IQGAP1 Antibody from MyBioSource.com

Supplier Page

Supplier Page from
MyBioSource.com for
IQGAP1 Antibody

Get Pricing
MyBioSource.com's IQGAP1 Antibody is a Rabbit Polyclonal antibody. This antibody has been shown to work in applications such as: ELISA, Immunocytochemistry, Immunofluorescence, and Western Blot. The IQGAP1 Antibody was generated using IQGAP1 as the antigen and it reacts with Human, and Mouse.

Description

Function: Plays a crucial role in regulating the dynamics and assembly of the actin cytoskeleton. Binds to activated CDC42 but does not stimulate its GTPase activity. It associates with calmodulin. Could serve as an assembly scaffold for the organization of a multimolecular complex that would interface incoming signals to the reorganization of the actin cytoskeleton at the plasma membrane. May promote neurite outgrowth (PubMed:15695813). May play a possible role in cell cycle regulation by contributing to cell cycle progression after DNA replication arrest (PubMed:20883816).
Subunit Structure: Interacts with CDC42; the interaction is demonstrated with IQGAP1 in GTP-bound and in nucleotide-free state (PubMed:15355962). Interacts with RAC1 (PubMed:15355962). Does not interact with RHOA. Interacts with TSG101 (PubMed:17853893). Interacts with PAK6 (PubMed:18642328). Interacts with TMEM14B; this interaction increases IQGAP1 phosphorylation and induces its nuclear translocation (PubMed:29033352).
Post-translational Modifications: Phosphorylation of Ser-1443 by PKC/PRKCE prevents interaction between C1 and C2, allowing binding of nucleotide-free CDC42. Ser-1443 phosphorylation enhances the ability to promote neurite outgrowth.
Similarity: Regions C1 and C2 can either interact with nucleotide-free CDC42, or interact together, depending on the phosphorylation state of Ser-1443. When Ser-1443 is not phosphorylated, C1 and C2 interact, which prevents binding of nucleotide-free CDC42 and promotes binding of GTP-bound CDC42. Phosphorylation of Ser-1443 prevents interaction between C1 and C2, which opens the structure of the C-terminus and allows binding and sequestration of nucleotide-free CDC42 on both C1 and C2