Abcam, ab263191, Human ERMP1 knockout HeLa cell lysate

Size: 1Kit
ERMP1 KO cell lysate available now. KO validated by. Free of charge wild type control included. Knockout achieved by using CRISPR/Cas9, Homozygous: 1 bp insertion in exon 1.
Key facts
Cell type:HeLa,
Species or organism:Human,
Tissue:Cervix,
Knockout validation:Sanger Sequencing,
Mutation description:Knockout achieved by using CRISPR/Cas9, Homozygous: 1 bp insertion in exon 1.,
Disease:Adenocarcinoma

Product details:
Knockout cell lysate achieved by CRISPR/Cas9.
REACH authorisation
Abcam has not and does not intend to apply for the REACH Authorisation of customers' uses of products that contain European Authorisation list (Annex XIV) substances.
It is the responsibility of our customers to check the necessity of application of REACH Authorisation, and any other relevant authorisations, for their intended uses.
Lysate preparation:
Our lysates are made using RIPA buffer to which we add a protease inhibitor cocktail and phosphatase inhibitor cocktail (ratio: 300:100:10).
This means that the protein of interest is denatured.
If you require a native form of the protein please use the live cell version. Please refer to our lysis protocol for further details on how our lysates are prepared.
User storage instructions:
Lyophilizate may be stored at 4°C. After reconstitution, store at -20°C for short-term storage or -80°C for long-term storage.
This product is subject to limited use licenses from The Broad Institute, ERS Genomics Limited and Sigma-Aldrich Co. LLC, and is developed with patented technology. For full details of the licenses and patents please refer to our
limited use license
patent pages

Properties and Storage Information:
Gene name-ERMP1, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Zygosity-Homozygous, Shipped at conditions-Ambient - Can Ship with Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
ERMP1 also known as Endoplasmic Reticulum Metallopeptidase 1 is a protein that plays an important role in cellular processes. The protein has a mass of approximately 127 kDa and is widely expressed in various tissues with higher expression levels in the pancreas liver and other organs with secretory functions. ERMP1 is located in the endoplasmic reticulum where it interfaces with cellular machinery involved in protein folding and processing.
Biological function summary
ERMP1 regulates protein quality control within its cellular environment. By maintaining the integrity of protein synthesis it contributes to the proper functioning of the cellular proteome. ERMP1 is part of the endoplasmic reticulum quality control system ensuring proteins are properly folded and functional before they proceed to their destination. This protein works synergistically with other components of the cellular machinery to execute its functions effectively though it is not part of a specific protein complex.
Pathways
ERMP1 plays a significant role in the endoplasmic reticulum-associated degradation (ERAD) pathway which is essential for clearing misfolded proteins. It contributes to the ubiquitin-proteasome system interacting with proteins involved in tagging defective proteins for degradation. ERMP1 is connected to proteins such as ubiquitin ligases which are important for identifying and targeting proteins for degradation therefore ensuring cellular homeostasis and preventing stress.
ERMP1 has implications in neurodegenerative diseases and diabetes. Its ability to control protein folding and degradation is critical in these contexts. In neurodegenerative diseases such as Alzheimer's ERMP1 can influence the accumulation of misfolded proteins thereby impacting disease progression. Similarly in diabetes the disruption of ERMP1's function affects insulin production and secretion. In both cases the protein's interaction with insulin factor proteins and other signal molecules highlights its importance in disease outcomes.