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PKN1 Antibody

Purified Rabbit Polyclonal Antibody (Pab)

     
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, ICC
Primary Accession Q16512
Reactivity Human, Mouse
Host Rabbit
Clonality Polyclonal
Calculated MW 103932 Da
Additional Information
Gene ID 5585
Other Names Serine/threonine-protein kinase N1, Protease-activated kinase 1, PAK-1, Protein kinase C-like 1, Protein kinase C-like PKN, Protein kinase PKN-alpha, Protein-kinase C-related kinase 1, Serine-threonine protein kinase N, PKN1, PAK1, PKN, PRK1, PRKCL1
Dilution WB~~1:1000
ICC~~N/A
Format 0.01M PBS, pH 7.2, 0.09% (W/V) Sodium azide, Glycerol 50%
StorageStore at -20 °C.Stable for 12 months from date of receipt
Protein Information
Name PKN1
Synonyms PAK1, PKN, PRK1, PRKCL1
Function PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro.
Cellular Location Cytoplasm. Nucleus Endosome. Cell membrane {ECO:0000250|UniProtKB:Q63433}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q63433}. Cleavage furrow. Midbody Note=Associates with chromatin in a ligand-dependent manner Localization to endosomes is mediated via its interaction with RHOB Association to the cell membrane is dependent on Ser-377 phosphorylation. Accumulates during telophase at the cleavage furrow and finally concentrates around the midbody in cytokinesis {ECO:0000250|UniProtKB:Q63433, ECO:0000269|PubMed:17332740}
Tissue Location Found ubiquitously. Expressed in heart, brain, placenta, lung, skeletal muscle, kidney and pancreas. Expressed in numerous tumor cell lines, especially in breast tumor cells
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser- 159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro.

REFERENCES

Mukai H.,et al.Biochem. Biophys. Res. Commun. 199:897-904(1994).
Palmer R.H.,et al.Eur. J. Biochem. 227:344-351(1995).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Grimwood J.,et al.Nature 428:529-535(2004).
Palmer R.H.,et al.FEBS Lett. 356:5-8(1994).

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