Recombinant Human Ret His-tag Protein, CF
Recombinant Human Ret His-tag Protein, CF Summary
Leu29-Arg635, with a C-terminal 10-His tag
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
2 μg/lane of Recombinant Human Ret His-tag (Catalog # 10302-CR) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 101-113 kDa.
Receptor tyrosine-protein kinase, also known as Ret, is encoded by the C-RET proto-oncogene. Mutations of the C-RET gene have been associated with various human diseases affecting tissues derived from the neural crest, including Hirschsprung's disease, multiple endocrine neoplasia MEN2A and MEN2B, and familial medullary thyroid carcinoma (1, 2, 3). Human C-RET cDNA encodes a 1115 amino acid (aa) with a 28 aa signal peptide, a 679 aa cysteine-rich extracellular domain that contains an membrane anchored Ret-Cadherin 120 Da fragment, and a 456 aa rcytoplasmic domain with a soluble Ret kinase fragment (4). Human and mouse Ret share 83% amino acid sequence homology (77% homology in the extracellular domain and 93% homology in the cytoplasmic domain). Although Ret does not bind GDNF ligands directly, the extracellular domain of Ret binds the GDNF-GFR-alpha complex with high affinity and is a potent GDNF antagonist in the presence of soluble GFR-alpha (5).
- Ma, Q. (2009) Neuron 64:773.
- Carlomagno, F. et al. (1998) Endocrinology 139:3613.
- Cabrera, J.R. et al. (2011) J. Biol. Chem. 286:14628.
- Iwamoto, T. et al. (1993) Oncogene 8:1087.
- Yang, L. et al. (2017) Nat. Med. 23:1158.
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