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HSP70 Products

(Heat Shock Protein 70 (HSP70))
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. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity 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. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of 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. Maintains protein homeostasis during cellular stress through two opposing acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation. Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle. Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation. Negatively regulates heat shock- induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response. {ECO:0000250|UniProtKB:P0DMV8}.

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Featured HSP70 Categories

HSP70 Antibodies

High quality antibodies with extensive validation data.

HSP70 ELISA Kits

Reliable ELISA kits for a wide range of species.

HSP70 Proteins

Proteins for various applications incl. WB, ELISA, IF etc.

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Cat. No. ABIN361708
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Recommended HSP70 ELISA Kits

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Latest Publications for our HSP70 products

Kuta, Larochelle, Fernandez, Pal, Minotti, Tibshirani, St Louis, Gentil, Nalbantoglu, Hermann, Durham et al.: "Depending on the stress, histone deacetylase inhibitors act as heat shock protein co-inducers in motor neurons and potentiate arimoclomol, exerting neuroprotection through multiple mechanisms in ALS ..." in: Cell stress & chaperones, Vol. 25, Issue 1, pp. 173-191, (2020) (PubMed).

Llorà-Batlle, Michel-Todó, Witmer, Toda, Fernández-Becerra, Baum, Cortés: "Conditional expression of PfAP2-G for controlled massive sexual conversion in Plasmodium falciparum." in: Science advances, Vol. 6, Issue 24, pp. eaaz5057, (2020) (PubMed).

Alnahdi, Sharaf: "Possible prophylactic effect of omega-3 fatty acids on cadmium-induced neurotoxicity in rats' brains." in: Environmental science and pollution research international, Vol. 26, Issue 30, pp. 31254-31262, (2020) (PubMed).

Hua, Wang, Lian, Li, Xi, Xue, Kang, Lei: "Small RNA-seq analysis of extracellular vesicles from porcine uterine flushing fluids during peri-implantation." in: Gene, Vol. 766, pp. 145117, (2020) (PubMed).

Bancells, Llorà-Batlle, Poran, Nötzel, Rovira-Graells, Elemento, Kafsack, Cortés: "Revisiting the initial steps of sexual development in the malaria parasite Plasmodium falciparum." in: Nature microbiology, Vol. 4, Issue 1, pp. 144-154, (2019) (PubMed).

Bhattacharya, Bernasconi, Picard: "Luminescence resonance energy transfer between genetically encoded donor and acceptor for protein-protein interaction studies in the molecular chaperone HSP70/HSP90 complexes." in: Scientific reports, Vol. 8, Issue 1, pp. 2801, (2019) (PubMed).

Zhang, Zhao, Zhang, Hao, Yu, Min, Li, Ma, Chen, Yi, Tang, Meng, Liu, Wang, Shen, Zhang: "Decrease in male mouse fertility by hydrogen sulfide and/or ammonia can Be inheritable." in: Chemosphere, Vol. 194, pp. 147-157, (2018) (PubMed).

Lamy, Jurkovich, Rodrigues, Geraldo, Cachucho, Silva, Matos, Capela E Silva, Pinheiro, Könyves, Bakony, Pereira: "Detection of 70 kDa heat shock protein in the saliva of dairy cows." in: The Journal of dairy research, Vol. 84, Issue 3, pp. 280-282, (2018) (PubMed).

Kaczmarek, Lagiedo, Masztalerz, Kozlowska, Nowicka, Brajer, Batura-Gabryel, Sikora: "Concentrations of SP-A and HSP70 are associated with polarization of macrophages in pleural effusions of non-small cell lung cancer." in: Immunobiology, Vol. 223, Issue 2, pp. 200-209, (2018) (PubMed).

Gonzalez-Rivas, DiGiacomo, Giraldo, Leury, Cottrell, Dunshea: "Reducing rumen starch fermentation of wheat with three percent sodium hydroxide has the potential to ameliorate the effect of heat stress in grain-fed wethers." in: Journal of animal science, Vol. 95, Issue 12, pp. 5547-5562, (2018) (PubMed).

Synonyms and alternative names related to HSP70

heat shock protein family A (Hsp70) member 4 (HSPA4), CG5834 gene product from transcript CG5834-RA (Hsp70Bbb), heat shock protein 70 (HSP70), heat shock protein family A (Hsp70) member 6 (HSPA6), heat shock 70kDa protein 2 (HSPA2), heat shock 70 kD protein cognate (HSP70), Hsp70 family chaperone (HSP70), Heat shock protein 70 (PCC7424_2419), Heat shock protein 70 (Isop_1041), Heat shock protein 70, putative (CGB_C3390W), Heat shock protein 70 (Bacsa_1698), heat shock protein 70 (dnaK-B), heat shock protein 70 (LOC100305036), heat shock protein 1B (Hspa1b), heat shock protein family A member 4 (Hspa4), heat shock 70kDa protein 1A (HSPA1A), heat shock protein 1 (hsp1), Heat Shock Protein (hsp-70), heat shock cognate 70-kd protein (hsp70), Heat shock 70 kDa protein 1A (LOC108348108), APG-2, ARABIDOPSIS HEAT SHOCK PROTEIN 70, ATHSP70, CG5834, CG31354, DmelCG5834, heat shock protein 70, HS24/P52, hsc70, hsp68, hsp70, HSP70, Hsp70, Hsp70-1, HSP70-1, HSP70-2, hsp70-5, Hsp70.1, HSP70.1, HSP70.2, hsp70B, HSP70B', Hsp70Bb, hsp70Bb-prime, hsp70RY, Hsp110, HSPA1, HSPA1B, HSPA2, HSPA6, HSPH2, irp94, LOC100305036, RY

Protein level used designations for HSP70

  • heat shock 70 kDa protein 4
  • heat shock 70-related protein APG-2
  • heat shock 70kD protein 4
  • heat shock protein, 110 kDa
  • hsp70 RY
  • Hsp70Bbb
  • CG5834-PA
  • Hsp70Bbb-PA
  • heat shock 70 kDa protein 1
  • Heat shock 70 kDa protein 6
  • heat shock 70 kDa protein
  • heat shock 70 kDa protein B'
  • dnaK-type molecular chaperone
  • heat shock protein 70
  • heat shock 70 kD protein cognate
  • hypothetical protein
  • Heat shock protein 70
  • CF Hsp70
  • Heat shock cognate 71 kDa protein
  • 68 kDa heat shock protein
  • heat shock 70 kDa protein 1B
  • heat shock 70kDa protein 1B
  • heat shock protein 70.1
  • heat shock protein, 70 kDa 1
  • ischemia responsive 94 kDa protein
  • 70 kda heat shock protein-2
  • HSP70.2
  • chaperone
  • heat shock 70 kD protein 2
  • heat shock 70 kDa protein 2
  • heat-shock 70-kilodalton protein 1B
  • CL45_1
  • CL45_1(648)
  • CL45_1_ov
  • Heat shock 70 kDa protein
  • heat shock protein 70 kDa
  • hsp 70-1
  • npi119-hsp1
  • heat shock 70 kDa protein 1A/1B
  • Heat shock cognate 70 kDa protein
  • heat shock cognate 70-kd protein
  • Heat shock 70 kDa protein 1
  • Heat shock 70 kDa protein 2
  • heat shock 70 kDa protein 1A
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