Girdin (Tyr-1764), Phosphospecific Antibody

Product Specifications

Background

Girdin, a member of the CCDC88 (Hook related protein) family, is an actin binding protein involved with cell migration and maintaining cytoskeletal organization. Girdin has conserved domains at the N- and C-terminus that bind microtubules and actin, respectively. It enhances PI3-kinase dependent phosphorylation of proteins, most notably Akt. This same activity can contribute to tumor proliferation, invasion, and metastasis in breast, ovarian, prostate, and pancreatic tissues. Girdin is phosphorylated at three separate locations: Ser-1416, Ser-1674, and Tyr-1764. Ser-1416 is the primary Akt phosphorylation site, while Cyclin-dependent kinases interact with Girdin and phosphorylate Ser-1674. Multiple receptor tyrosine kinases can bind girdin and phosphorylate Tyr-1764.

Synonyms

APE, Galpha, vesicle, GIV, Girders actin filament, HkRP1, GRDN, CCDC88A

Swiss Prot

Q3V6T2

Modification Site

Tyr-1764

Host

Rabbit

Cross Reactivity

Human, Mouse, Rat

Target

Girdin (Tyr-1764)

Clonality

Polyclonal

Isotype

IgG

Conjugation

Unconjugated

Source

Phospho-Girdin (Tyr-1764) synthetic peptide (coupled to carrier) corresponding to amino acid residues around tyrosine 1764 in human Girdin.

Applications

Purification

Antigen Affinity purification

Dilution

WB (1:300-5000)

Buffer

PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol

Modification

Phosphorylation

Storage Conditions

Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.

Specificity

The antibody was cross-absorbed to unphosphorylated Girdin (Tyr-1764) peptide before affinity purification using phospho-Girdin (Tyr-1764) peptide. This antibody detects a 250 kDa* protein on SDS-PAGE immunoblots of human A431 cells stimulated with EGF and Pervanadate. These reactivities are not observed after alkaline phosphatase treatment to dephosphorylate Girdin. This sequence has high homology to rat and mouse Girdin, and the site is not conserved in other Girdin family members.