Hsc70 anticorps
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- Antigène Voir toutes Hsc70 (HSPA8) Anticorps
- Hsc70 (HSPA8) (Heat Shock 70kDa Protein 8 (HSPA8))
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Reactivité
- Humain, Rat, Souris
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Hôte
- Lapin
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Clonalité
- Polyclonal
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Conjugué
- Cet anticorp Hsc70 est non-conjugé
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Application
- Western Blotting (WB), ELISA, Immunocytochemistry (ICC), Immunofluorescence (IF)
- Specificité
- Hsc70 Antibody detects endogenous levels of total hsc70
- Réactivité croisée
- Humain, Souris, Rat (Rattus)
- Purification
- The antiserum was purified by peptide affinity chromatography using SulfoLinkTM Coupling Resin (Thermo Fisher Scientific).
- Immunogène
- A synthesized peptide derived from human hsc70
- Isotype
- IgG
- Top Product
- Discover our top product HSPA8 Anticorps primaire
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- Indications d'application
- WB 1:500-1:2000, IF/ICC 1:100-1:500
- Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- 1 mg/mL
- Buffer
- Rabbit IgG in phosphate buffered saline , pH 7.4, 150 mM NaCl, 0.02 % sodium azide and 50 % glycerol.
- Agent conservateur
- Sodium azide
- Précaution d'utilisation
- This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
- Stock
- -20 °C
- Stockage commentaire
- Store at -20 °C.Stable for 12 months from date of receipt
- Date de péremption
- 12 months
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Aging as a Precipitating Factor in Chronic Restraint Stress-Induced Tau Aggregation Pathology, and the Protective Effects of Rosmarinic Acid." dans: Journal of Alzheimer's disease : JAD, Vol. 49, Issue 3, pp. 829-44, (2016) (PubMed).
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Aging as a Precipitating Factor in Chronic Restraint Stress-Induced Tau Aggregation Pathology, and the Protective Effects of Rosmarinic Acid." dans: Journal of Alzheimer's disease : JAD, Vol. 49, Issue 3, pp. 829-44, (2016) (PubMed).
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- Antigène
- Hsc70 (HSPA8) (Heat Shock 70kDa Protein 8 (HSPA8))
- Autre désignation
- hsc70 (HSPA8 Produits)
- Synonymes
- anticorps hsc54, anticorps hsc70, anticorps hsc71, anticorps hsp71, anticorps hsp73, anticorps hspa10, anticorps lap1, anticorps nip71, anticorps HSC54, anticorps HSC70, anticorps HSC71, anticorps HSP71, anticorps HSP73, anticorps HSPA10, anticorps LAP1, anticorps NIP71, anticorps Hsc70, anticorps 2410008N15Rik, anticorps Hsc71, anticorps Hsc73, anticorps Hsp73, anticorps Hspa10, anticorps wu:fb01g06, anticorps wu:fi48b06, anticorps heat shock protein family A (Hsp70) member 8 L homeolog, anticorps heat shock protein family A (Hsp70) member 8, anticorps heat shock 70kDa protein 8, anticorps heat shock protein 8, anticorps hspa8.L, anticorps HSPA8, anticorps Hspa8, anticorps hspa8
- Sujet
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Description: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24318877, PubMed:27474739, PubMed:24121476, PubMed:26865365). Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:10722728, PubMed:11276205). Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 (PubMed:23990462).
Gene: HSPA8
- Poids moléculaire
- 70 kDa
- ID gène
- 3312
- UniProt
- P11142
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