Abcam, ab316509, Recombinant Human REST / NRSF Protein Standard (His tag)

Size: 10µg
Recombinant Human REST / NRSF Protein Standard (His tag) is a Human Fragment protein, expressed in Escherichia coli, with >80%, suitable for SDS-PAGE, sELISA.
Key facts
Purity:>80% SDS-PAGE,
Expression system:Escherichia coli,
Tags:His tag C-Terminus,
Applications:sELISA, SDS-PAGESee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:Q13127,
Animal free:Yes,
Carrier free:No,
Species:Human,
Storage buffer:pH: 7.3 - 7.5Constituents: 2.922% Sodium chloride, 0.64107% disodium;hydrogen phosphate;dodecahydrate, 0.02858% Potassium phosphate monobasic

Product details:
While the standard is the same as the one provided in the corresponding SimpleStep ELISA Kit, it cannot be treated as the consumable provided with our SimpleStep ELISA Kit due to differences in its concentration calibration.
Abcam guarantee that this protein standard is suitable for use in a sandwich ELISA. Individual results may vary due to differences in technique, laboratory equipment, buffers, and other experimental factors. The detection range provided for this protein standard is based on initial sandwich ELISA validation data.
The protein concentration is the concentration after validation on our sandwich ELISA platform. This Standard protein is guaranteed to work with our Capture and Detector antibodies in sELISA. Please contact our Scientific Support team to know which antibody pair is suitable for this protein.

Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
REST also known as NRSF (neuron-restrictive silencer factor) is a transcriptional repressor weighing approximately 116 kDa. It regulates gene expression by binding to the RE1 silencing transcription factor (RE1-silencing element) in the DNA. REST is widely expressed in non-neuronal cells and plays a significant role in maintaining neuronal gene silencing in embryonic and adult stem cells. By interacting with co-repressors REST recruits histone deacetylases and methylases to modify chromatin structure effectively shutting down gene transcription in specific contexts.
Biological function summary
REST regulates neuronal differentiation and plasticity by controlling the expression of neuronal-specific genes. It forms a complex with co-repressors such as mSin3 and CoREST participating in diverse biological processes including neurogenesis. REST expression is important for balancing the neuronal gene expression program preventing untimely or inappropriate activation of neuronal genes in non-neuronal tissues. By modulating the expression of synaptic proteins and neurotransmitter receptors REST influences synaptic plasticity and neuronal excitability.
Pathways
REST participates in the neural stem cell differentiation pathway and cell fate determination. It interacts with pathways involving proteins such as HDAC1 and SWI/SNF complexes contributing to chromatin remodeling and transcriptional regulation. Within these pathways REST ensures the maintenance of non-neuronal identity by repressing neuronal gene activation coordinating with other proteins to influence cellular outcomes and fate decisions.
REST has been linked to neurological disorders such as Huntington's disease and epilepsy. In Huntington's disease REST dissociation from the Huntingtin protein increases leading to misregulation of neuronal genes and contributing to neurodegenerative changes. REST also plays a role in epilepsy where its dysregulation can lead to an imbalance in excitatory and inhibitory signals within the brain potentially triggering epileptic episodes. Through its interactions with disease-associated proteins REST exemplifies the complex interplay between transcriptional regulation and cellular dysfunction in disease pathology.