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AB96772

Recombinant Human SAE1 protein (His tag N-Terminus + T7 tag N-Terminus)

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(1 Publication)

Recombinant Human SAE1 protein (His tag N-Terminus + T7 tag N-Terminus) is a Human protein, in the 1 to 346 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

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

1 Images
SDS-PAGE - Recombinant Human SAE1 protein (His tag N-Terminus + T7 tag N-Terminus) (AB96772)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human SAE1 protein (His tag N-Terminus + T7 tag N-Terminus) (AB96772)

15% SDS-PAGE showing ab96772 at approximately 42.2kDa (3μg).

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus T7 tag N-Terminus

Applications

SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

Q9UBE0

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

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Complementary Products

Primary Antibodies

AB185552

Anti-SAE1 antibody [EPR15398]

RabMAb|Recombinant

Immunocytochemistry/ Immunofluorescence - Anti-SAE1 antibody [EPR15398] (AB185552)

  • 5
  • 1
Proteins & Peptides

AB99263

Recombinant Human Tryptophanyl tRNA synthetase/WRS protein (His tag N-Terminus)

SDS-PAGE - Recombinant Human Tryptophanyl tRNA synthetase/WRS protein (His tag N-Terminus) (AB99263)

  • 0
  • 0
Proteins & Peptides

AB98233

Recombinant Human THTPA protein (His tag N-Terminus)

SDS-PAGE - Recombinant Human THTPA protein (His tag N-Terminus) (AB98233)

  • 0
  • 0
Proteins & Peptides

AB211951

Recombinant Human SUGT1 protein

  • 0
  • 0
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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>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MHHHHHHMASMTGGQQMGRDLYDDDDKDRWGSMVEKEEAGGGISEEEAAQYDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASLERAQNLNPMVDVKVDTEDIEKKPESFFTQFDAVCLTCCSRDVIVKVDQICHKNSIKFFTGDVFGYHGYTFANLGEHEFVEEKTKVAKVSQGVEDGPDTKRAKLDSSETTMVKKKVVFCPVKEALEVDWSSEKAKAALKRTTSDYFLLQVLLKFRTDKGRDPSSDTYEEDSELLLQIRNDVLDSLGISPDLLPEDFVRYCFSEMAPVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMKGNGIVECLGPK","proteinLength":null,"predictedMolecularWeight":"42.2 kDa","actualMolecularWeight":null,"aminoAcidEnd":346,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q9UBE0","tags":[{"tag":"His","terminus":"N-Terminus"},{"tag":"T7","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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Supplementary information

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

The protein SAE1 also known as SUMO-activating enzyme subunit 1 functions mechanically as a part of the SUMOylation process. It has a mass of approximately 39 kDa and is expressed in multiple cell types but is mainly found in the nucleus. SAE1 forms a heterodimeric structure with the protein SAE2 and together they are responsible for the initial step of SUMO activation which is important for SUMOylation a post-translational modification process.
Biological function summary

SAE1 is integral to numerous cellular processes that require precise regulation such as transcription DNA repair and signal transduction. It functions as part of the SUMO E1 enzyme complex which is essential for conjugating SUMO proteins to target substrates. This modification influences protein stability localization and interaction adding a layer of control in these cellular activities. The modulation of protein function by SAE1 impacts cell cycle control and stress responses indicating its breadth of influence across cellular mechanisms.

Pathways

The actions of SAE1 significantly impact the PI3K-Akt and DNA damage repair pathways. Its involvement in these pathways highlights its role in regulating cell survival and maintaining genomic integrity. SAE1's interaction within the SUMOylation machinery connects it to other proteins such as Ubc9 the E2 conjugating enzyme which highlights its importance in facilitating modifications necessary for a wide array of cellular functions and signaling cascades.

Defects or dysregulation of SAE1 have been linked to cancer and neurodegenerative conditions. Altered SUMOylation levels controlled by SAE1 can influence tumorigenesis through abnormal cell proliferation or impaired DNA damage responses connecting it with proteins like p53 and PARP1 which are critical in those pathways. Additionally SAE1's involvement in neurological disorders is associated with disrupted protein homeostasis linking it to pathologies where proper cellular regulatory mechanisms are compromised.
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Specifications

Form

Liquid

Additional notes

ab96772 is purified using conventional chromatography techniques.

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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

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Product protocols

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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
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Publications (1)

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

Plant physiology 179:88-106 PubMed30333149

2018

The SUMO E3 Ligase MdSIZ1 Targets MdbHLH104 to Regulate Plasma Membrane H-ATPase Activity and Iron Homeostasis.

Applications

Unspecified application

Species

Unspecified reactive species

Li-Jie Zhou,Chun-Ling Zhang,Rui-Fen Zhang,Gui-Luan Wang,Yuan-Yuan Li,Yu-Jin Hao
View all publications
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Product promise

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