot
Q06481 (APLP2) T736 Uniprot
Q07817 (BCL2L1) T47 Uniprot
Q07817 (BCL2L1) S62 Uniprot
Q07817 (BCL2L1) T115 Uniprot
Q07820 (MCL1) S64 Uniprot
Q07820 (MCL1) S121 Uniprot
Q07820 (MCL1) T163 Uniprot
Q12904 (AIMP1) S140 Uniprot
Q12904 (AIMP1) T164 Uniprot
Q13043 (STK4) S82 Uniprot
Q13363 (CTBP1) S422 Uniprot
Q13950 (RUNX2) S118 Uniprot
Q14653 (IRF3) S173 Uniprot
Q14934 (NFATC4) S213 Uniprot
Q14934 (NFATC4) S217 Uniprot
Q15672 (TWIST1) S68 Uniprot
Q16621 (NFE2) S157 Uniprot
Q5JR12 (PPM1J) S93 Uniprot
Q5JR12 (PPM1J) T201 Uniprot
Q5JR12 (PPM1J) T204 Uniprot
Q8N122 (RPTOR) S696 Uniprot
Q8N122 (RPTOR) T706 Uniprot
Q8N122 (RPTOR) S863 Uniprot
Q8WYK2-1 (JDP2) T148 Uniprot
Q92934 (BAD) S75 Uniprot
Q92934 (BAD) S91 Uniprot
Q93045 (STMN2) S62 Uniprot
Q93045 (STMN2) S73 Uniprot
Q96EB6 (SIRT1) S27 Uniprot
Q96EB6 (SIRT1) S47 Uniprot
Q96EB6 (SIRT1) T530 Uniprot
Q96J02 (ITCH) S240 Uniprot
Q96J02 (ITCH) T263 Uniprot
Q96J02 (ITCH) S273 Uniprot
Q96LC9-2 (BMF) S74 Uniprot
Q96LC9-2 (BMF) S77 Uniprot
Q99607 (ELF4) S641 Uniprot
Q99640 (PKMYT1) S83 Uniprot
Q9H211 (CDT1) T29 Uniprot
Q9H2B2 (SYT4) S135 Uniprot
Q9NPI6 (DCP1A) S315 Uniprot
Q9NR28 (DIABLO) S6 Uniprot
Q9NR28 (DIABLO) S9 Uniprot
Q9NRA8 (EIF4ENIF1) S301 Uniprot
Q9NRA8 (EIF4ENIF1) S374 Uniprot
Q9NRA8 (EIF4ENIF1) S513 Uniprot
Q9NRA8 (EIF4ENIF1) S587 Uniprot
Q9NRA8 (EIF4ENIF1) S693 Uniprot
Q9NRA8 (EIF4ENIF1) S752 Uniprot
Q9UPT6-1 (MAPK8IP3) T265 Uniprot
Q9UPT6-1 (MAPK8IP3) T275 Uniprot
Q9UPT6 (MAPK8IP3) T286 Uniprot
Q9UQF2 (MAPK8IP1) S15 Uniprot
Q9UQF2 (MAPK8IP1) S29 Uniprot
Q9UQF2 (MAPK8IP1) T103 Uniprot
Q9UQF2 (MAPK8IP1) S197 Uniprot
Q9UQF2 (MAPK8IP1) T205 Uniprot
Q9UQF2 (MAPK8IP1) T284 Uniprot
Q9UQF2 (MAPK8IP1) S341 Uniprot
Q9UQF2 (MAPK8IP1) S421 Uniprot
Q9Y4H2 (IRS2) T350 Uniprot
Q9Y4H2 (IRS2) S491 Uniprot
Q9Y5Q3 (MAFB) T62 Uniprot
Q9Y6Q9 (NCOA3) T24 Uniprot
Q9Y6Q9 (NCOA3) S505 Uniprot
Q9Y6Q9 (NCOA3) S543 Uniprot
Q9Y6Q9 (NCOA3) S860 Uniprot
Q9Y6Q9 (NCOA3) S867 Uniprot
Substrate Site Source
O00418 (EEF2K) S396 Uniprot
O43521-2 (BCL2L11) T56 Uniprot
O43521-1 (BCL2L11) S59 Uniprot
O43521 (BCL2L11) S69 Uniprot
O43521-1 (BCL2L11) S77 Uniprot
O43602-2 (DCX) T321 Uniprot
O43602-2 (DCX) T331 Uniprot
O43602-2 (DCX) S334 Uniprot
O60239-2 (SH3BP5) S194 Uniprot
O60239-2 (SH3BP5) S264 Uniprot
O60239 (SH3BP5) S351 Uniprot
O60239-1 (SH3BP5) S421 Uniprot
O95140 (MFN2) S27 Uniprot
P01106 (MYC) S62 Uniprot
P01106 (MYC) S71 Uniprot
P04150 (NR3C1) S226 Uniprot
P04637 (TP53) S6 Uniprot
P04637 (TP53) S20 Uniprot
P04637 (TP53) S37 Uniprot
P04637 (TP53) T81 Uniprot
P05067-4 (APP) T668 Uniprot
P05067 (APP) T743 Uniprot
P05412 (JUN) S63 Uniprot
P05412 (JUN) S73 Uniprot
P10636-8 (MAPT) T181 Uniprot
P10636-8 (MAPT) S202 Uniprot
P10636-8 (MAPT) T212 Uniprot
P10636-8 (MAPT) T217 Uniprot
P10636-8 (MAPT) T231 Uniprot
P10636 (MAPT) T498 Uniprot
P10636 (MAPT) S516 Uniprot
P10636 (MAPT) S519 Uniprot
P10636 (MAPT) T529 Uniprot
P10636 (MAPT) T548 Uniprot
P10636 (MAPT) S713 Uniprot
P10636 (MAPT) S721 Uniprot
P10636 (MAPT) S739 Uniprot
P15036 (ETS2) T72 Uniprot
P15336 (ATF2) T69 Uniprot
P15336 (ATF2) T71 Uniprot
P15336 (ATF2) S90 Uniprot
P16104 (H2AFX) S140 Uniprot
P16949 (STMN1) S25 Uniprot
