HERPUD1 Full-Length MS Protein Standard

homocysteine-inducible, endoplasmic reticulum stress-inducible, ubiquitin-like domain member 1

HERPUD1 Full-Length MS Protein Standard (NP_001010989), Labeled with [U- ¹³C₆, ¹⁵N₄]-L-Arginine and [U- ¹³C₆, ¹⁵N₂]-L-Lysine, was produced in human 293 cells (HEK293) with fully chemically defined cell culture medium to obtain incorporation efficiency at Creative-Proteomics. The accumulation of unfolded proteins in the endoplasmic reticulum (ER) triggers the ER stress response. This response includes the inhibition of translation to prevent further accumulation of unfolded proteins, the increased expression of proteins involved in polypeptide folding, known as the unfolded protein response (UPR), and the destruction of misfolded proteins by the ER-associated protein degradation (ERAD) system. This gene may play a role in both UPR and ERAD. Its expression is induced by UPR and it has an ER stress response element in its promoter region while the encoded protein has an N-terminal ubiquitin-like domain which may interact with the ERAD system. This protein has been shown to interact with presenilin proteins and to increase the level of amyloid-beta protein following its overexpression. Alternative splicing of this gene produces multiple transcript variants encoding different isoforms. The full-length nature of all transcript variants has not been determined.

HERPUD1

HERP; Mif1; SUP

NM_001010989

16q13

[U- ¹³C₆, ¹⁵N₄]-L-Arg and [U- ¹³C₆, ¹⁵N₂]-L-Lys

>RC200693 representing NM_001010989
MESETEPEPVTLLVKSPNQRHRDLELSGDRGWSVGHLKAHLSRVYPERPRPEDQRLIYSGKLLLDHQCLR
DLLPKQEKRHVLHLVCNVKSPSKMPEINAKVAESTEEPAGSNRGQYPEDSSSDGLRQREVLRNLSSPGWE
NISRPEAAQQAFQGLGPGFSGYTPYGWLQLSWFQQIYARQYYMQYLAATAASGAFVPPPSAQEIPVVSAP
APAPIHNQFPAENQPANQNAAPQVVVNPGANQNLRMNAQGGPIVEEDDEINRDWLDWTYSAATFSVFLSI
LYFYSSLSRFLMVMGATVVMYLHHVGWFPFRPRPVQNFPNDGPPPDVVNQDPNNNLQEGTDPETEDPNHL
PPDRDVLDGEQTSPSFMSTAWLVFKTFFASLLPEGPPAIAN