Product: HSP70 Antibody
Catalog: AF5466
Description: Rabbit polyclonal antibody to HSP70
Application: WB IHC IF/ICC
Cited expt.: WB
Reactivity: Human, Mouse, Rat, Monkey
Prediction: Pig, Bovine, Sheep, Xenopus
Mol.Wt.: 70 kDa; 70kD(Calculated).
Uniprot: P0DMV8
RRID: AB_2837950

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 100ul $280 In stock
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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat,Monkey
Prediction:
Pig(100%), Bovine(100%), Sheep(100%), Xenopus(100%)
Clonality:
Polyclonal
Specificity:
HSP70 Antibody detects endogenous levels of total HSP70.
RRID:
AB_2837950
Cite Format: Affinity Biosciences Cat# AF5466, RRID:AB_2837950.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

DnaK type molecular chaperone HSP70 1; Epididymis secretory protein Li 103; FLJ54303; FLJ54370; FLJ54392; FLJ54408; FLJ75127; Heat shock 70 kDa protein 1; Heat shock 70 kDa protein 1/2; Heat shock 70 kDa protein 1A/1B; Heat shock 70kDa protein 1A; Heat shock 70kDa protein 1B; Heat shock induced protein; HEL S 103; HSP70 1; HSP70 1B; HSP70 2; HSP70-1/HSP70-2; HSP70-1A; HSP70.1; HSP70.1/HSP70.2; HSP70I; HSP71_HUMAN; HSP72; HSPA1; HSPA1A; HSPA1B;

Immunogens

Immunogen:

A synthesized peptide derived from human HSP70, corresponding to a region within C-terminal amino acids.

Uniprot:
Gene(ID):
Description:
In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins.
Sequence:
MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Pig
100
Bovine
100
Sheep
100
Xenopus
100
Horse
0
Dog
0
Zebrafish
0
Chicken
0
Rabbit
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

Research Backgrounds

Function:

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 three types: J-domain co-chaperones such as 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. Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its 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.

(Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell.

PTMs:

In response to cellular stress, acetylated at Lys-77 by NA110 and then gradually deacetylated by HDAC4 at later stages. Acetylation enhances its chaperone activity and also determines whether it will function as a chaperone for protein refolding or degradation by controlling its binding to co-chaperones HOPX and STUB1. The acetylated form and the non-acetylated form bind to HOPX and STUB1 respectively. Acetylation also protects cells against various types of cellular stress.

Subcellular Location:

Cytoplasm. Nucleus. Cytoplasm>Cytoskeleton>Microtubule organizing center>Centrosome.
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Family&Domains:

The N-terminal nucleotide binding domain (NBD) (also known as the ATPase domain) is responsible for binding and hydrolyzing ATP. The C-terminal substrate-binding domain (SBD) (also known as peptide-binding domain) binds to the client/substrate proteins. The two domains are allosterically coupled so that, when ATP is bound to the NBD, the SBD binds relatively weakly to clients. When ADP is bound in the NBD, a conformational change enhances the affinity of the SBD for client proteins.

Belongs to the heat shock protein 70 family.

Research Fields

· Cellular Processes > Transport and catabolism > Endocytosis.   (View pathway)

· Environmental Information Processing > Signal transduction > MAPK signaling pathway.   (View pathway)

· Genetic Information Processing > Transcription > Spliceosome.

· Genetic Information Processing > Folding, sorting and degradation > Protein processing in endoplasmic reticulum.   (View pathway)

· Human Diseases > Neurodegenerative diseases > Prion diseases.

· Human Diseases > Infectious diseases: Bacterial > Legionellosis.

· Human Diseases > Infectious diseases: Parasitic > Toxoplasmosis.

· Human Diseases > Infectious diseases: Viral > Measles.

· Human Diseases > Infectious diseases: Viral > Influenza A.

· Human Diseases > Infectious diseases: Viral > Epstein-Barr virus infection.