P16949 (STMN1) S38 Uniprot
P19419-1 (ELK1) S383 Uniprot
P19419 (ELK1) S389 Uniprot
P19793 (RXRA) S56 Uniprot
P19793 (RXRA) S70 Uniprot
P19793 (RXRA) T82 Uniprot
P19793 (RXRA) S260 Uniprot
P23443 (RPS6KB1) S434 Uniprot
P29353 (SHC1) S36 Uniprot
P30307 (CDC25C) S168 Uniprot
P31645 (SLC6A4) T616 Uniprot
P31947 (SFN) S186 Uniprot
P35222 (CTNNB1) S191 Uniprot
P35222 (CTNNB1) S605 Uniprot
P35568 (IRS1) S307 Uniprot
P35568 (IRS1) S315 Uniprot
P35568 (IRS1) Y612 Uniprot
P35568 (IRS1) Y632 Uniprot
P40763 (STAT3) S727 Uniprot
P41970 (ELK3) S357 Uniprot
P41970 (ELK3) S363 Uniprot
P41970 (ELK3) S396 Uniprot
P41970 (ELK3) S401 Uniprot
P42224 (STAT1) S727 Uniprot
P46937 (YAP1) T119 Uniprot
P46937 (YAP1) S138 Uniprot
P46937 (YAP1) T154 Uniprot
P46937 (YAP1) S367 Uniprot
P49768 (PSEN1) S319 Uniprot
P49768 (PSEN1) T320 Uniprot
P50616 (TOB1) S152 Uniprot
P50616 (TOB1) S154 Uniprot
P50616 (TOB1) S164 Uniprot
P52945 (PDX1) S61 Uniprot
P52945 (PDX1) S66 Uniprot
P54259 (ATN1) S739 Uniprot
P55957 (BID) T59 Uniprot
P63104 (YWHAZ) S184 Uniprot
P68431 (HIST1H3J) S29 Uniprot
P84243 (H3F3B) S29 Uniprot
P98177 (FOXO4) T451 Uniprot
P98177 (FOXO4) T455 Uniprot
Q06481 (APLP2) T736 Uniprot
Q07817 (BCL2L1) T47 Uniprot
Q07817 (BCL2L1) S62 Uniprot
Q07817 (BCL2L1) T115 Uniprot
Q12968 (NFATC3) S163 Uniprot
Q12968-1 (NFATC3) S165 Uniprot
Q14653 (IRF3) S173 Uniprot
Q14934 (NFATC4) S213 Uniprot
Q14934 (NFATC4) S217 Uniprot
Q5JR12 (PPM1J) S93 Uniprot
Q8IW41 (MAPKAPK5) T182 Uniprot
Q8WYK2 (JDP2) T148 Uniprot
Q9BQQ3 (GORASP1) S274 Uniprot
Q9NYV6 (RRN3) T200 Uniprot
Q9UIG0 (BAZ1B) S158 Uniprot
Q9UPT6 (MAPK8IP3) T265 Uniprot
Q9UPT6 (MAPK8IP3) T275 Uniprot
Q9UPT6 (MAPK8IP3) T286 Uniprot
Q9UQF2 (MAPK8IP1) T103 Uniprot
Substrate Site Source
O43521-2 (BCL2L11) S58 Uniprot
O43521-1 (BCL2L11) S59 Uniprot
O43521-1 (BCL2L11) S69 Uniprot
O43521-1 (BCL2L11) S77 Uniprot
O43521 (BCL2L11) T116 Uniprot
O60282 (KIF5C) S176 Uniprot
O95644 (NFATC1) S172 Uniprot
P01106 (MYC) T58 Uniprot
P01106 (MYC) S62 Uniprot
P01106 (MYC) S71 Uniprot
P04150 (NR3C1) S226 Uniprot
P04637 (TP53) S37 Uniprot
P05067-4 (APP) T668 Uniprot
P05067 (APP) T743 Uniprot
P05412 (JUN) S63 Uniprot
P05412 (JUN) S73 Uniprot
P10415 (BCL2) T56 Uniprot
P10415 (BCL2) S70 Uniprot
P10415 (BCL2) T74 Uniprot
P10415 (BCL2) S87 Uniprot
P10636 (MAPT) T498 Uniprot
P10636 (MAPT) S516 Uniprot
P10636 (MAPT) S519 Uniprot
P10636 (MAPT) T522 Uniprot
P10636 (MAPT) T529 Uniprot
P10636 (MAPT) T534 Uniprot
P10636 (MAPT) S713 Uniprot
P10636 (MAPT) S721 Uniprot
P10636 (MAPT) S739 Uniprot
P16949 (STMN1) S25 Uniprot
P16949 (STMN1) S38 Uniprot
P29353 (SHC1) S36 Uniprot
P30307 (CDC25C) S168 Uniprot
P31947 (SFN) S186 Uniprot
P54259 (ATN1) S739 Uniprot
P55957 (BID) T59 Uniprot
P61978-1 (HNRNPK) S216 Uniprot
P61978-1 (HNRNPK) S284 Uniprot
P61978-1 (HNRNPK) S353 Uniprot
P63104 (YWHAZ) S184 Uniprot
Q06481 (APLP2) T736 Uniprot
Q07820 (MCL1) S121 Uniprot
Q07820 (MCL1) T163 Uniprot
Q16600 (ZNF239) S38 Uniprot
Q16600 (ZNF239) S129 Uniprot
Q5JR12 (PPM1J) S93 Uniprot
Q93045 (STMN2) S62 Uniprot
Q93045 (STMN2) S73 Uniprot
Q9UPT6 (MAPK8IP3) T265 Uniprot
Q9UPT6 (MAPK8IP3) T275 Uniprot
Q9UPT6-1 (MAPK8IP3) T286 Uniprot

