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Recombinant Human Transmembrane Protein 27

Source : Escherichia Coli. TMEM27 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 15-141) containing 137 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 15.64kDa (calculated) . Transmembrane Protein 27 (TMEM27) is a type 1 transmembrane protein which is imperative for trafficking amino acid transporters to the apical brush border of proximal tubules. TMEM27 binds to amino acid transporters and regulates their expression on the plasma membrane. In addition, TMEM27 has a role in regulating insulin exocytosis by regulating formation of the SNARE (soluble N-ethylmaleimide-sensitive-factor attachment protein receptor) complex in pancreatic beta cells. The extracellular domain of TMEM27 is cleaved off the surface of beta cells.

Product Specifications

Product Name Alternative

Collectrin||Transmembrane protein 27||TMEM27||NX17||NX-17.

Purification

Greater than 95.0% as determined by SDS-PAGE.

Components

TMEM27 filtered (0.4μm) and lyophilized from 0.5mg/mL in 0.05M Acetate buffer pH-4.0.

Storage Conditions

Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

Applications Notes

It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely at 37°C. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited. TMEM27 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

Amino Acids

MKHHHHHHASELCQPGAENA FKVRLSIRTA LGDKAYAWDT NEEYLFKAMV AFSMRKVPNR EATEISHVLL CNVTQRVSFW FVVTDPSKNH TLPAVEVQSA IRMNKNRINN AFFLNDQTLE FLKIPSTLAP PMDPSVP.

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