· Organismal Systems > Aging > Longevity regulating pathway - multiple species.   (View pathway)

· Organismal Systems > Immune system > Antigen processing and presentation.   (View pathway)

· Organismal Systems > Endocrine system > Estrogen signaling pathway.   (View pathway)

References

1). Design of a self-driven probiotic-CRISPR/Cas9 nanosystem for sono-immunometabolic cancer therapy. Nature Communications, 2022 (PubMed: 36550159) [IF=16.6]

2). Cold to Hot: Rational Design of Minimalist Multifunctional Photo-Immunotherapy Nanoplatform toward Boosting Immunotherapy Capability. ACS Applied Materials & Interfaces, 2019 (PubMed: 31429272) [IF=8.3]

Application: WB    Species: mouse    Sample: B16F10 cells

Figure 3. |(A) Fluorescence microscopy images of CRT exposure of different treated B16F10 cells. Nucleus: blue color, CRT: green color. The scale bars are 12.5 μm. (B) Western blots of HSP70 expression of different treated B16F10 cells (n = 3). Statistical significance: *p < 0.05, **p <0.01, and ***p < 0.001.

3). A marine-derived small molecule induces immunogenic cell death against triple-negative breast cancer through ER stress-CHOP pathway. International Journal of Biological Sciences, 2023 (PubMed: 35541893) [IF=8.2]

Application: WB    Species: human    Sample: TNBC cells

Figure 4.| MHO7 induced the release of DAMPs from TNBC cells.(B) Expression of CRT and HSP70 proteins in the cell cytosol and the cell membrane were measured by western blot under treatment with MHO7.

4). PD-L1 blockade potentiates the antitumor effects of ALA-PDT and optimizes the tumor microenvironment in cutaneous squamous cell carcinoma. OncoImmunology, 2022 (PubMed: 35402079) [IF=6.5]

Application: WB    Species: mouse    Sample: tumor

Figure 4.| Synergistic antitumor effects of an anti-PD-L1 mAb and ALA-PDT in a UV-induced cSCC mouse model. (g) After 6 h of treatment,A431 cell membrane lysates were subjected to Western blotting using the indicated antibodies. The blots were probed with Na-K-ATPase as the loading control

5). Mesenchymal stem cell-derived exosome mitigates colitis via the modulation of the gut metagenomics–metabolomics–farnesoid X receptor axis. Biomaterials Science, 2022 (PubMed: 35858469) [IF=5.8]

6). hucMSC-Ex Alleviates IBD-Associated Intestinal Fibrosis by Inhibiting ERK Phosphorylation in Intestinal Fibroblasts. Stem Cells International, 2023 (PubMed: 36845967) [IF=3.8]

7). Exosomes with Highly Angiogenic Potential for Possible Use in Pulp Regeneration. JOURNAL OF ENDODONTICS, 2018 (PubMed: 29426641) [IF=3.5]

8). Aging as a Precipitating Factor in Chronic Restraint Stress-Induced Tau Aggregation Pathology, and the Protective Effects of Rosmarinic Acid. JOURNAL OF ALZHEIMERS DISEASE, 2016 (PubMed: 26577520) [IF=3.4]

Application: WB    Species: mouse    Sample: mouse

Fig. 5. The effect of chronic restraint stress on the expression of chaperone proteins. Homogenates of cerebral cortex from adult (6 months) and middle-age (13 months) mice with or without chronic restraint stress were detected by immunoblotting with antibodies against chaperones including heat shock proteins (HSP70, HSC70, HSP90, and HDJ2/HSP40) and chaperonin TCP1, and also the antibody against Pin1 (A). The protein levels were present as the fold change compared with the level in control of 13-month-old mice. The quantified data of (A) are shown in histograms (B-G). Data were expressed as mean ± SEM, n = 4. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001. H) The expression of HDJ2/HSP40 or Pin1 in HEK293 cells was inhibited by siRNA, and tau gene was transfected by 2.5 g (+) or 5g (++) GV143-tau plasmids. The total extraneous tau, which contained a FLAG tag, were analyzed by anti-FLAG antibody, and P-tau was detected by PS396 antibody.

9). Novel methyltransferase G9a inhibitor induces ferroptosis in multiple myeloma through Nrf2/HO-1 pathway. Annals of hematology, 2024 (PubMed: 38538975) [IF=3.0]

10). Scutellaria barbata Flavonoids Improve the Composited Aβ-induced Abnormal Changes in Glial Cells of the Brains of Rats. COMBINATORIAL CHEMISTRY & HIGH THROUGHPUT SCREENING, 2022 (PubMed: 33297910) [IF=1.6]

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