Research Backgrounds

Function:

Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK8/JNK1. In turn, MAPK8/JNK1 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN, JDP2 and ATF2 and thus regulates AP-1 transcriptional activity. Phosphorylates the replication licensing factor CDT1, inhibiting the interaction between CDT1 and the histone H4 acetylase HBO1 to replication origins. Loss of this interaction abrogates the acetylation required for replication initiation. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including p53/TP53 and Yes-associates protein YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Contributes to the survival of erythroid cells by phosphorylating the antagonist of cell death BAD upon EPO stimulation. Mediates starvation-induced BCL2 phosphorylation, BCL2 dissociation from BECN1, and thus activation of autophagy. Phosphorylates STMN2 and hence regulates microtubule dynamics, controlling neurite elongation in cortical neurons. In the developing brain, through its cytoplasmic activity on STMN2, negatively regulates the rate of exit from multipolar stage and of radial migration from the ventricular zone. Phosphorylates several other substrates including heat shock factor protein 4 (HSF4), the deacetylase SIRT1, ELK1, or the E3 ligase ITCH. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation of the circadian clock. Phosphorylates the heat shock transcription factor HSF1, suppressing HSF1-induced transcriptional activity. Phosphorylates POU5F1, which results in the inhibition of POU5F1's transcriptional activity and enhances its proteosomal degradation (By similarity). Phosphorylates JUND and this phosphorylation is inhibited in the presence of MEN1 (By similarity). In neurons, phosphorylates SYT4 which captures neuronal dense core vesicles at synapses (By similarity).

