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Home / Assay Kits / ELISA Kits

ELISA Kit for Mouse Serine/threonine-protein kinase pim-1

SKU : BHE13809198

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EIAAB SCIENCE INC, WUHAN

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Mfr.No.	E1997m
Alternative Names	Pim-1
Categories	Elisa
Function	May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3 (By similarity). Promotes the G1/S transition of the cell cycle via up-regulation of CDK2 activity and phosphorylation of CDKN1B, resulting in enhanced nuclear export and proteasome-dependent degradation of CDKN1B (By similarity). Also represses CDKN1B transcription by phosphorylating and inactivating the transcription factor FOXO3 (By similarity). Plays a role in signal transduction in blood cells (By similarity). Contributes to both cell proliferation and survival thus providing a selective advantage in tumorigenesis.
Specificity	Natural and recombinant Mouse Serine/threonine-protein kinase pim-1
Subcellular Location	Cytoplasm Nucleus
Detection Range	0.156-10ng/mL
Entryname	PIM1_MOUSE
Method Type	Sandwich
Platform	PF00069
Protein Name	Serine/threonine-protein kinase pim-1
Sensitivity	0.082ng/mL
Sequence	50: MGPAAPLALP ; PPALPDPAGE ; PARGQPRQRP ; QSSSDSPSAL ; RASRSQSRNA ; 100: TRSLSPGRRL ; SPSSLRRRCC ; SSRHRRRTDT ; LEVGMLLSKI ; NSLAHLRARP ; 150: CNDLHATKLA ; PGKEKEPLES ; QYQVGPLLGS ; GGFGSVYSGI ; RVADNLPVAI ; 200: KHVEKDRISD ; WGELPNGTRV ; PMEVVLLKKV ; SSDFSGVIRL ; LDWFERPDSF ; 250: VLILERPEPV ; QDLFDFITER ; GALQEDLARG ; FFWQVLEAVR ; HCHNCGVLHR ; 300: DIKDENILID ; LSRGEIKLID ; FGSGALLKDT ; VYTDFDGTRV ; YSPPEWIRYH ; 350: RYHGRSAAVW ; SLGILLYDMV ; CGDIPFEHDE ; EIIKGQVFFR ; QTVSSECQHL ; 397: IKWCLSLRPS ; DRPSFEEIRN ; HPWMQGDLLP ; QAASEIHLHS ; LSPGSSK
Sequence Length	397
String	P06803
Sub Unit	Binds to RP9. Interacts with CDKN1B and FOXO3 (By similarity). Isoform 2 is isolated as a monomer whereas isoform 1 complexes with other proteins. Isoform 1, but not isoform 2, binds BMX.

Uniprot	P06803
Gene Name	Pim1
Immunogen Species	Mus musculus (Mouse)
Unigene	Mm.405293

Reference	1. "The primary structure of the putative oncogene pim-1 shows extensive homology with protein kinases." Selten G., Cuypers H.T., Boelens W., Robanus-Maandag E., Verbeek J., Domen J., van Beveren C., Berns A. Cell46:603-611(1986) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2) 2. "The pim-1 oncogene encodes two related protein-serine/threonine kinases by alternative initiation at AUG and CUG." Saris C.J., Domen J., Berns A. EMBO J.10:655-664(1991) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);ALTERNATIVE INITIATION;FUNCTION;COMPLEX FORMATION;AUTOPHOSPHORYLATION;SUBCELLULAR LOCATION;MUTAGENESIS OF LYS-151 3. "Impaired interleukin-3 response in Pim-1-deficient bone marrow-derived mast cells." Domen J., van der Lugt N.M., Laird P.W., Saris C.J., Clarke A.R., Hooper M.L., Berns A. Blood82:1445-1452(1993) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: DISRUPTION PHENOTYPE 4. "Pim-1 levels determine the size of early B lymphoid compartments in bone marrow." Domen J., van der Lugt N.M., Acton D., Laird P.W., Linders K., Berns A. J. Exp. Med.178:1665-1673(1993) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: DISRUPTION PHENOTYPE 5. "PAP-1, a novel target protein of phosphorylation by Pim-1 kinase." Maita H., Harada Y., Nagakubo D., Kitaura H., Ikeda M., Tamai K., Takahashi K., Ariga H., Iguchi-Ariga S.M.M. Eur. J. Biochem.267:5168-5178(2000) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH RP9 6. "Pim-1 kinase promotes inactivation of the pro-apoptotic Bad protein by phosphorylating it on the Ser112 gatekeeper site." Aho T.L., Sandholm J., Peltola K.J., Mankonen H.P., Lilly M., Koskinen P.J. FEBS Lett.571:43-49(2004) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN PHOSPHORYLATION OF BAD;INTERACTION WITH BAD 7. "Mice deficient for all PIM kinases display reduced body size and impaired responses to hematopoietic growth factors." Mikkers H., Nawijn M., Allen J., Brouwers C., Verhoeven E., Jonkers J., Berns A. Mol. Cell. Biol.24:6104-6115(2004) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: DISRUPTION PHENOTYPE;FUNCTION 8. "Pim kinase-dependent inhibition of c-Myc degradation." Zhang Y., Wang Z., Li X., Magnuson N.S. Oncogene27:4809-4819(2008) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN PHOSPHORYLATION OF MYC;INTERACTION WITH MYC 9. "Dissection of PIM serine/threonine kinases in FLT3-ITD-induced leukemogenesis reveals PIM1 as regulator of CXCL12-CXCR4-mediated homing and migration." Grundler R., Brault L., Gasser C., Bullock A.N., Dechow T., Woetzel S., Pogacic V., Villa A., Ehret S., Berridge G., Spoo A., Dierks C., Biondi A., Knapp S., Duyster J., Schwaller J. J. Exp. Med.206:1957-1970(2009) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN PHOSPHORYLATION OF CXCR4;FUNCTION IN CELL MIGRATION

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