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Recombinant Human Sumo 1 protein is a Human Full Length protein, in the 2 to 97 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, WB.

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Images

SDS-PAGE - Recombinant Human Sumo 1 protein (AB140417), expandable thumbnail
  • Western blot - Recombinant Human Sumo 1 protein (AB140417), expandable thumbnail
  • Western blot - Recombinant Human Sumo 1 protein (AB140417), expandable thumbnail
  • Western blot - Recombinant Human Sumo 1 protein (AB140417), expandable thumbnail
  • Western blot - Recombinant Human Sumo 1 protein (AB140417), expandable thumbnail

Key facts

Purity
>90% Densitometry
Expression system
Escherichia coli
Tags
His tag N-Terminus
Applications
SDS-PAGE, WB
Biologically active
No

Amino acid sequence

S D Q E A K P S T E D L G D K K E G E Y I K L K V I G Q D S S E I H F K V K M T T H L K K L K E S Y C Q R Q G V P M N S L R F L F E G Q R I A D N H T P K E L G M E E E D V I E V Y Q E Q T G G

Reactivity data

Application
SDS-PAGE
Reactivity
Reacts
Dilution info
-
Notes

-

Application
WB
Reactivity
Reacts
Dilution info
-
Notes

-

Target data

Function

Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1 (PubMed:19223394). Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3 (PubMed:24651376).

Alternative names

SMT3C, SMT3H3, UBL1, OK/SW-cl.43, SUMO1, Small ubiquitin-related modifier 1, SUMO-1, GAP-modifying protein 1, SMT3 homolog 3, Sentrin, Ubiquitin-homology domain protein PIC1, Ubiquitin-like protein SMT3C, Ubiquitin-like protein UBL1, GMP1, Smt3C

Recommended products

Recombinant Human Sumo 1 protein is a Human Full Length protein, in the 2 to 97 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, WB.

Key facts

Purity
>90% Densitometry
Expression system
Escherichia coli
Applications
SDS-PAGE, WB
Accession
P63165-1
Animal free
No
Species
Human
Concentration
Loading...
Storage buffer

pH: 7
Preservative: 1.02% Imidazole
Constituents: 25% Glycerol (glycerin, glycerine), 1.75% Sodium chloride, 0.82% Sodium phosphate, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.002% PMSF

Sequence info

Amino acid sequence

S D Q E A K P S T E D L G D K K E G E Y I K L K V I G Q D S S E I H F K V K M T T H L K K L K E S Y C Q R Q G V P M N S L R F L F E G Q R I A D N H T P K E L G M E E E D V I E V Y Q E Q T G G
Accession
P63165
Protein length
Full Length
Predicted molecular weight
19 kDa
Amino acids
2 to 97
Nature
Recombinant
Tags
His tag N-Terminus

Specifications

Form
Liquid

General info

Function

Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1 (PubMed:19223394). Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3 (PubMed:24651376).

Sequence similarities

Belongs to the ubiquitin family. SUMO subfamily.

Post-translational modifications

Cleavage of precursor form by SENP1 or SENP2 is necessary for function.

Subcellular localisation
Nucleus membrane, Nucleus speckle, Nucleus, PML body

Storage

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

Supplementary info

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

SUMO 1 also known as small ubiquitin-like modifier 1 is part of the protein family involved in post-translational modification. The protein mechanically adds a SUMO group to target proteins through sumoylation a process similar to ubiquitination. SUMO 1 typically has a molecular mass of around 11 kDa. It expresses in various tissues and cells including the nucleus and cytoplasm of eukaryotic cells. In addition it is important in processes like nuclear transport transcriptional regulation and protein stabilization.

Biological function summary

SUMO 1 contributes significantly to maintaining cellular homeostasis. It is an integral part of a SUMOylation complex that modifies other proteins to alter their function localization or interactions. Through its modification actions SUMO 1 affects processes such as DNA repair and the cell cycle. By interacting with components of the nuclear pore complex and transcription factors SUMO 1 modulates essential biological activities at multiple levels within the cell.

Pathways

This protein plays a significant role in the PI3K/Akt pathway and Wnt signaling. SUMO 1 associates with proteins like RanGAP1 and various transcription factors highlighting the complexity of its regulatory actions. These associations are important for the regulation of cell survival proliferation and differentiation. SUMOylation by SUMO 1 has been linked to an interference with phosphorylation showing its potential influence on cell signaling pathways.

Associated diseases and disorders

The dysregulation of SUMO 1 is seen in cancer and neurodegenerative diseases. For instance altered SUMOylation patterns contribute to the progression of certain cancers. Furthermore SUMO 1 interacts with proteins like p53 and these interactions can affect tumor suppression and cell cycle regulation. In neurodegenerative disorders disturbed SUMOylation is associated with protein aggregation and neuronal damage implicating SUMO 1 in diseases like Alzheimer's.

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