JNK1 isoforms display different binding patterns: beta-1 preferentially binds to c-Jun, whereas alpha-1, alpha-2, and beta-2 have a similar low level of binding to both c-Jun or ATF2. However, there is no correlation between binding and phosphorylation, which is achieved at about the same efficiency by all isoforms.

PTMs:

Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and MAP2K4, which activates the enzyme. Phosphorylated by TAOK2. May be phosphorylated at Thr-183 and Tyr-185 by MAP3K1/MEKK1. Phosphorylated form is more concentrated at synapses than none-phosphorylated (By similarity).

Subcellular Location:

Cytoplasm. Nucleus. Cell junction>Synapse.
Note: In the cortical neurons, predominantly cytoplasmic and associated with the Golgi apparatus and endosomal fraction. Increased neuronal activity increases phosphorylated form at synapses (By similarity). Colocalizes with POU5F1 in the nucleus.

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

Binds to at least four scaffolding proteins, MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK8IP3/JIP-3/JSAP1 and SPAG9/MAPK8IP4/JIP-4. These proteins also bind other components of the JNK signaling pathway. Interacts with TP53 and WWOX. Interacts with JAMP (By similarity). Forms a complex with MAPK8IP1 and ARHGEF28 (By similarity). Interacts with HSF1 (via D domain and preferentially with hyperphosphorylated form); this interaction occurs under both normal growth conditions and immediately upon heat shock. Interacts (phosphorylated form) with NFE2; the interaction phosphorylates NFE2 in undifferentiated cells (By similarity). Interacts with NFATC4. Interacts with MECOM; regulates JNK signaling. Interacts with PIN1; this interaction mediates MAPK8 conformational changes leading to the binding of MAPK8 to its substrates. Interacts with GRIPAP1. Interacts with POU5F1; phosphorylates POU5F1 at 'Ser-355'. Found in a complex with SH3RF1, RAC1, MAP3K11/MLK3, MAP2K7/MKK7 and MAPK8IP1/JIP1. Found in a complex with SH3RF1, RAC2, MAP3K7/TAK1, MAP2K7/MKK7, MAPK8IP1/JIP1 and MAPK9/JNK2 (By similarity).

Family&Domains:

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.

Function:

Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK9/JNK2. In turn, MAPK9/JNK2 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. In response to oxidative or ribotoxic stresses, inhibits rRNA synthesis by phosphorylating and inactivating the RNA polymerase 1-specific transcription initiation factor RRN3. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including TP53 and YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Upon T-cell receptor (TCR) stimulation, is activated by CARMA1, BCL10, MAP2K7 and MAP3K7/TAK1 to regulate JUN protein levels. Plays an important role in the osmotic stress-induced epithelial tight-junctions disruption. When activated, promotes beta-catenin/CTNNB1 degradation and inhibits the canonical Wnt signaling pathway. Participates also in neurite growth in spiral ganglion neurons. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation of the circadian clock. Phosphorylates POU5F1, which results in the inhibition of POU5F1's transcriptional activity and enhances its proteosomal degradation (By similarity).

MAPK9 isoforms display different binding patterns: alpha-1 and alpha-2 preferentially bind to JUN, whereas beta-1 and beta-2 bind to ATF2. However, there is no correlation between binding and phosphorylation, which is achieved at about the same efficiency by all isoforms. JUNB is not a substrate for JNK2 alpha-2, and JUND binds only weakly to it.

PTMs:

Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and MAP2K4, which activates the enzyme. Autophosphorylated in vitro.

Subcellular Location:

Cytoplasm. Nucleus.
Note: Colocalizes with POU5F1 in the nucleus.

