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Recombinant human TMEM111 protein

Cat:P05812

Summary:

【Derived From】: E.coli
【Endotoxin】: Not measured
【Amino Acid】: 150-262aa
【Purity】: ≥85% by SDS-PAGE.
【Name】: TMEM111
【Full Name】: transmembrane protein 111
【Uniprot】: Q9P0I2
【Gene ID】: 55831
【Species Reactivity】: Human Mouse Rat (Bovine Zebrafish Orangutan)
【Mol Mass】: 13kDa
【Application】: Immunology research
【Purification】: NI-NTA affinity purification
【Bioactive】: N0
【Tag】: With a 6×His tag at the N/C-terminus.
【Concentration】: 1mg/ml by SDS-PAGE.

Store:

【Reconstitution】: Reconstituted protein solution can be diluted with distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. (It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water.)
【Storage】: Reconstituted protein solution can be stored at 4-7℃ for 1-2 weeks, stored at < -20℃ for 1 year.
【Formulation】: Powder: Lyophilized from a 0.2 μm filtered solution of 2-8M Urea, 20mM Tris-HCl, 150mM NaCl, 1mM DTT, PH7.2-8.0.

Background:

Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins (PubMed:30415835, PubMed:29809151, PubMed:29242231, PubMed:32459176, PubMed:32439656).Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues (PubMed:30415835, PubMed:29809151, PubMed:29242231).Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices (PubMed:30415835, PubMed:29809151).It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes (PubMed:29809151, PubMed:29242231).By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of

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