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Transmembrane protein 27 Protein Datasheet
TMEM27 Protein Price Inquiry ( Available Sizes )
TMEM27 Protein Product Information
A DNA sequence encoding the human TMEM27(Q9HBJ8) (Met1-Pro141) was expressed, fused with the Fc region of human IgG1 at the C-terminus.
|Expression Host:||Human Cells|
TMEM27 Protein QC Testing
|Purity:||> 95 % as determined by SDS-PAGE||SDS-PAGE:
|Endotoxin:||< 1.0 EU per μg of the protein as determined by the LAL method|
|Stability:||Samples are stable for up to twelve months from date of receipt at -70℃|
|Predicted N terminal:||Glu 15|
The recombinant human TMEM27 /Fc is a disulfide-linked homodimer. The reduced monomer comprises 368 amino acids and has a predicted molecular mass of 41.4 kDa. The apparent molecular mass of the protein is approximately 53-57 kDa in SDS-PAGE under reducing conditions.
|Formulation:||Lyophilized from sterile PBS, pH7.4.
TMEM27 Protein Usage Guide
|Storage:||Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.|
|Reconstitution:||A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.|
TMEM27 Protein Related Products & Topics
TMEM27 Protein Description
TMEM27 is a membrane protein. It forms dimers and its extracellular domain is glycosylated, cleaved and shed from the plasma membrane of beta cells. Thus it has been proposed as a beta cell mass biomarker. Overexpression of TMEM27 leads to increased thymidine incorporation, whereas silencing of Tmem27 using RNAi results in a reduction of cell replication. Furthermore, transgenic mice with increased expression of Tmem27 in pancreatic beta cells exhibit increased beta cell mass. TMEM27 is important for trafficking amino acid transporters to the apical brush border of proximal tubules.
- Pasquali L. et al., 2009, J Genet. 88 (1): 105-8.
- Tosetto E. et al., 2009, Pediatr Nephrol. 24 (10): 1967-73.
- Singer D. et al., 2011, Channels (Austin). 5 (5): 410-23.