{"product_id":"abcam-ab91598","title":"Abcam, ab91598, Recombinant E. coli Hsp40 protein","description":"\u003cp\u003eSize: 50µg\u003cbr\u003e\nRecombinant E. coli Hsp40 protein is a Human Full Length protein, expressed in Escherichia coli, with \u0026gt;90%, suitable for SDS-PAGE, WB, FuncS.\u003cbr\u003e\nKey facts\u003cbr\u003e\nPurity:\u0026gt;90% SDS-PAGE,\u003cbr\u003e\nExpression system:Escherichia coli,\u003cbr\u003e\nTags:Tag free,\u003cbr\u003e\nApplications:WB, SDS-PAGE, FuncSSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,\u003cbr\u003e\nBiologically active:Yes,\u003cbr\u003e\nBiological activity:Protein Refolding Assay: Positive Tested positive for its ability to stimulate DnaK's protein-refolding activity in the presence of GrpE.,\u003cbr\u003e\nAccession:P25685,\u003cbr\u003e\nAnimal free:No,\u003cbr\u003e\nCarrier free:No,\u003cbr\u003e\nSpecies:Human,\u003cbr\u003e\nStorage buffer:Constituents: 10% Glycerol (glycerin, glycerine), 1.5% Potassium chloride, 0.595% HEPES, 0.077% (R*,R*)-1,4-Dimercaptobutan-2,3-diol\u003c\/p\u003e\n\n\u003cp\u003eProduct details:\u003cbr\u003e\nDnaJ has a tendency to aggregate in solution with ionic strength lower than 0.1 M KCl. Where lower salt conditions are required, addition of 0.05% Triton-X100 or Brij 58 is recommended.\u003c\/p\u003e\n\n\u003cp\u003eProperties and Storage Information:\u003cbr\u003e\nShipped at conditions-Dry Ice, Appropriate long-term storage conditions--80°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze \/ thaw cycle\u003c\/p\u003e\n\n\u003cp\u003eSupplementary Information:\u003cbr\u003e\nThis supplementary information is collated from multiple sources and compiled automatically.\u003cbr\u003e\nHsp40 also known as DnaJB1 is a member of the heat shock protein family that acts mechanically as a molecular chaperone. This protein with a mass of approximately 41 kDa assists in protein folding and stabilization preventing aggregation under stress conditions. Hsp40 proteins are widely expressed in various tissues and are important in maintaining cellular homeostasis. In addition to DnaJB1 other aliases include 3b9 and 2a7 which emphasize its variety within the Hsp40 family.\u003cbr\u003e\nBiological function summary\u003cbr\u003e\nHsp40 proteins participate in cell signaling and stress response by modulating the activity of Hsp70 forming a functional complex with it to guide protein folding processes. This process is essential for protein quality control and cellular protection. It interacts with unfolded proteins and delivers them to Hsp70 enhancing its ATPase activity necessary for the proper functioning of these molecular chaperones. The expression of Hsp40 in stress conditions highlights its importance in the protein quality control system.\u003cbr\u003e\nPathways\u003cbr\u003e\nHsp40 is involved in important cellular mechanisms like the unfolded protein response and protein catabolism pathways. It works closely with Hsp70 playing a pivotal role in managing protein misfolding and aggregation vital for cellular stress response and recovery. In these pathways Hsp40's function ensures the proper folding and degradation of damaged proteins maintaining proteostasis in the cell.\u003cbr\u003e\nHsp40 influences the development of neurodegenerative diseases and certain cancers. Mutations or altered expression of Hsp40 can lead to disrupted protein homeostasis contributing to conditions like Alzheimer's disease and tumor progression. In Alzheimer's disease besides interacting with Hsp70 Hsp40 affects the accumulation of amyloid-beta peptides. In cancer contexts it may interact with other chaperone proteins affecting their function and therefore promoting tumor aggressiveness and resistance to stress.\u003c\/p\u003e","brand":"Abcam","offers":[{"title":"Default Title","offer_id":46843852325033,"sku":"ab91598","price":0.99,"currency_code":"USD","in_stock":true}],"url":"https:\/\/iright.com\/ar\/products\/abcam-ab91598","provider":"Iright","version":"1.0","type":"link"}