Product Description
Size: 10µg
Recombinant Human SORL1 Protein Standard (His tag) is a Human Fragment protein, expressed in HEK 293 cells, with >80%, suitable for SDS-PAGE, sELISA.
Key facts
Purity:>80% SDS-PAGE,
Expression system:HEK 293 cells,
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:Q92673,
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.
SorLA also known as SORL1 or sortilin-related receptor 1 plays a mechanical role in intracellular transport processes. This multi-domain protein with a molecular weight of approximately 250 kDa assists in the trafficking of proteins between the Golgi apparatus endosomes and the cell surface. SorLA expresses most abundantly in neurons but also shows presence in other tissues like the heart and kidney. Its functional expression in these areas indicates a broad role in cellular logistics particularly in neurons where it impacts synaptic functioning.
Biological function summary
SorLA acts as a sorting receptor and contributes significantly to the regulation of protein sorting and signaling pathways within the cell. SorLA interacts with various ligands and forms complexes including lipid transport proteins and neuropeptides. The protein also plays a role in the sorting of the amyloid precursor protein (APP) assisting in the regulation of its processing and reducing the production of amyloid-beta a component significant in neurodegenerative processes.
Pathways
SorLA participates actively in the cellular pathways associated with protein trafficking and processing. It is integral to pathways involving endocytosis and the regulation of APP processing. SorLA interacts with important proteins such as APP and the low-density lipoprotein receptor-related protein 1 (LRP1). These interactions exemplify SorLA’s critical involvement in the cellular maintenance of protein homeostasis and in mitigating the production of potentially pathogenic peptides therefore interfacing with wider neurobiological functions.
SorLA’s role connects with neurodegenerative conditions with a notable focus on Alzheimer’s disease. The protein's interaction with APP processing places it in a central position in the pathology of Alzheimer’s disease as dysregulation can lead to increased amyloid-beta production and plaque formation. Additionally SorLA exhibits relevance in some cardiovascular diseases through its modulation of lipoprotein metabolism linking it with the functioning of proteins like apolipoproteins which when disrupted can contribute to the progression of atherosclerosis.
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Collaboration
Tony Tang
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