WWC1 Antibody

Product Specifications

Background

The WW and C2 domain containing 1 (WWC1) protein, also known as KIBRA, possesses two WW domains and an internal C2-like domain (1) . WWC1 was originally identified as a memory performance-associated protein in humans (2) and has recently been shown to be a novel regulator of the Hippo pathway (3) . WWC1 is phosphorylated by the mitotic kinases Aurora-A and –B (4), and in turn activates the Aurora kinases and is required for precise chromosome alignment during mitosis (5) .

NCBI Gene ID

23286

Swiss Prot

Q8IX03

Accession Number

NP_001155133

Host

Rabbit

Reactivity

Human, Mouse, Rat

Clonality

Polyclonal

Conjugation

Unconjugated

Type

Primary Antibodies

Field of Research

Homeostasis, Neuroscience

Purification

WWC1 antibody is affinity chromatography purified via peptide column.

Positive Control

Cat. No. 1303 - Human Brain Tissue Lysate

Concentration

1 mg/mL

Buffer

WWC1 antibody is supplied in PBS containing 0.02% sodium azide.

Modification

None

Shipping Conditions

Blue Ice

Storage Conditions

WWC1 antibody can be stored at 4˚ C for three months and -20˚ C, stable for up to one year.

Fragment

IgG

Specificity

WWC1 antibody is human, mouse and rat reactive. At least three isoforms of WWC1 are known to exist; this antibody will detect all three isoforms.

Symbol

WWC1

NCBI Official Name

WW and C2 domain containing 1

NCBI Organism

Homo sapiens

Background Reference 01

Kremerskothen J, Plaas C, Buther K, et al. Characterization of KIBRA, a novel WW domain-containing protein. Biochem. Biophys. Res. Commun. 2003; 300:862-7.

Background Reference 02

Papassotiropoulos A, Stephan DA, Huentelman MJ, et al. Common Kibra alleles are associated with human memory performance. Science 2006; 314:475-8.

Background Reference 03

Genevet A, Wehr MC, Brain R, et al. Kibra is a regulator of the Salvador/Warts/Hippo signaling network. Dev. Cell 2010; 18:309-16.

Background Reference 04

Xiao L, Chen Y, Ji M, et al. KIBRA protein phosphorylation is regulated by mitotic kinase aurora and protein phosphatase 1. J. Biol. Chem. 2011; 286:36304-15.