GeneTex
United States (US)

Wnt1 recombinant protein

WNT-1-recombinant-protein_WB_GTX65281-1_18121411_161.jpg

Cat No. GTX65281

Application WB, ELISA, Functional Assay, Apuri, Blocking
Reactivity Human
Species Human
APPLICATION

Application Note

The ED50 was determined by its ability to enhance BMP-2 induced alkaline phosphatase production by murine ATDC5 cells. The expected ED50 for this effect is 1.5 - 2.5 ng/ml in the presence of 200 ng/ml of human BMP-2.

Calculated MW

38.4 kDa. ( Note )
PROPERTIES

Form

Lyophilized powder

Storage

Reconstitute in water to a concentration of 0.1-1.0 mg/ml. The solution can then be diluted into other aqueous buffers. Store at -20ºC.

Antigen Species

Human

Expression System

E. coli

Purification


Purity was assessed by SDS-PAGE (≥98%) and by HPLC (≥98%).

Note

For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
TARGET

Synonyms

Wnt Family Member 1,Bmnd16,Int1,Oi15,Wnt1

Background

Wnt-1 is a secreted protein that signals through the Frizzled family of cell surface receptors and is required for normal embryonic development. Wnt-1 activation induces a complex signaling cascade that ultimately leads to the increased expression of over fifty genes. An important component of Wnt-1 signaling is the stabilization, and resulting accumulation, of the intraCellular signaling protein, beta-catenine. Wnt signaling induces and maintains the transformed phenotype and, in certain embryonic cell lines, supports self renewal in the absence of significant differentiation. Elevated levels of Wnt proteins are associated with tumorigenesis and are present in numerous human breast cancers. Mature human Wnt-1 is a glycosylated protein containing 343 amino acid residues. Recombinant human Wnt-1 is a 38.4 kDa, non-glycosylated protein containing 343 amino acid residues.

Research Area

DATA IMAGES
WNT-1-recombinant-protein_WB_GTX65281-1_18121411_161.jpg

GTX65281 WB Image

Purity of recombinant Wnt-1 (2 µg) was analyzed by reduced SDS-PAGE electrophoresis