Product: HSP70 Antibody
Catalog: DF6085
Source: Rabbit
Application: WB, ELISA(peptide)
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Sheep
Mol.Wt.: 70kD; 70kD(Calculated).
Uniprot: P0DMV8
RRID: AB_2838053

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 100ul $280 In stock
 200ul $350 In stock

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Product Info

WB 1:500-1:2000, ELISA(peptide) 1:20000-1:40000
*The optimal dilutions should be determined by the end user.
Pig(100%), Bovine(100%), Sheep(100%)
HSP70 Antibody detects endogenous levels of total HSP70.
Cite Format: Affinity Biosciences Cat# DF6085, RRID:AB_2838053.
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
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.


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;


HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).



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.

Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P0DMV8 As Substrate

Site PTM Type Enzyme
A2 Acetylation
K3 Acetylation
K3 Ubiquitination
T13 Phosphorylation
Y15 Phosphorylation
S16 Phosphorylation
C17 S-Nitrosylation
K25 Ubiquitination
T37 Phosphorylation
T38 Phosphorylation
S40 Phosphorylation
Y41 Phosphorylation
T45 Phosphorylation
T47 Phosphorylation
R49 Methylation
K56 Acetylation
K56 Ubiquitination
T66 Phosphorylation Q9HC98 (NEK6)
K71 Acetylation
K71 Sumoylation
K71 Ubiquitination
K77 Acetylation
K77 Ubiquitination
S85 Phosphorylation
K88 Acetylation
K88 Ubiquitination
H89 Phosphorylation
K100 Ubiquitination
K102 Ubiquitination
S106 Phosphorylation
Y107 Phosphorylation
K108 Acetylation
K108 Ubiquitination
K112 Acetylation
K112 Ubiquitination
Y115 Phosphorylation
S120 Phosphorylation
S121 Phosphorylation
T125 Phosphorylation
K126 Acetylation
K126 Ubiquitination
K128 Ubiquitination
T140 Phosphorylation
T145 Phosphorylation
Y149 Phosphorylation
S153 Phosphorylation
K159 Acetylation
K159 Ubiquitination
Y183 Phosphorylation
K190 Ubiquitination
K220 Ubiquitination
T222 Phosphorylation
R236 Methylation
K246 Acetylation
K246 Ubiquitination
K250 Ubiquitination
K251 Ubiquitination
S254 Phosphorylation
K257 Ubiquitination
T265 Phosphorylation
T298 Phosphorylation
C306 S-Nitrosylation
S307 Phosphorylation
S312 Phosphorylation
T313 Phosphorylation
K319 Acetylation
K319 Ubiquitination
K325 Ubiquitination
K328 Acetylation
K328 Ubiquitination
K345 Ubiquitination
K348 Acetylation
K348 Ubiquitination
K361 Sumoylation
K361 Ubiquitination
S362 Phosphorylation
Y371 Phosphorylation
K415 Ubiquitination
R416 Methylation
S418 Phosphorylation P17612 (PRKACA)
T419 Phosphorylation
K423 Ubiquitination
S432 Phosphorylation
K451 Ubiquitination
R458 Methylation
R469 Methylation
K497 Ubiquitination
K500 Acetylation
K500 Ubiquitination
T502 Phosphorylation
K507 Acetylation
K507 Sumoylation
K507 Ubiquitination
K512 Acetylation
K512 Ubiquitination
K524 Acetylation
K524 Ubiquitination
Y525 Phosphorylation
K526 Acetylation
K526 Ubiquitination
S537 Phosphorylation
K539 Ubiquitination
S544 Phosphorylation
Y545 Phosphorylation
K550 Methylation
K550 Ubiquitination
S551 Phosphorylation
K559 Methylation
K559 Ubiquitination
K561 Methylation
K561 Ubiquitination
K567 Methylation
K567 Ubiquitination
K568 Methylation
K573 Ubiquitination
S579 Phosphorylation
K589 Ubiquitination
K595 Acetylation
K595 Ubiquitination
K597 Ubiquitination
S608 Phosphorylation
Y611 Phosphorylation
K628 Sumoylation
K628 Ubiquitination
S631 Phosphorylation
S633 Phosphorylation
T636 Phosphorylation

Research Backgrounds


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.


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
Subunit Structure:

Component of the CatSper complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C and TSC2. Interacts with TERT; the interaction occurs in the absence of the RNA component, TERC, and dissociates once the TERT complex has formed. Interacts with TRIM5 (via B30.2/SPRY domain). Interacts with METTL21A. Interacts with DNAAF2 (By similarity). Interacts with PRKN. Interacts with FOXP3. Interacts with NOD2; the interaction enhances NOD2 stability. Interacts with DNAJC9 (via J domain). Interacts with ATF5; the interaction protects ATF5 from degradation via proteasome-dependent and caspase-dependent processes. Interacts with RNF207 (via the C-terminus); this interaction additively increases KCNH2 expression. Interacts with HSF1 (via transactivation domain); this interaction results in the inhibition of heat shock- and HSF1-induced transcriptional activity during the attenuation and recovery phase period of the heat shock response. Interacts with NAA10, HSP40, HSP90 and HDAC4. The acetylated form and the non-acetylated form interact with HOPX and STUB1 respectively. Interacts with NEDD1. Interacts (via NBD) with BAG1, BAG2, BAG3 and HSPH1/HSP105. Interacts with SMAD3. Interacts with DNAJC8. Interacts with NLRP12.


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)

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