Recombinant Human E3 ubiquitin-protein ligase MYCBP2 (MYCBP2), partial

SKU: O75592

Size: 100ug. Other sizes are also available.

Activity: Not tested

Research Areas: Cell Biology

Uniprot ID: O75592

Gene Names: MYCBP2

Alternative Name(s): Myc-binding protein 2;Protein associated with Myc

Abbreviation: Recombinant Human MYCBP2 protein, partial

Organism: Homo sapiens (Human)

Source: E.coli

Expression Region: 4417-4676aa

Protein Length: Partial

Tag Info: C-terminal 6xHis-tagged

Target Protein Sequence: ATSLKQDADDMCMICFTEALSAAPAIQLDCSHIFHLQCCRRVLENRWLGPRITFGFISCPICKNKINHIVLKDLLDPIKELYEDVRRKALMRLEYEGLHKSEAITTPGVRFYNDPAGYAMNRYAYYVCYKCRKAYFGGEARCDAEAGRGDDYDPRELICGACSDVSRAQMCPKHGTDFLEYKCRYCCSVAVFFCFGTTHFCNACHDDFQRMTSIPKEELPHCPAGPKGKQLEGTECPLHVVHPPTGEEFALGCGVCRNAH

MW: 36.3 kDa

Purity: Greater than 90% as determined by SDS-PAGE.

Endotoxin: Not test

Biological_Activity:

Form: Liquid or Lyophilized powder

Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.

Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.

Relevance: Atypical E3 ubiquitin-protein ligase which specifically mediates ubiquitination of threonine and serine residues on target proteins, instead of ubiquitinating lysine residues. Shows esterification activity towards both threonine and serine, with a preference for threonine, and acts via two essential catalytic cysteine residues that relay ubiquitin to its substrate via thioester intermediates. Interacts with the E2 enzymes UBE2D1, UBE2D3, UBE2E1 and UBE2L3. Plays a key role in neural development, probably by mediating ubiquitination of threonine residues on target proteins (Probable). Involved in different processes such as regulation of neurite outgrowth, synaptic growth, synaptogenesis and axon degeneration. Required for the formation of major central nervous system axon tracts. Required for proper axon growth by regulating axon navigation and axon branching: acts by regulating the subcellular location and stability of MAP3K12/DLK. Required for proper localization of retinogeniculate projections but not for eye-specific segregation. Regulates axon guidance in the olfactory system. Involved in Wallerian axon degeneration, an evolutionarily conserved process that drives the loss of damaged axons: acts by promoting destabilization of NMNAT2, probably via ubiquitination of NMNAT2. Catalyzes ubiquitination of threonine and/or serine residues on NMNAT2, consequences of threonine and/or serine ubiquitination are however unknown. Regulates the internalization of TRPV1 in peripheral sensory neurons. Mediates ubiquitination and subsequent proteasomal degradation of TSC2/tuberin. Independently of the E3 ubiquitin-protein ligase activity, also acts as a guanosine exchange factor (GEF) for RAN in neurons of dorsal root ganglia. May function as a facilitator or regulator of transcriptional activation by MYC. Acts in concert with HUWE1 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1.

Reference:

Function: