M130; MBS; Myosin binding subunit; Myosin phosphatase target subunit 1; Myosin phosphatase targeting subunit 1; Myosin phosphatase-targeting subunit 1; MYPT1; MYPT1_HUMAN; PPP1R12A; Protein phosphatase 1 regulatory inhibitor subunit 12A; Protein phosphatase 1 regulatory subunit 12A; Protein phosphatase 1, regulatory (inhibitor) subunit 12A; Protein phosphatase myosin binding subunit; Protein phosphatase myosin-binding subunit;
WB 1:500-1:2000, IHC 1:50-1:200, ELISA(peptide) 1:20000-1:40000
Human, Mouse, Rat
Zebrafish(100%), Horse(100%), Rabbit(100%), Dog(100%), Chicken(100%), Xenopus(88%)
The antibody is from purified rabbit serum by affinity purification via sequential chromatography on phospho-peptide and non-phospho-peptide affinity columns.
Phospho-MYPT1 (Thr853) Antibody detects endogenous levels of MYPT1 only when phosphorylated at Thr853.
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.
A synthesized peptide derived from human MYPT1 around the phosphorylation site of Thr853.
Observed Mol.Wt.: 115 kDa.
Predicted Mol.Wt.: 116kDa.
Cytoplasm. Along actomyosin filaments and stress fibers.
Expressed in striated muscles, specifically in type 2a fibers (at protein level).
Heterotetramerization is mediated by the interaction between a coiled-coil of PRKG1 and the leucine/isoleucine zipper of PPP1R12A/MBS, the myosin-binding subunit of the myosin phosphatase.
10 20 30 40 50
MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS
60 70 80 90 100
GDTDEVLKLL HRGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN
110 120 130 140 150
QPDNEGWIPL HAAASCGYLD IAEFLIGQGA HVGAVNSEGD TPLDIAEEEA
160 170 180 190 200
MEELLQNEVN RQGVDIEAAR KEEERIMLRD ARQWLNSGHI NDVRHAKSGG
210 220 230 240 250
TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA HWGKEEACRI
260 270 280 290 300
LVDNLCDMEM VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKRDKKSP
310 320 330 340 350
LIESTANMDN NQSQKTFKNK ETLIIEPEKN ASRIESLEQE KVDEEEEGKK
360 370 380 390 400
DESSCSSEED EEDDSESEAE TDKTKPLASV TNANTSSTQA APVAVTTPTV
410 420 430 440 450
SSGQATPTSP IKKFPTTATK ISPKEEERKD ESPATWRLGL RKTGSYGALA
460 470 480 490 500
EITASKEGQK EKDTAGVTRS ASSPRLSSSL DNKEKEKDSK GTRLAYVAPT
510 520 530 540 550
IPRRLASTSD IEEKENRDSS SLRTSSSYTR RKWEDDLKKN SSVNEGSTYH
560 570 580 590 600
KSCSFGRRQD DLISSSVPST TSTPTVTSAA GLQKSLLSST STTTKITTGS
610 620 630 640 650
SSAGTQSSTS NRLWAEDSTE KEKDSVPTAV TIPVAPTVVN AAASTTTLTT
660 670 680 690 700
TTAGTVSSTT EVRERRRSYL TPVRDEESES QRKARSRQAR QSRRSTQGVT
710 720 730 740 750
LTDLQEAEKT IGRSRSTRTR EQENEEKEKE EKEKQDKEKQ EEKKESETSR
760 770 780 790 800
EDEYKQKYSR TYDETYQRYR PVSTSSSTTP SSSLSTMSSS LYASSQLNRP
810 820 830 840 850
NSLVGITSAY SRGITKENER EGEKREEEKE GEDKSQPKSI RERRRPREKR
860 870 880 890 900
RSTGVSFWTQ DSDENEQEQQ SDTEEGSNKK ETQTDSISRY ETSSTSAGDR
910 920 930 940 950
YDSLLGRSGS YSYLEERKPY SSRLEKDDST DFKKLYEQIL AENEKLKAQL
960 970 980 990 1000
HDTNMELTDL KLQLEKATQR QERFADRSLL EMEKRERRAL ERRISEMEEE
1010 1020 1030
LKMLPDLKAD NQRLKDENGA LIRVISKLSK
Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity.
Phosphorylated by CIT (Rho-associated kinase) (By similarity). Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-696. Phosphorylated on upon DNA damage, probably by ATM or ATR. In vitro, phosphorylation of Ser-695 by PKA and PKG appears to prevent phosphorylation of the inhibitory site Thr-696, probably mediated by PRKG1. Phosphorylation at Ser-445, Ser-472 and Ser-910 by NUAK1 promotes interaction with 14-3-3, leading to inhibit interaction with myosin light chain MLC2, preventing dephosphorylation of MLC2. May be phosphorylated at Thr-696 by DMPK; may inhibit the myosin phosphatase activity. Phosphorylated at Ser-473 by CDK1 during mitosis, creating docking sites for the POLO box domains of PLK1. Subsequently, PLK1 binds and phosphorylates PPP1R12A.
PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, and one or several targeting or regulatory subunits. PPP1R12A mediates binding to myosin. Interacts with ARHA and CIT (By similarity). Binds PPP1R12B, ROCK1 and IL16. Interacts directly with PRKG1. Non-covalent dimer of 2 dimers; PRKG1-PRKG1 and PPP1R12A-PPP1R12A. Interacts with SMTNL1 (By similarity). Interacts with PPP1CB; the interaction is direct. Interacts (when phosphorylated at Ser-445, Ser-472 and Ser-910) with 14-3-3. Interacts with ROCK1 and ROCK2. Interacts with isoform 1 and isoform 2 of ZIPK/DAPK3. Interacts with RAF1. Interacts with HIF1AN. Interacts with NCKAP1L (PubMed:16417406).
Heterotetramerization is mediated by the interaction between a coiled-coil of PRKG1 and the leucine/isoleucine zipper of PPP1R12A/MBS, the myosin-binding subunit of the myosin phosphatase.The KVKF motif mediates interaction with PPP1CB.
· Cellular Processes > Cellular community - eukaryotes > Focal adhesion.(View pathway)
· Cellular Processes > Cell motility > Regulation of actin cytoskeleton.(View pathway)
· Environmental Information Processing > Signal transduction > cGMP-PKG signaling pathway.(View pathway)
· Environmental Information Processing > Signal transduction > cAMP signaling pathway.(View pathway)
· Human Diseases > Cancers: Overview > Proteoglycans in cancer.
· Organismal Systems > Immune system > Platelet activation.(View pathway)
· Organismal Systems > Circulatory system > Vascular smooth muscle contraction.(View pathway)
· Organismal Systems > Endocrine system > Oxytocin signaling pathway.
Application: WB Species:rat; Sample:Not available
Figure 4. Effect of Ac-SDKP on col I, α-SMA and α-Ac-Tub in fibroblasts induced by Ang II. (a) The coexpression of α-SMA and α-Ac-Tub in fibroblasts induced by Ang II measured by immunofluorescence. Scale bar=50μm. (b) Effect of Ac-SDKP, valsartan (AT1 inhibitor), TCS HDAC6 20b (specific HDAC6 inhibitor), and Y-27632 (ROCK inhibitor) on fibroblasts measured by Western blot. Data presented as mean±SEM; N=4 independent experiments.
Application: WB Species:rat; Sample:Not available
Fig. 3. Icariin treatment increased active RhoA in rASCs. (A) The active and total RhoA protein levels were determined by Western blot analysis on days 0, 1, 3, 5, 7 and 9. The densitometric analysis of active RhoA protein expression was normalized to total RhoA. (B) The p-MYPT1 and GAPDH protein levels were determined by Western blot analysis on days 0, 1, 3, 5, 7 and 9. The densitometric analysis of p-MYPT1 protein expression was normalized to GAPDH. Data are shown as mean SD (n = 3) in three independent experiments. *P < 0.05 compared to 0 day group.
Tips: For phospho antibody, we provide phospho peptide（0.5mg) and non-phospho peptide(0.5mg).
Blocking peptides are peptides that bind specifically to the target antibody and block antibody binding. These peptide usually contains the epitope recognized by the antibody. Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. This mechanism is useful when non-specific binding is an issue, for example, in Western blotting (immunoblot) and immunohistochemistry (IHC). By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific; Specific binding will be absent from the western blot or immunostaining performed with the neutralized antibody.
Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 10 mg/ml.The purity is >90%,tested by HPLC and MS.Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
This product is for research use only. Not for use in diagnostic or therapeutic procedures.
|S445||Phosphorylation||O60285 (NUAK1) , O95835 (LATS1)||Uniprot|
|S695||Phosphorylation||P17612 (PRKACA) , Q13976 (PRKG1)||Uniprot|
|T696||Phosphorylation||Q09013 (DMPK) , P04049 (RAF1) , Q13464 (ROCK1) , P17612 (PRKACA) , O75116 (ROCK2) , Q13418 (ILK)||Uniprot|
|S852||Phosphorylation||P17612 (PRKACA) , O75116 (ROCK2) , Q13976 (PRKG1) , Q9Y5S2 (CDC42BPB) , Q13464 (ROCK1)||Uniprot|
|T853||Phosphorylation||P17612 (PRKACA) , Q13464 (ROCK1) , Q04759 (PRKCQ)||Uniprot|