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AB111626

Recombinant Human COX4NB protein

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Recombinant Human COX4NB protein is a Human Full Length protein, in the 1 to 210 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

C16orf2, C16orf4, COX4AL, COX4NB, FAM158B, NOC4, EMC8, ER membrane protein complex subunit 8, Neighbor of COX4, Protein FAM158B

1 Images
SDS-PAGE - Recombinant Human COX4NB protein (AB111626)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human COX4NB protein (AB111626)

15% SDS-PAGE showing ab111626 at approximately 25.9kDa (3μg).

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

O43402

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMPGVKLTTQAYCKMVLHGAKYPHCAVNGLLVAEKQKPRKEHLPLGGPGAHHTLFVDCIPLFHGTLALAPMLEVALTLIDSWCKDHSYVIAGYYQANERVKDASPNQVAEKVASRIAEGFSDTALIMVDNTKFTMDCVAPTIHVYEHHENRWRCRDPHHDYCEDWPEAQRISASLLDSRSYETLVDFDNHLDDIRNDWTNPEINKAVLHLC","proteinLength":"Full Length","predictedMolecularWeight":"25.9 kDa","actualMolecularWeight":null,"aminoAcidEnd":210,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"O43402","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The protein COX4NB also known as Cytochrome C Oxidase Subunit 4 Neighbor has a mass of around 20 kDa. It plays a mechanical role closely related to the function of its neighboring COX4 isoform proteins which are part of the cytochrome C oxidase complex. COX4NB is expressed in various human tissues including the heart and skeletal muscle suggesting its involvement in energy metabolism.
Biological function summary

COX4NB participates in mitochondrial function. The protein integrates into the cytochrome C oxidase complex which is an important component of the electron transport chain in mitochondria. Through this involvement COX4NB contributes to cellular respiration and ATP production which maintain energy homeostasis in cells.

Pathways

COX4NB is involved in key metabolic pathways. It is part of the oxidative phosphorylation pathway which is essential for the generation of ATP in aerobic organisms. In this process COX4NB works alongside proteins like COX4I1 and other subunits of the cytochrome C oxidase complex to facilitate efficient electron transfer and energy production.

COX4NB has associations with conditions tied to mitochondrial dysfunction. Its altered expression or mutation could relate to mitochondrial cardiomyopathy or hypertrophic cardiomyopathy conditions that affect heart muscle efficiency. Researchers are studying the link between COX4NB and proteins like COX4I1 as changes in these proteins could illuminate pathological mechanisms underpinning such mitochondrial diseases.

Specifications

Form

Liquid

Additional notes

ab111626 was purified using conventional chromatography techniques.

General info

Function

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 : 29242231, PubMed : 29809151, PubMed : 30415835, PubMed : 32439656, PubMed : 32459176). Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues (PubMed : 29242231, PubMed : 29809151, PubMed : 30415835). Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices (PubMed : 29809151, PubMed : 30415835). It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes (PubMed : 29242231, PubMed : 29809151). 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).

Sequence similarities

Belongs to the EMC8/EMC9 family.

Product protocols

Target data

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 : 29242231, PubMed : 29809151, PubMed : 30415835, PubMed : 32439656, PubMed : 32459176). Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues (PubMed : 29242231, PubMed : 29809151, PubMed : 30415835). Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices (PubMed : 29809151, PubMed : 30415835). It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes (PubMed : 29242231, PubMed : 29809151). 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).
See full target information EMC8

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