Blogs for February 2017

4EBP1 and skeletal muscle protein synthesis

Wednesday, February 22, 2017 - 15:58

Eukaryotic translation initiation factor 4E binding protein 1, or 4EBP1, is an mRNA translational repressor protein that negatively regulates eukaryotic translation initiation factor 4E, or EIF4E.  EIF4E is a protein that forms a complex necessary to block the 5’ ends of mRNA with a 7-methyl-guanosine five-prime cap structure, which is important for normal translation of mRNA.  Specifically, the EIF4E complex recruits 40s ribosome subunits to scan mRNA in order to regulate protein synthesis.  When EIF4E is bound to 4EBP1, it is held in an inactive state, however phosphorylation of 4EBP1 will cause its release.  While 4EBP1 has broad implications in translational research, the following articles hone in on how a 4EBP1 antibody plays a role in the regulation of skeletal muscle protein synthesis.


The use of Beta Actin (AC-15) as a loading control across multiple species

Friday, February 17, 2017 - 14:46

Actin is a fundamental component of the cytoskeleton, where it has the ability to create and break down actin filament formation in response to various cell needs.  Actin has six highly conserved isoforms, however beta and gamma actin are the two isoforms that are highly and ubiquitously expressed in the cell.  For this reason, measuring beta-actin levels has served as a useful control in research experiments in order to have a baseline of protein expression to compare cell manipulations to.  However, beta actin has other implications in scientific research aside from acting as a housekeeping gene, and plays a role in cell motility, development, wound healing, cell division and more.  The following articles used the Beta Actin (AC-15) antibody as a loading control in chicken, human and rat samples in order to illustrate its conservation and reliability when used across species. 


The role of HIF-2 alpha in the progression and therapy of clear cell renal cell carcinoma

Monday, February 13, 2017 - 14:51

HIF-2 alpha, also known as hypoxia-inducible factor 2, endothelial PAS domain protein-1, and member of PAS superfamily 2 is part of the HIF family of proteins.  The HIF family is composed of HIF-1, HIF-2 and HIF-3, where HIF-2 is a dimeric protein that consists of an alpha and beta subunit.HIF-2 alphais activated in the presence of oxygen deprivation, or hypoxia, via prolyl hydroxylase-domain enzymes (PHDs) that facilitate its degradation.  HIF-2 alphais expressed in endothelial and intestinal cells, as well as in tumor tissue of a variety of prominent cancers, and is not typically detected in normoxic conditions.  Given the fact that loss of HIF-1 alpha was a notable hallmark of renal cell carcinoma, HIF-2 alpha and the hypoxia mediated gene therapy has been an area of interest in...

Dual applications of a c-Myc antibody in mitochondrial research

Thursday, February 9, 2017 - 08:10

c-Myc, a proto-oncogene, has documented involvement in cellular differentiation, cell growth, cell death and tumor formation.  Target genes of the Myc family include those that participate in cell survival, translation, transcription, metabolism and more.  On a more specific level, c-Myc is a transcription factor that can both activate and repress its target protein by way of DNA modifications.  This allows for the use of a c-Myc antibody in two manners; it can be used to monitor the actual c-Myc protein expression levels, or, it can be used as a probe against a c-Myc protein tagged to another protein of interest. These interactions can be exploited when trying to detect proteins that c-myc interacts with if antibodies against the protein are not available. The structure of c-Myc is what allows for its duality, where its basic-helix-loop-helix-leucine zipper c-term domain can mediate DNA specific binding.  The...

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