Product Details

Uniprot No.

P0DMV8

Target Names

HSPA1A

Alternative Names

Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 1) (HSP70-1) (HSP70.1), HSPA1A, HSP72 HSPA1 HSX70

Species Reactivity

Human, Mouse

Immunogen

Recombinant Human HSPA1A protein

Immunogen Species

Homo sapiens (Human)

Conjugate

Non-conjugated

Clonality

Monoclonal

Isotype

hIgG1

Clone No.

10H11

Purification Method

Affinity-chromatography

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4

Form

Liquid

Tested Applications

ELISA, WB, IHC, IF, FC

Recommended Dilution

Application	Recommended Dilution
WB	1:500-1:2000
IHC	1:50-1:200
IF	1:50-1:200
FC	1:50-1:200

Protocols

ELISA Protocol
Western Blotting(WB) Protocol
Immunohistochemistry (IHC) Protocol
Immunofluorescence (IF) Protocol
Flow Cytometry (FC) Protocol

Troubleshooting and FAQs

Antibody FAQs

Storage

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Lead Time

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Description

HSPA1A, also known as HSP70-1 or HSP72, is a stress-inducible member of the heat shock protein 70 family that plays a central role in cellular proteostasis. This molecular chaperone assists in protein folding, prevents aggregation of misfolded proteins, and facilitates the degradation of damaged polypeptides. HSPA1A expression is rapidly upregulated in response to heat shock, oxidative stress, and other cellular insults, making it a critical marker in studies of stress response, cancer biology, and neurodegenerative disease research.

This recombinant monoclonal antibody, clone 10H11, offers the reproducibility and batch consistency that demanding experimental workflows require. Because recombinant antibodies are produced from defined sequences rather than hybridoma supernatants, researchers can expect uniform performance across experiments and over time, eliminating concerns about lot-to-lot variability that can compromise longitudinal studies.

Validation data demonstrates robust performance across multiple applications. In Western blot analysis, the antibody detects a clean 70 kDa band matching the predicted molecular weight across diverse human cell lines including HEK293, MCF-7, HeLa, Jurkat, and A-431, as well as mouse NIH/3T3 cells, confirming cross-species reactivity with both human and mouse samples. Immunohistochemistry staining in paraffin-embedded human liver cancer tissue shows specific signal with citrate buffer antigen retrieval. Immunofluorescence studies in HepG2 and A549 cells reveal characteristic cytoplasmic localization, while flow cytometry analysis in HeLa cells demonstrates clear separation from isotype control.

This versatile antibody supports researchers investigating cellular stress responses, tumor microenvironment biology, and protein quality control mechanisms across multiple experimental platforms.

Usage

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

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Target Background

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. Involved in the clearance of misfolded PRDM1/Blimp-1 proteins. Sequesters them in the cytoplasm and promotes their association with SYNV1/HRD1, leading to proteasomal degradation.; (Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell.

Gene References into Functions

binding of IL-5 to IL-5Ralpha receptors enhances angiogenic responses by stimulating the expression of HSP70-1 via the eNOS signaling pathway. PMID: 28317868
Downregulation of HSPA1A impaired mesenchymal stem cell osteogenic and chondrogenic differentiation. PMID: 29323151
HSPA1A overexpression promotes lipid accumulation in hepatocytes. PMID: 29631603
Study demonstrates that HSP72 inhibits HDACi-induced apoptosis in Jurkat cell line. PMID: 29395577
In conclusion, HSP70 modulates NF-kappaB activation in alveolar macrophages of TB patients, through inhibiting IkappaB-alpha phosphorylation or acting as a chaperon molecule to prevent NF-kappaB binding to the target genes by facilitating degradation. The upregulated HSP70 may suppress the release of pro-inflammatory cytokines during active pulmonary tuberculosis infection, and prevent overwhelming tissue damage. PMID: 28450725
that HSPA6 and HSPA1A contribute to protection of differentiated human neuronal cells from cellular stress PMID: 29090408
ultramarathon running caused a substantial increase in eHsp72 concentration, but probiotic + glutamine supplementation did not affect eHsp72 levels PMID: 28460195
uHSP72 may be considered as a novel potential diagnostic biomarker for the early detection of Diabetic nephropathy (DN). Moreover, these data support the pivotal role of NLRP3 in the development and progression of DN PMID: 28631886
The G allele of rs1008438G>T of HSPA1A may be a protective factor for cervical cancer among ethnic Han Chinese from Yunnan. PMID: 29188629
measurable HSP72 was not associated with graft versus host disease following allogeneic hematopoietic cell transplantation PMID: 27020764
studies demonstrated that ovarian cancer cells isolated from patients with type II tumors released high levels of immunosuppressive cytokines (i.e., interleukin 10 and transforming growth factor beta) and HspA1A in vitro. PMID: 26868087
This study suggests that logotherapy affects the expression of cortisol, BDI, and pain scales in advanced cervical cancer patients, and that it does not affect the expression of HSP70. PMID: 27644267
Data suggest that two putative NEF (nucleotide exchange factors) orthologs, GRPEL1 and GRPEL2, modulate function of mitochondrial HSP70 (mtHSP70); both GRPEL1 and GRPEL2 associate with mtHSP70 as hetero-oligomeric subcomplex and regulate mtHSP70 transport. (GRPEL = mitochondrial GrpE-like protein; HSP70 = heat-shock protein 70) PMID: 28848044
High HSP72 expression is associated with Cluster Amplified Centrosomes in cancer. PMID: 28720575
mRNA levels of HSP family members (HSP70B', HSP72, HSP40/DNAJ, and HSP20/CRYAB) are upregulated by the intracellular MMP3 overload. PMID: 27206651
Data suggest that both ATP- and peptide-binding domains of HSPA1A can form complexes with an AU-rich element in VEGFA mRNA in vitro; only peptide-binding domain can recover cellular VEGFA mRNA in ribonucleoprotein immunoprecipitation; RNA-binding and mRNA-stabilizing functions of HSPA1A are independent of its protein chaperone cycle. (HSPA1A = heat shock 70 kDa protein 1A; VEGFA = vascular endothelial growth factor A) PMID: 28679534
It has been demonstrated that HSPB8-BAG3-HSP70 ensures the functionality of stress granules and restores proteostasis by targeting defective ribosomal products for degradation. PMID: 27570075
The rs2763979 locus of the HSP70 genes may be associated with susceptibility to noise-induced hearing loss (NIHL) in Chinese individuals, and other HSP70 genes may also be susceptibility genes for NIHL, but the results must be further replicated in additional independent sample sets. PMID: 28182740
These results suggest that NFkappaB engaged with the kappaB motif on the promoter cooperates in Hsp70A1A activation under heat shock in human cells as part of a DNA-break repair complex including DNA-PK and PARP-1. PMID: 28099440
Systematic proteomic identification of the heat shock proteins that interact with estrogen receptor alpha and biochemical characterization of the ERalpha-hsp70 interaction has been reported. PMID: 27483141
epidermal Hsp70-1A contributes to the diversity of skin color by regulating the amount of melanin synthesized in melanocytes and modulating autophagic melanosome degradation in keratinocytes PMID: 27094592
Extracellular Hsp72 immediately post-exercise decreased back to baseline levels by 1 h post-exercise, but cellular Hsp72 expression continued to rise and remained elevated 24 h post-exercise. These data suggest that in addition to the classic physiological biomarkers of exercise heat stress, using cellular Hsp72 as an indicator of lasting effects of stress into recovery may be most appropriate for determining long-term ef PMID: 26643874
HSPA1A and HSPA8 have roles in parturition through stimulating immune inflammatory and estrogen response PMID: 28025138
Data show that BAG2 Inhibits CHIP-Mediated HSP72 ubiquitination in aged cells. PMID: 28042827
indicates increased expression levels of heat shock proteins 90 and 70 and glucose related protein 78 levels in medullary thyroid carcinoma PMID: 28038712
