• Western blot analysis of lysates from mouse brain, using PAK1/2/3 (Phospho-Ser144/141/139) Antibody. The lane on the right is blocked with the phospho peptide.
  • Immunohistochemistry analysis of paraffin-embedded human brain, using PAK1/2/3 (Phospho-Ser144/141/139) Antibody. The picture on the right is blocked with the phospho peptide.

Anti-Phospho-PAK Alpha/Beta/Gamma-Ser144/141/139 antibody (111-160 aa) (STJ90827)

SKU:
STJ90827

Current Stock:
Host: Rabbit
Applications: WB/IHC/IF/ELISA
Reactivity: Human/Mouse/Rat
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Rabbit polyclonal antibody anti-Phospho-Serine/threonine-protein kinase PAK 1 and Serine/threonine-protein kinase PAK 2 and Serine/threonine-protein kinase PAK 3-Ser144/141/139 (111-160 aa) is suitable for use in Western Blot, Immunohistochemistry, I
Clonality: Polyclonal
Conjugation: Unconjugated
Isotype: IgG
Formulation: Liquid in PBS containing 50% Glycerol, 0.5% BSA and 0.02% Sodium Azide.
Purification: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Concentration: 1 mg/mL
Dilution Range: WB 1:500-1:2000
IHC 1:100-1:300
ELISA 1:10000
IF 1:50-200
Storage Instruction: Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles.
Gene Symbol: PAK2
PAK1
5062
5058
5063
PAK2_HUMAN
PAK1_HUMAN
PAK3_HUMAN
Immunogen Region: 111-160 aa
Specificity: Phospho-PAK Alpha/Beta/Gamma (S144/141/139) Polyclonal Antibody detects endogenous levels of PAK Alpha/Beta/Gamma protein only when phosphorylated at S144/141/139.
Immunogen: The antiserum was produced against synthesized peptide derived from the human PAK1/2/3 around the phosphorylation site of Ser144/141/139 at the amino acid range 111-160
Post Translational Modifications Autophosphorylated in trans, meaning that in a dimer, one kinase molecule phosphorylates the other one. Activated by autophosphorylation at Thr-423 in response to a conformation change, triggered by interaction with GTP-bound CDC42 or RAC1. Activated by phosphorylation at Thr-423 by BRSK2 and by PDPK1. Phosphorylated by JAK2 in response to PRL.this increases PAK1 kinase activity. Phosphorylated at Ser-21 by PKB/AKT.this reduces interaction with NCK1 and association with focal adhesion sites. Upon DNA damage, phosphorylated at Thr-212 and translocates to the nucleoplasm. Phosphorylated at tyrosine residues, which can be enhanced by NTN1.
Function Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes. Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2. Phosphorylates SNAI1 at 'Ser-246' promoting its transcriptional repressor activity by increasing its accumulation in the nucleus. In podocytes, promotes NR3C2 nuclear localization. Required for atypical chemokine receptor ACKR2-induced phosphorylation of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation. Plays a role in RUFY3-mediated facilitating gastric cancer cells migration and invasion. In response to DNA damage, phosphorylates MORC2 which activates its ATPase activity and facilitates chromatin remodeling.
Protein Name Serine/Threonine-Protein Kinase Pak 1
Alpha-Pak
P21-Activated Kinase 1
Pak-1
P65-Pak
Database Links Reactome: R-HSA-202433
Reactome: R-HSA-2029482
Reactome: R-HSA-2871796
Reactome: R-HSA-376172
Reactome: R-HSA-389359
Reactome: R-HSA-3928662
Reactome: R-HSA-3928664
Reactome: R-HSA-399954
Reactome: R-HSA-428540
Reactome: R-HSA-445144
Reactome: R-HSA-445355
Reactome: R-HSA-5218920
Reactome: R-HSA-5621575
Reactome: R-HSA-5625740
Reactome: R-HSA-5627117
Reactome: R-HSA-5627123
Reactome: R-HSA-5687128
Reactome: R-HSA-8964616
Cellular Localisation Cytoplasm
Cell Junction
Focal Adhesion
Cell Membrane
Cell Projection
Ruffle Membrane
Invadopodium
Nucleus
Nucleoplasm
Chromosome
Colocalizes With Rufy3
F-Actin And Other Core Migration Components In Invadopodia At The Cell Periphery
Recruited To The Cell Membrane By Interaction With Cdc42 And Rac1
Recruited To Focal Adhesions Upon Activation
Colocalized With Cib1 Within Membrane Ruffles During Cell Spreading Upon Readhesion To Fibronectin
Upon Dna Damage
Translocates To The Nucleoplasm When Phosphorylated At Thr-212 Where Is Co-Recruited With Morc2 On Damaged Chromatin
Alternative Antibody Names Anti-Serine/Threonine-Protein Kinase Pak 1 antibody
Anti-Alpha-Pak antibody
Anti-P21-Activated Kinase 1 antibody
Anti-Pak-1 antibody
Anti-P65-Pak antibody
Anti-PAK1 antibody

Information sourced from Uniprot.org

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