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AB99522

Recombinant Human Methionine Sulfoxide Reductase B protein

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(1 Publication)

Recombinant Human Methionine Sulfoxide Reductase B protein is a Human Full Length protein, in the 1 to 116 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.

View Alternative Names

SEPX1, HSPC270, MSRB1, Methionine-R-sulfoxide reductase B1, MsrB1, Selenoprotein X, SelX

1 Images
SDS-PAGE - Recombinant Human Methionine Sulfoxide Reductase B protein (AB99522)
  • SDS-PAGE

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SDS-PAGE - Recombinant Human Methionine Sulfoxide Reductase B protein (AB99522)

15% SDS-PAGE analysis of 3μg ab99522.

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q9NZV6

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 10% Glycerol (glycerin, glycerine), 0.316% Tris HCl, 0.0584% EDTA, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.00174% PMSF

storage-buffer

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Reactivity data

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

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMSFCSFFGGEVFQNHFEPGVYVCAKCGYELFSSRSKYAHSSPWPAFTETIHADSVAKRPEHNRSEALKVSCGKCGNGLGHEFLNDGPKPGQSRFCIFSSSLKFVPKGKETSASQGH","proteinLength":"Full Length","predictedMolecularWeight":"14.8 kDa","actualMolecularWeight":null,"aminoAcidEnd":116,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q9NZV6","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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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
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Specifications

Form

Liquid

Additional notes

ab99522 was purified using conventional chromatography.

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General info

Function

Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Acts as a regulator of actin assembly by reducing methionine (R)-sulfoxide mediated by MICALs (MICAL1, MICAL2 or MICAL3) on actin, thereby promoting filament repolymerization. Plays a role in innate immunity by reducing oxidized actin, leading to actin repolymerization in macrophages.

Sequence similarities

Belongs to the MsrB Met sulfoxide reductase family.

Post-translational modifications

Truncated MSRB1/SEPX1 proteins produced by failed UGA/Sec decoding are ubiquitinated by some Cul2-RING E3 ubiquitin-protein ligase complexes (containing either PRAME, PRAMF6, PRAMF9 or FEM1C as substrate-recognition component).

Subcellular localisation

Nucleus

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Product protocols

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Target data

Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Acts as a regulator of actin assembly by reducing methionine (R)-sulfoxide mediated by MICALs (MICAL1, MICAL2 or MICAL3) on actin, thereby promoting filament repolymerization. Plays a role in innate immunity by reducing oxidized actin, leading to actin repolymerization in macrophages.
See full target information MSRB1
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

PLoS biology 16:e2005140 PubMed30086131

2018

Surf4 (Erv29p) binds amino-terminal tripeptide motifs of soluble cargo proteins with different affinities, enabling prioritization of their exit from the endoplasmic reticulum.

Applications

Unspecified application

Species

Unspecified reactive species

Ying Yin,Mekka R Garcia,Alexander J Novak,Allison M Saunders,Raira S Ank,Anna S Nam,Larry W Fisher
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