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

Interacts with MECOM (By similarity). Interacts with DCLK2 (By similarity). Binds to at least four scaffolding proteins, MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK8IP3/JIP-3/JSAP1 and SPAG9/MAPK8IP4/JIP-4. These proteins also bind other components of the JNK signaling pathway (By similarity). Interacts with NFATC4. Interacts with ATF7; the interaction does not phosphorylate ATF7 but acts as a docking site for ATF7-associated partners such as JUN. Interacts with BCL10. Interacts with CTNNB1 and GSK3B. Interacts with MAPKBP1. Interacts with POU5F1; phosphorylates POU5F1 at 'Ser-355'. Found in a complex with SH3RF1, RAC2, MAP3K7/TAK1, MAP2K7/MKK7, MAPK8IP1/JIP1 and MAPK8/JNK1 (By similarity).

Family&Domains:

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.

Function:

Serine/threonine-protein kinase involved in various processes such as neuronal proliferation, differentiation, migration and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK10/JNK3. In turn, MAPK10/JNK3 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. Plays regulatory roles in the signaling pathways during neuronal apoptosis. Phosphorylates the neuronal microtubule regulator STMN2. Acts in the regulation of the amyloid-beta precursor protein/APP signaling during neuronal differentiation by phosphorylating APP. Participates also in neurite growth in spiral ganglion neurons. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the photic regulation of the circadian clock. Phosphorylates JUND and this phosphorylation is inhibited in the presence of MEN1.

PTMs:

Dually phosphorylated on Thr-221 and Tyr-223 by MAP2K4 and MAP2K7, which activates the enzyme. MAP2K7 shows a strong preference for Thr-221 while MAP2K4 phosphorylates Tyr-223 preferentially. Weakly autophosphorylated on threonine and tyrosine residues in vitro.

Palmitoylation regulates subcellular location and axonal development.

Subcellular Location:

Cytoplasm. Membrane>Lipid-anchor. Nucleus. Mitochondrion.
Note: Palmitoylation regulates MAPK10 trafficking to cytoskeleton. Recruited to the mitochondria in the presence of SARM1 (By similarity).

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

Specific to a subset of neurons in the nervous system. Present in the hippocampus and areas, cerebellum, striatum, brain stem, and weakly in the spinal cord. Very weak expression in testis and kidney.

Subunit Structure:

Interacts with MAPKBP1 (By similarity). Interacts with MAPK8IP1/JIP-1 and MAPK8IP3/JIP-3/JSAP1 (By similarity). Interacts with SPAG9/MAPK8IP4/JIP4. Interacts with HDAC9. Interacts with ARRB2; the interaction enhances MAPK10 activation by MAP3K5. Interacts with SARM1 (By similarity). Interacts with JUND; interaction is inhibited in the presence of MEN1.

Family&Domains:

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.

Research Fields

· Cellular Processes > Transport and catabolism > Autophagy - animal.   (View pathway)

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

· Cellular Processes > Cell growth and death > Apoptosis - multiple species.   (View pathway)

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

· Cellular Processes > Cellular community - eukaryotes > Focal adhesion.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Tight junction.   (View pathway)

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

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

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

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

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

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

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

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

· Genetic Information Processing > Folding, sorting and degradation > Protein processing in endoplasmic reticulum.   (View pathway)

· Human Diseases > Drug resistance: Antineoplastic > Endocrine resistance.

· Human Diseases > Endocrine and metabolic diseases > Type II diabetes mellitus.

· Human Diseases > Endocrine and metabolic diseases > Insulin resistance.

· Human Diseases > Endocrine and metabolic diseases > Non-alcoholic fatty liver disease (NAFLD).

· Human Diseases > Infectious diseases: Bacterial > Epithelial cell signaling in Helicobacter pylori infection.

· Human Diseases > Infectious diseases: Bacterial > Shigellosis.

· Human Diseases > Infectious diseases: Bacterial > Salmonella infection.

· Human Diseases > Infectious diseases: Bacterial > Pertussis.

· Human Diseases > Infectious diseases: Parasitic > Chagas disease (American trypanosomiasis).

· Human Diseases > Infectious diseases: Parasitic > Toxoplasmosis.

· Human Diseases > Infectious diseases: Bacterial > Tuberculosis.

· Human Diseases > Infectious diseases: Viral > Hepatitis C.

· Human Diseases > Infectious diseases: Viral > Hepatitis B.

· Human Diseases > Infectious diseases: Viral > Influenza A.

· Human Diseases > Infectious diseases: Viral > HTLV-I infection.

· Human Diseases > Infectious diseases: Viral > Herpes simplex infection.

· Human Diseases > Infectious diseases: Viral > Epstein-Barr virus infection.

