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Rombinant Human TDGF1 / Cripto Protein, Fc Tag, 50µg  

Rombinant Human TDGF1 / Cripto Protein, Fc Tag, 50µg

Recombinant Human Cripto /TDGF1 Protein (Leu 31 - Thr 172), expressed in human 293 cells (HEK293), Fc tag

Synonym
recombinant, human, TDGF1, CRGF, CRIPTO

More details

CRO-H5253-50

Availability: within 7 days

348,00 €

Background
Teratocarcinoma-derived growth factor 1 (TDGF1) is also known as Cripto-1 growth factor (CRGF), Epidermal growth factor-like cripto protein CR1, CRIPTO, is a cell membrane which contains one EGF-like domain. TDGF1 is preferentially expressed in gastric and colorectal carcinomas than in their normal counterparts. TDGF1 interacts with the activin type-1 receptor ACVR1B. TDGF1 could play a role in the determination of the epiblastic cells that subsequently give rise to the mesoderm.

Source
Recombinant Human TDGF1, Fc Tag (CRO-H5253) is expressed from human 293 cells (HEK293). It contains AA Leu 31 - Thr 172 (Accession # P13385-1).
Predicted N-terminus: Leu 31

Molecular Characterization
rh Cripto /TDGF1 Fc Chimera is fused with a human IgG1 Fc tag at the C-terminus, and has a calculated MW of 42.6 kDa. The predicted N-terminus is Leu 31. The reducing (R) protein migrates as 44-55 kDa in SDS-PAGE due to glycosylation.

Endotoxin
Less than 1.0 EU per μg of the rh Cripto /TDGF1 Fc Chimera by the LAL method.

Purity
>95% as determined by SDS-PAGE.

Formulation
Lyophilized from 0.22 μm filtered solution in Tris with Glycine, Arginine and NaCl, pH7.5. Normally trehalose is added as protectant before lyophilization.

Reconstitution
See Certificate of Analysis for reconstitution instructions and specific concentrations.

Storage
Avoid repeated freeze-thaw cycles.
No activity loss was observed after storage at:
In lyophilized state for 1 year (4°C); After reconstitution under sterile conditions for 3 months (-70°C).

References

(1) Bianco C., et al., 2002, Mol. Cell. Biol. 22:2586-2597.
(2) Foley S.F., et al., 2003, Eur. J. Biochem. 270:3610-3618.
(3) Sun C., et al., 2008, Biochem. Biophys. Res. Commun. 377:215-220.