117048 New Product for COD analysis - Sulfuric acid 95 - 97% for COD determination
- Document Type:
- Technical Information
1.17048
14 Results
Advanced Search
Showing
Narrow Your Results Use the filters below to refine your search
Document Type
-
-
COA 117048
- Document Type:
- Certificate of Analysis
- Product Catalog Number:
- 117048
-
Manual Spectroquant®Prove Connect to Dashboard - English
- Document Type:
- User Guide
- Product Catalog Number:
- Multiple
- Product Catalog Name:
- Multiple
-
SQ Test Kits Power Generation Plant
- Document Type:
- Brochure
- Product Catalog Number:
- Multiple
- Product Catalog Name:
- Multiple
-
Spectroquant®Prove Quick Guide - Chinese Simplified
- Document Type:
- Instructions for Use
- Product Catalog Number:
- Multiple
- Product Catalog Name:
- Multiple
-
Manual Spectroquant®Prove Connect to LIMS - English
- Document Type:
- User Guide
- Product Catalog Number:
- Multiple
- Product Catalog Name:
- Multiple
-
- Document Type:
- Operational Excellence Dossier
- Product Catalog Number:
- 137048
- Product Catalog Name:
- D(+)-Glucose
-
Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. Coactivator-associated arginine methyltransferase.
- The RNA-binding protein HuR stabilizes labile mRNAs carrying AU-rich instability elements. This mRNA stabilization can be induced by hypoxia, lipopolysaccharide, and UV light. The mechanism by which these stimuli activate HuR is unclear and might be related to post-translational modification of this protein. Here we show that HuR can be methylated on arginine. However, HuR is not a substrate for PRMT1, the most prominent protein-arginine methyltransferase in mammalian cells, which methylates a number of heterogeneous nuclear ribonucleoproteins. Instead, HuR is specifically methylated by coactivator-associated arginine methyltransferase 1 (CARM1), a protein-arginine methyltransferase previously shown to serve as a transcriptional coactivator. By analyzing methylation of specific HuR arginine-to-lysine mutants and by sequencing radioactively methylated HuR peptides, Arg(217) was identified as the major HuR methylation site. Arg(217) is located in the hinge region between the second and third of the three HuR RNA recognition motif domains. Antibodies against a methylated HuR peptide were used to demonstrate in vivo methylation of HuR. HuR methylation increased in cells that overexpressed CARM1. Importantly, lipopolysaccharide stimulation of macrophages, which leads to HuR-mediated stabilization of tumor necrosis factor alpha mRNA in these cells, caused increased methylation of endogenous HuR. Thus, CARM1, which plays a role in transcriptional activation through histone H3 methylation, may also play a role in post-transcriptional gene regulation by methylating HuR.
- Document Type:
- Reference
- Product Catalog Number:
- 14-1048
- Product Catalog Name:
- Human recombinant CARM1
-
Certificate of Analysis 1.120SB 9-048-002
- Document Type:
- Certificate of Analysis
- Lot Number:
- 9-048-002
- Product Catalog Number:
- 1.120SB
- Product Catalog Name:
- Readycult® Sample Bottle, Gamma Irradiated
