Catalogue number
PRO-1581
Synonyms
Collectrin, Transmembrane protein 27, TMEM27, NX17, NX-17.
Introduction
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. The extracellular domain of TMEM27 is cleaved off the surface of beta cells.
Description
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).
Source
Escherichia Coli.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Formulation
TMEM27 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.05M Acetate buffer pH-4.0.
Solubility
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 10?g/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.
Stability
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.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Amino acid sequence
MKHHHHHHASELCQPGAENA FKVRLSIRTA LGDKAYAWDT NEEYLFKAMV AFSMRKVPNR EATEISHVLL CNVTQRVSFW FVVTDPSKNH TLPAVEVQSA IRMNKNRINN AFFLNDQTLE FLKIPSTLAP PMDPSVP.
Safety Data Sheet
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
