Monoclonal Anti-USP14 antibody produced in mouse

Ubiquitin specific peptidase 14 (USP14) is a 494 amino acid protein containing a 45kDa catalytic domain at its amino-terminus. Its ubiquitin-like (Ubl) domain associates with 19S regulatory particle (RP) 26S proteasome. This binding activates the deubiquitinating activity of the protein. USP14 is part of the ubiquitin-specific processing (UBP) family of proteases.

USP14 (NP_005142, 395 a.a. ~ 494 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
PQKEVKYEPFSFADDIGSNNCGYYDLQAVLTHQGRSSSSGHYVSWVKRKQDEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYGPRRVEIMEEESEQ

Ubiquitin specific peptidase 14 (USP14) releases ubiquitin from the proteasome-targeted ubiquitinated proteins resulting in regeneration of ubiquitin at the proteasome. It is involved in the degradation of chemokine receptor CXCR4. Under endoplasmic reticulum (ER) stress, USp14 binds to ER stress receptor, which is involved in unfolded protein response (UPR), a mechanism to control the accumulation of unfolded proteins within the ER lumen. Its overexpression leads to ER-associated degradation (ERAD) pathway inhibition.

Solution in phosphate buffered saline, pH 7.4

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