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Recombinant Human UBE2L3 Protein - RP00025LQ

Recombinant Human UBE2L3 Protein - RP00025LQ

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Recombinant Human UBE2L3 Protein

Sizes: 50ug, 100ug

Catalogue Number: RP00025LQ-50, RP00025LQ-100

Citations, Manuals and MSDS Available upon request.

Description: Recombinant Human UBE2L3 Protein is produced by E. coli expression system. The target protein is expressed with sequence (Met1-Asp154) of human UBE2L3 (Accession #NP_003338.1) fused with a 6×His tag at the C-terminus.

Alternate Names: UBE2L3, E2-F1, L-UBC, UBCH7, UbcM4, Ube2L3 / UBCH7

SWISS: P68036

GeneID: 7332

Species: Human

Purity: ≥ 95 % as determined by SDS-PAGE.

Storage: Store at -70℃. This product is stable at ≤ -70℃ for up to 1 year from the date of receipt. For optimal storage, aliquot into smaller quantities after centrifugation and store at recommended temperature. Avoid repeated freeze-thaw cycles.

Background: Ubiquitin-conjugating Enzyme E2L 3 (UBE2L3),also known as Ubiquitin-conjugating Enzyme H7 (UbcH7), is a member of the Ubiquitin-conjugating (E2) enzyme family (1). The human UbcH7 protein shares 100% amino acid (aa) sequence identity with the mouse and rat orthologs. UBE2L3 is catalytically active with HECT and RBR domain-containing families of Ubiquitin ligases (E3s). UBE2L3 localizes to both the nucleus and cytoplasm in human cells. UBE2L3 depletion results in an extended S phase and a reduced rate of proliferation, suggesting that it may play a role in the cell cycle. In humans, single nucleotide polymorphisms in UBE2L3 are associated with systemic lupus erythematosus and Crohn's disease, suggesting that UbcH7 is important for proper immune system function.

Source: E. coli

Tag: C-His

Formulation: Supplied in 50mM HEPES, 200mM NaCl, 10%glycerol, 1mM TCEP, pH 7.0Contact us for customized product form or formulation.

Antigen Sequence: MAASRRLMKELEEIRKCGMKNFRNIQVDEANLLTWQGLIVPDNPPYDKGAFRIEINFPAEYPFKPPKITFKTKIYHPNIDEKGQVCLPVISAENWKPATKTDQVIQSLIALVNDPQPEHPLRADLAEEYSKDRKKFCKNAEEFTKKYGEKRPVD

Endotoxin: Please contact us for more information.

Research Use Only