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PIN4 encodes a member of the parvulin subfamily of the peptidyl-prolyl cis/trans isomerase protein family. Additionally we are shipping PIN4 Antibodies (46) and PIN4 Kits (14) and many more products for this protein.
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Data indicate the association of Par14 with insulin receptor substrate 1 (IRS-1 (show IRS1 Proteins)) in human HepG2 cells overexpressing both as well as endogenously in the mouse liver.
Par14 can be described as an endogenous non-histone chromatin protein, which binds DNA in vivo
Ca(2 (show CA2 Proteins)+)/Calmodulin (show CALM1 Proteins) binding to the N-terminal of Par17 causes steric hindrance of the Par17 active site, thus interfering with the Par17/tubulin (show TUBB Proteins) interaction.
Data indicate that Pin1 (show PIN1 Proteins) prolyl isomerase active site cysteine, Cys113, is highly susceptible to oxidation.
The N-terminal basic domain of human parvulin (show PPIC Proteins) hPar14 is responsible for the entry to the nucleus and high-affinity DNA-binding.
subcellular localization and DNA binding properties of hPar14 are regulated by phosphorylation of the N-terminal domain
Identification of a longer Parvulin (show PPIC Proteins) isoform (Par17) that has an extension at the 5' end including a 75 bp extended open reading frame.
This gene encodes a member of the parvulin subfamily of the peptidyl-prolyl cis/trans isomerase protein family. The encoded protein catalyzes the isomerization of peptidylprolyl bonds, and may play a role in the cell cycle, chromatin remodeling, and/or ribosome biogenesis. The encoded protein may play an additional role in the mitochondria.
, peptidyl-prolyl cis-trans isomerase NIMA-interacting 4
, peptidyl-prolyl cis-trans isomerase Pin4
, rotamase Pin4
, PPIase PIN4
, eukaryotic parvulin homolog
, peptidyl-prolyl cis/trans isomerase EPVH
, rotamase PIN4
, protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting, 4 (parvulin)
, protein NIMA-interacting, 4
, Rotamase Pin4
, putative peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 variant 1