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UBE1L (E996) pAb

UBE1L (E996) pAb

Cat no: BS1486

Supplier: Bioworld Technology, Inc.
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The ubiquitin activating enzyme E1 (UBE1) catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation. UBE1 activates ubiquitin by first adenylating (with ATP) its carboxy-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and a free AMP. UBE1 is an example of an X-Y homologous gene, which is X-linked with a distinct Y-linked gene in many mammals. UBE1L (Ubiquitin-activating enzyme E1 homolog), also known as UBA7 (Ubiquitin-like modifier-activating enzyme 7) or UBE2, is a 1011 amino acid homolog of UBE1. Like UBE1, UBE1L functions in the activation of ubiquitin through ATP-dependent adenylation. UBE1L is expressed in tumor cells and is a retinoid target that, through conjugation with ISG15 (Interferon-induced 15 kDa protein), triggers degradation and apoptosis in acute promyelocytic leukemia.
Catalogue number: BS1486
Reactivities: Human, Mouse, Rat
Hosts: Rabbit
Applications: Immunohistochemistry, Western Blot
Size: 100ug/100ul
Swiss prot: P41226
Dilutions: WB: 1:500~1:1000 IHC: 1:50~1:200
Form: liquid
Storage buffer: 1 mg/ml in Phosphate buffered saline (PBS) with 0.05% sodium azide, approx. pH 7.2.
Concentration: 1ug/ul
Antigen: Synthetic peptide, corresponding to amino acids C-terminus of Human UBE1L.
Species: UBE1L (E996) pAb detects endogenous levels of UBE1L protein.
Molecular weight: ~ 112 kDa
Purity: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Storage temp: Store at 4 degrees C short term. Aliquot and store at -20 degrees C long term. Avoid freeze-thaw cycles.
Alternative names: Ubiquitin-like modifier-activating enzyme 7; Ubiquitin-activating enzyme 7; D8; Ubiquitin-activating enzyme E1 homolog; UBA7; UBE1L; UBE2
Additional info: For research use only, not for use in diagnostic procedure.

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