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AB268952

Recombinant human SAE1 + UBA2 protein (Active)

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Recombinant human SAE1 + UBA2 protein (Active) is a Human Full Length protein, expressed in Baculovirus infected Sf9 cells, with >75%, suitable for SDS-PAGE, FuncS.

View Alternative Names

AOS1, SUA1, UBLE1A, SAE1, SUMO-activating enzyme subunit 1, Ubiquitin-like 1-activating enzyme E1A

2 Images
Functional Studies - Recombinant human SAE1 + UBA2 protein (Active) (AB268952)
  • FuncS

Supplier Data

Functional Studies - Recombinant human SAE1 + UBA2 protein (Active) (AB268952)

The specific activity of ab268952 was 45 nmol/min/mg in a sumoylation assay using human SUMO2 (1-93) and RanGAP protein as substrate.

SDS-PAGE - Recombinant human SAE1 + UBA2 protein (Active) (AB268952)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human SAE1 + UBA2 protein (Active) (AB268952)

SDS-PAGE analysis of ab268952.

Key facts

Purity

>75% SDS-PAGE

Expression system

Baculovirus infected Sf9 cells

Tags

Tag free

Applications

SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

The specific activity of ab268952 was 45 nmol/min/mg in a sumoylation assay using human SUMO2 (1-93) and RanGAP protein as substrate.

Accession

Q9UBE0

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 25% Glycerol (glycerin, glycerine), 0.79% Tris HCl, 0.31% Glutathione, 0.29% Sodium chloride, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.003% EDTA, 0.002% PMSF

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>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

Full-length recombinant human SAE1 and UBA2 were co-expressed.

Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q9UBE0","tags":[{"tag":"His","terminus":"N-Terminus"}]},{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q9UBT2","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True

Supplementary information

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

SAE1 also known as SUMO-activating enzyme subunit 1 and UBA2 known as SUMO-activating enzyme subunit 2 work together as a heterodimer to activate small ubiquitin-related modifier (SUMO) proteins. SAE1 has a molecular weight of about 40 kDa. These proteins operate mainly in the nucleus where they facilitate the conjugation of SUMO to target proteins. SAE1 and UBA2 initiate the SUMOylation process by forming a thioester bond between the SUMO molecule and a catalytic cysteine residue on UBA2 through ATP hydrolysis.
Biological function summary

SAE1 and UBA2 play important roles in cellular processes like DNA repair transcriptional regulation and chromosome segregation. This heterodimer forms the initial step in the SUMOylation cascade which is important for modulating protein interactions locations and stability. These processes regulate gene expression and maintain genomic integrity. By modifying several key proteins SAE1 and UBA2 affect cellular responses to stress and DNA damage.

Pathways

Many cellular mechanisms rely on the SUMOylation pathway that SAE1 and UBA2 facilitate. The SUMOylation pathway interacts closely with the ubiquitin-proteasome system as both systems regulate protein homeostasis. Key proteins such as PIAS and SENP families are also involved in the SUMO pathway either as ligases or proteases and they modulate the effects initiated by SAE1 and UBA2. Additionally the pathway influences the response to cellular stress by modulating transcription factors and DNA repair enzymes.

The function of SAE1 and UBA2 holds significance in cancer development and neurodegenerative diseases. In various cancer types alterations in SUMOylation controlled by SAE1 and UBA2 can lead to unchecked cellular proliferation and survival. UBA2 in particular often becomes a focus in cancer biology for its role in cellular stress pathways. In neurodegenerative diseases these proteins influence the aggregation and degradation of proteins such as tau and alpha-synuclein linking SUMOylation deficits to disease progression.

Specifications

Form

Liquid

Additional notes

Affinity purified.

General info

Function

The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2.

Sequence similarities

Belongs to the ubiquitin-activating E1 family.

Subcellular localisation

Nucleus

Product protocols

Target data

The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2.
See full target information SAE1

Additional targets

UBA2

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