Anti-UCHL5 (C-term) antibody produced in rabbit

NA.41

Covalent attachment of the C-terminus of ubiquitin to cellular proteins plays a role in a variety of cellular processes. Ubiquitin C-terminal hydrolysis is catalyzed by deubiquitinating (DUB) enzymes and is necessary for several functions, including liberation of monomeric ubiquitin from the precursors encoded by ubiquitin genes and recycling of ubiquitin monomers. There are 2 distinct families of DUBs, ubiquitin-specific proteases (UBPs) and ubiquitin C-terminal hydrolases (UCHs). Mayer and Wilkinson (1989) identified 4 distinct UCH activities from bovine thymus. All 4 were thiol proteases and had high-affinity binding sites for ubiquitin. Wilkinson et al. (1989) purified the predominant isozyme, UCHL3, and raised antibodies against it. By screening a human B-cell expression library with the antibodies, the authors isolated cDNAs encoding human UCHL3. Sequence comparisons revealed that the sequence of the predicted 230-amino acid human UCHL3 protein is 54% identical to that of UCHL1.

UCHL5 (UBL5_HUMAN, 304-339)
This antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected from the C-terminal region of human UCHL5.

Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide.

rabbit

100

unconjugated

IgG fraction of antiserum

primary antibodies

polyclonal

buffered aqueous solution

human

indirect ELISA: 1:1000

NP_057068

Q9Y5K5

dry ice

−20℃

human ... UCHL5(59286)

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12 - Non Combustible Liquids

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