{"product_id":"abcam-ab318970","title":"Abcam, ab318970, Anti-groEL antibody [EPR28718-8]","description":"\u003cp\u003eSize: 20µL \/ 100µL \/ 1mL\u003cbr\u003e\nRabbit Recombinant Monoclonal Hsp60 antibody. Suitable for WB, IHC-P, ICC\/IF, Flow Cyt (Intra) and reacts with Transfected cell lysate - Escherichia coli K-12, Escherichia coli BL21(DE3), Transfected cell line - Escherichia coli K-12 samples.\u003cbr\u003e\nKey facts\u003cbr\u003e\nHost species:Rabbit,\u003cbr\u003e\nClonality:Monoclonal,\u003cbr\u003e\nClone number:EPR28718-8,\u003cbr\u003e\nIsotype:IgG,\u003cbr\u003e\nCarrier free:No,\u003cbr\u003e\nReacts with:Escherichia coli,\u003cbr\u003e\nApplications:IHC-P, ICC\/IF, Flow Cyt (Intra), WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,\u003cbr\u003e\nImmunogen:The exact immunogen used to generate this antibody is proprietary information.\u003c\/p\u003e\n\n\u003cp\u003eProduct details:\u003cbr\u003e\nPatented technology\u003cbr\u003e\nOur RabMAb\u003cbr\u003e\ntechnology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to\u003cbr\u003e\nRabMAb® patents\u003cbr\u003e\nWhat are the advantages of a recombinant monoclonal antibody?\u003cbr\u003e\nThis product is a recombinant monoclonal antibody, which offers several advantages including:\u003cbr\u003e\n- High batch-to-batch consistency and reproducibility\u003cbr\u003e\n- Improved sensitivity and specificity\u003cbr\u003e\n- Long-term security of supply\u003cbr\u003e\n- Animal-free batch production\u003cbr\u003e\nFor more information, read more on\u003cbr\u003e\nrecombinant antibodies\u003c\/p\u003e\n\n\u003cp\u003eProperties and Storage Information:\u003cbr\u003e\nForm-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.2 - 7.4Preservative: 0.01% Sodium azideConstituents: PBS, 40% Glycerol (glycerin, glycerine), 0.05% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°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\nThe groEL protein often known as 60 kDa chaperonin is a highly conserved molecular chaperone with an approximate mass of 60 kilodaltons. It plays an integral role in assisting the correct folding of nascent or stress-denatured proteins in the cell. Expressed prominently in prokaryotic organisms such as E. coli groEL is an important component of the E. coli expression system due to its ability to maintain protein functionality. By forming a double-ring structure that encapsulates substrates groEL collaborates with its co-chaperonin groES to perform essential protein folding.\u003cbr\u003e\nBiological function summary\u003cbr\u003e\nGroEL functions in collaboration with groES as part of a chaperonin complex that stabilizes unfolded proteins and prevents aggregation. It operates by undergoing ATP-dependent conformational changes that create an environment conducive to proper protein folding. E. coli products such as enzymes and structural proteins rely on the folding mechanism orchestrated by groEL to achieve their native conformation. Consequently its role is indispensable for protein homeostasis within E. coli affecting diverse cellular processes.\u003cbr\u003e\nPathways\u003cbr\u003e\nMolecular chaperones including groEL integrate into the protein quality control network which monitors and manages protein integrity and turnover. In particular groEL operates in the folding and stress response pathways. Working closely with other proteins such as DnaK and DnaJ groEL ensures efficient protein folding and repair especially during heat shock conditions. This function maintains cellular viability and is important for cellular adaptation to environmental stressors.\u003cbr\u003e\nDisruptions in groEL function can lead to protein misfolding-related diseases like Alzheimer's and Parkinson's. Although direct links to groEL are less observed in eukaryotic systems similar chaperone proteins like HSP60 show connections to neurodegenerative disorders. Dysfunctional protein homeostasis due to insufficient chaperone activity highlights the role of molecular chaperones in preventing protein aggregation which is implicated in these diseases.\u003c\/p\u003e","brand":"Abcam","offers":[{"title":"Default Title","offer_id":46850364342441,"sku":"ab318970","price":0.99,"currency_code":"USD","in_stock":true}],"url":"https:\/\/iright.com\/products\/abcam-ab318970","provider":"Iright","version":"1.0","type":"link"}