Recombinant Human HERPUD1 protein (His tag N-Terminus)
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Recombinant Human HERPUD1 protein (His tag N-Terminus) is a Human Fragment protein, in the 1 to 263 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
HERP, KIAA0025, MIF1, HERPUD1, Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein, Methyl methanesulfonate (MMF)-inducible fragment protein 1
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human HERPUD1 protein (His tag N-Terminus) (AB187459)
15% SDS-PAGE analysis of ab187459 (3μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
HERPUD1 helps maintain cellular homeostasis during periods of ER stress by facilitating the degradation of misfolded proteins. It forms part of a larger complex in the ER-associated degradation (ERAD) pathway which targets these proteins for retrotranslocation and subsequent destruction by the proteasome. HERPUD1 therefore plays a vital role in mitigating the buildup of potentially harmful proteins within the cell.
Pathways
HERPUD1 is integral to the unfolded protein response (UPR) and the ERAD pathway. In the UPR HERPUD1 is involved in signaling mechanisms that help restore normal ER function. It interacts with other proteins such as SEL1L and DERLIN-1 within the ERAD pathway to ensure the proper disposal of misfolded proteins preventing cellular damage.
Specifications
Form
Liquid
Additional notes
ab187459 was purified by using conventional chromatography techniques.
General info
Function
Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins (PubMed : 16289116, PubMed : 28827405). Could enhance presenilin-mediated amyloid-beta protein 40 generation. Binds to ubiquilins and this interaction is required for efficient degradation of CD3D via the ERAD pathway (PubMed : 18307982).
Target data
Product promise
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