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

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

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

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

· Organismal Systems > Development > Osteoclast differentiation.   (View pathway)

· Organismal Systems > Immune system > Toll-like receptor signaling pathway.   (View pathway)

· Organismal Systems > Immune system > NOD-like receptor signaling pathway.   (View pathway)

· Organismal Systems > Immune system > RIG-I-like receptor signaling pathway.   (View pathway)

· Organismal Systems > Immune system > IL-17 signaling pathway.   (View pathway)

· Organismal Systems > Immune system > Th1 and Th2 cell differentiation.   (View pathway)

· Organismal Systems > Immune system > Th17 cell differentiation.   (View pathway)

· Organismal Systems > Immune system > T cell receptor signaling pathway.   (View pathway)

· Organismal Systems > Immune system > Fc epsilon RI signaling pathway.   (View pathway)

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

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

· Organismal Systems > Nervous system > Dopaminergic synapse.

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

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

· Organismal Systems > Endocrine system > Progesterone-mediated oocyte maturation.

· Organismal Systems > Endocrine system > Prolactin signaling pathway.   (View pathway)

· Organismal Systems > Endocrine system > Adipocytokine signaling pathway.

· Organismal Systems > Endocrine system > Relaxin signaling pathway.

References

1). Hepatoma cell-intrinsic TLR9 activation induces immune escape through PD-L1 upregulation in hepatocellular carcinoma. Theranostics (PubMed: 32483468) [IF=12.4]

2). p47phox deficiency impairs platelet function and protects mice against arterial and venous thrombosis. Redox Biology (PubMed: 32422541) [IF=11.4]

Application: WB    Species: Human    Sample: platelets

Fig. 4. ROS generation and phosphorylation of VASP, ERK1/2, p38 MAPK, ERK5, JNK, AKT and c-PLA2. (A) Western blot analysis of the expression of NOX2, p67phox, NOX1, NOXO1 and Rac in WT and p47phox-/- platelets. (B) ROS generation in platelets after stimulation with CRP (2 μg/ml) or thrombin (0.5 U/ml) was expressed as mean fluorescent intensity (MFI) (mean ± SE, n = 6) (Student t-test). (C) The phosphorylation level of VASP, ERK1/2, p38, ERK5 and JNK in CRPstimulated platelets was detected by western blot and (D) quantified as a ratio relative to the total level (mean ± SD, n = 3) (Two-way ANOVA). (E) The phosphorylation level of AKT and c-PLA2 was also detected and (F) quantified (mean ± SD, n = 3) (Two-way ANOVA). *p < 0.05; **p < 0.01; ***p < 0.001.

3). Elamipretide alleviates pyroptosis in traumatically injured spinal cord by inhibiting cPLA2-induced lysosomal membrane permeabilization. Journal of Neuroinflammation (PubMed: 36609266) [IF=9.3]

4). A De Novo Frameshift Mutation in TNFAIP3 Impairs A20 Deubiquitination Function to Cause Neuropsychiatric Systemic Lupus Erythematosus. JOURNAL OF CLINICAL IMMUNOLOGY (PubMed: 31625129) [IF=9.1]

Application: WB    Species: human    Sample: T cells

Fig. 2| Impaired ubiquitin editing function of mutant A20 activated NFκB and MAPK pathway.c NF-κB and MAPK pathways were activated in stimulated patient-derived T cells. Patient-derived T cells were stimulated with TNF-α (50 ng/ml). Whole cell lysates were immunoblotted with respective target proteins. Healthy parents from the pedigree served as healthy controls

5). LncRNA CD27-AS1 promotes acute myeloid leukemia progression through the miR-224-5p/PBX3 signaling circuit. Cell Death & Disease (PubMed: 34006845) [IF=9.0]

Application: WB    Species: Human    Sample: AML cells

Fig. 5 CD27-AS1 regulates MAPK signaling pathway in the AML cell lines. a HL-60 and KG-1 cells were infected with LV-CD27-AS1 and LV-CD27- AS1-Sh1. Protein levels of P38, p-P38, JNK, p-JNK, p-C-raf, p-MEK1/2, ERK, and p-ERK were detected using western blotting. b Densitometry analysis of protein levels in both cells was performed. c U0126, a MEK1/2 inhibitor, was used to treat the AML cells with CD27-AS1 upregulation. Relative protein levels of p-ERK and ERK were measured using western blotting. d CCK-8 assay was performed to check cell viability. N = 3. Data were shown as means ± SD. *P < 0.05, **P < 0.01, and ***P < 0.001.

