Human Recombinant SUMO2 protein, His Tag (V2LY-0526-LY7018)

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Basic Information

Expressed Host
E. coli
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant SUMO2 protein, His Tag consist of Amino Acid: 1-93 and predicts a molecular mass of 17.5 kDa.
Molecule Mass
17.5 kDa
Sequence
Amino Acid: 1-93
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
Batch dependent.
Endotoxin
Please contact us for more information.
Format
Liquid
Buffer
PBS
Preservative
None
Storage
Store product at -70°C. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.
More Infomation

Target

Full Name
SUMO2
Function
Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as 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 an E3 ligase such as PIAS1-4, RANBP2, CBX4 or ZNF451 (PubMed:26524494).
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. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins (PubMed:18408734, PubMed:18538659, PubMed:21965678, PubMed:9556629).
Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744).
Biological Process
Biological Process positive regulation of proteasomal ubiquitin-dependent protein catabolic processManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process protein sumoylationManual Assertion Based On ExperimentIDA:UniProtKB
Cellular Location
Nucleus
Nucleus, PML body
PTM
Polymeric chains can be formed through Lys-11 cross-linking. Polymeric SUMO2 chains undergo 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4.
Cleavage of precursor form by SENP1 or SENP2 is necessary for function.
Monoubiquitinated N-terminally by UBE2W, which primes it for RNF4-dependent polyubiquitination by the UBE2V1-UBE2N heterodimer.
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For research use only. Not intended for any clinical use.

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