COX4NB (1-210, His-tag) Human Protein

Specifications

Product Data
Species	Human
Expression Host	E. coli
Expression cDNA Clone or AA Sequence	Protein Sequence (showhide) MGSSHHHHHH SSGLVPRGSH MPGVKLTTQA YCKMVLHGAK YPHCAVNGLL VAEKQKPRKE HLPLGGPGAH HTLFVDCIPL FHGTLALAPM LEVALTLIDS WCKDHSYVIA GYYQANERVK DASPNQVAEK VASRIAEGFS DTALIMVDNT KFTMDCVAPT IHVYEHHENR WRCRDPHHDY CEDWPEAQRI SASLLDSRSY ETLVDFDNHL DDIRNDWTNP EINKAVLHLC
Tag	His-tag
Predicted MW	25.9 kDa
Concentration	lot specific
Purity	>95%
Buffer	Presentation State: Purified State: Liquid purified protein Buffer System: 20 mM Tris-HCl buffer (pH 8.0) containing 1 mM DTT, 10% glycerol, 0.1M NaCl
Preparation	Liquid purified protein
Protein Description	Recombinant human COX4NB protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
Storage	Store undiluted at 2-8°C for up to two weeks or (in aliquots) at -20°C or -70°C for longer. Avoid repeated freezing and thawing.
Stability	Shelf life: one year from despatch.
Reference Data
RefSeq	NP_001135760
Locus ID	10328
UniProt ID	O43402
Cytogenetics	16q24.1
Synonyms	C16orf2; C16orf4; COX4NB; FAM158B; NOC4
Summary	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 multi-pass membrane proteins like the G protein-coupled receptors (PubMed:30415835). By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (Probable).[UniProtKB/Swiss-Prot Function]

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