6). LAGE3 promoted cell proliferation, migration, and invasion and inhibited cell apoptosis of hepatocellular carcinoma by facilitating the JNK and ERK signaling pathway. CELLULAR & MOLECULAR BIOLOGY LETTERS (PubMed: 34837962) [IF=8.3]

Application: WB    Species: Human    Sample: Hep-3B cells

Fig. 6 LAGE3 aggravated HCC progression by enhancing the JNK and ERK signaling pathway. Hep-3B cells were transfected with LAGE3-OE and then incubated with ERK inhibitor SCH772984 or JNK inhibitor SP600125. A Western blot bands of p-p38, p38, p-JNK, JNK, p-ERK, and ERK in Hep3B cells. B Proliferation ability of Hep3B cells. C–D Migration and invasion abilities of Hep3B cells. Data are shown as mean ± standard deviation. *p < 0.05, **p < 0.01

7). Separation, purification, structural analysis and immune-enhancing activity of sulfated polysaccharide isolated from sea cucumber viscera. International Journal of Biological Macromolecules (PubMed: 31712137) [IF=8.2]

Application: WB    Species: Mouse    Sample: RAW264.7 cells

Fig.14 Effect of MAPKs signaling pathways on SCVP-1-induced macrophage activation. (A) The effect of SCVP-1 on the level of phosphorylation of ERK1/2, p38 and JNK1/2 in RAW264.7 cells by Western blotting. (B) Relative quantitative analysis of p-p38/p38, p-ERK/ERK and p-JNK/JNK protein phosphorylation levels. (C-F) Effect of specific MAPKs inhibitors (ERK1/2 inhibitor: CI-1040, p38 inhibitor: SB239063 and JNK1/2 inhibitor: SP600125) on SCVP-1/LPS-induced NO, IL-1β, IL-6 and TNF-α production of RAW264.7 cells. The results were expressed as means ± SD (n = 3). (B) *p<0.05, **p<0.01 vs. control group. (C-F) *p<0.05, **p<0.01 vs. without anti-MAPKs antibodies

8). Prostaglandin E1 attenuates high glucose-induced apoptosis in proximal renal tubular cells by inhibiting the JNK/Bim pathway. ACTA PHARMACOLOGICA SINICA (PubMed: 31685975) [IF=8.2]

Application: WB    Species: Human    Sample: HK-2 cells

Fig. 5 PGE1 suppressed Bim, Bax, caspase-3, cleaved caspase-3 expression and phosphorylation of JNK in HK-2 cells. a Bim expression in HK-2 cells was detected by immunofluorescence (×600 magnification). The red fluorescence represents Bim expression, and blue fluorescence represents nuclei. b, c Western blot analysis of Bax, caspase-3 and cleaved caspase-3 expression in the MG, HG and HG + PGE1 groups. The data represent the means ± SEM. *P < 0.05, **P < 0.01 versus HG group. d, e Western blot analysis of Bim, p-JNK and JNK expression in the MG, HG and HG + PGE1 groups. f qRT-PCR was performed to determine the mRNA levels of Bim, Bax, and caspase-3 in HK-2 cells. The data represent the means ± SEM. *P < 0.05, **P < 0.01 versus the HG group

9). Total flavonoids of Inula japonica alleviated the inflammatory response and oxidative stress in LPS-induced acute lung injury via inhibiting the sEH activity: Insights from lipid metabolomics. PHYTOMEDICINE (PubMed: 36150346) [IF=7.9]

10). Trimethylamine N-oxide promotes atherosclerosis via CD36-dependent MAPK/JNK pathway. BIOMEDICINE & PHARMACOTHERAPY (PubMed: 29136772) [IF=7.5]

Load more

Restrictive clause

 

Affinity Biosciences tests all products strictly. Citations are provided as a resource for additional applications that have not been validated by Affinity Biosciences. Please choose the appropriate format for each application and consult Materials and Methods sections for additional details about the use of any product in these publications.

For Research Use Only.
Not for use in diagnostic or therapeutic procedures. Not for resale. Not for distribution without written consent. Affinity Biosciences will not be held responsible for patent infringement or other violations that may occur with the use of our products. Affinity Biosciences, Affinity Biosciences Logo and all other trademarks are the property of Affinity Biosciences LTD.