The cardioprotective effect of 40-60 g/d of alcohol consumption could be due in part, to increased intracellular HSPA1A, a potent anti-inflammatory protein. Excessive intake of alcohol increases antibodies anti-Hsp60, stimulating proinflammatory cytokines. This fact may explain the mortality from cardiovascular disease in heavy drinkers. PMID: 26902796
There is a direct correlation between plasma HSPA1A and PAI-1 levels in patients with diabetes, which is lost when they develop albuminuria. PMID: 26637413
The present study revealed that salivary extracellular HSP70 significantly increased at 4 h after the 59 min of intense exercise in sedentary male subjects and correlated with resting salivary secretory immunoglobulin A (SIgA) levels at rest. PMID: 26608509
HSP70-2 (+1267A/G) gene polymorphism was associated with Henoch-Schonlein purpura in children PMID: 26547206
HSP72 blocks fibroblast activation and proliferation in renal fibrosis via targeting the STAT3 pathway and may serve as a novel therapeutic agent for chronic kidney disease regardless of the etiology PMID: 26851345
Studies suggest that heat shock protein 72/70 (Hsp70 proteins) are beneficial to the patient in slowing the onset of neurodegenerative disorders. PMID: 26450908
P53 could be used to distinguish early HCC from advanced hepatocellular carcinoma, but HSP70 cannot PMID: 26494212
cytokines, not being influenced by HSP72 polymorphisms, cortisol, or illness severity. Gln may depress l/mHSP72 after LPS exposure and enhance them after HS induction, but it may not affect early induced HSP72 mRNA. PMID: 26550577
heat acclimation reduces physiological strain, and the transcription of HSP72, but not HSP90alpha mRNA in acute normobaric hypoxia. PMID: 26205540
Hsp72 (HSPA1A) prevents h-IAPP aggregation and toxicity. PMID: 26960140
HSPA1A (rs1043618) is associated with a decreased risk of idiopathic pulmonary fibrosis in a Mexican population. PMID: 26496868
Lysine methylation of HSPA1 differs between metastatic breast and ovarian carcinoma. PMID: 26448330
Together, these results implicate HSP70-1A as a novel angiogenic regulator. PMID: 26657847
The aim of this study was to demonstrate the effects of 6-week low-intensity training on changes in indicators of aerobic capacity and on HSPA1A, HSPB1, and LDHb expression in white blood cells in high level rowers. PMID: 26214432
BDNF, APOE, and HSP70-1 genes, but not GRIN2B, might be associated with a risk of POAG occurrence in the Polish population PMID: 25893192
Leukocyte Hsp72 mRNA was increased immediately after exercise following downhill running compared to flat running and in hot compared to temperate conditions. PMID: 25722377
Equal Hsp72 mRNA increases occurring from consistent, reduced, or increased endogenous strain following short-term heat acclimation and long-term heat acclimation suggest that transcription occurs following attainment of sufficient endogenous criteria. PMID: 25943677
higher levels of plasma Hsp70 and lower levels of plasma Hsp27 might be associated with an increased risk of COPD among coal workers. PMID: 25620081
Serum HSPA1A levels correlate with disease status in rheumatoid arthritis. PMID: 25739548
This is indicative of improved tolerance and ability to cope with the hypoxic insult, potentially mediated in part by increased basal reserves of HSP72. PMID: 25874231
Data indicate that the smallest average tumor weight was present in the AdSurp-heat shock 70kDa protein (Hsp70)+CIK treatment group. PMID: 25473902
Results report high resolution crystal structure of the substrate-bound human HSP70-substrate-bound domain and particularly the alpha and beta loops. PMID: 25058147
HSP72 preserves renal function in I/R injury through its antiapoptotic effects, which act by suppressing mitochondrial Smac/Diablo release and preserving XIAP protein content. PMID: 25394481
The results demonstrate a key role for inducible HSP70 in aiding the processing and hindering the accumulation of misfolded PMP22, which in turn alleviates proteotoxicity within the cells. PMID: 25694550
Nek6 facilitates association of Hsp72 with the mitotic spindle, where it promotes stable K-fiber assembly through recruitment of the ch-TOG-TACC3 complex. PMID: 25940345

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Subcellular Location

Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Secreted. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

Protein Families

Heat shock protein 70 family

Database Links

HGNC: 5232

OMIM: 140550

KEGG: hsa:3303

STRING: 9606.ENSP00000364802

UniGene: Hs.274402

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Code	CSB-RA357302MA1HU
Size	US$210
	Order now
Image	Western Blot Positive WB detected in: HEK293 whole cell lysate(30µg), MCF-7 whole cell lysate(30µg), Hela whole cell lysate(30µg), Jurkat whole cell lysate(30µg), A-431 whole cell lysate(30µg), NIH/3T3 whole cell lysate(30µg) All lanes: HSPA1A antibody at 1:1000 Secondary Goat polyclonal to human IgG at 1/40000 dilution Predicted band size: 70 kDa Observed band size: 70 kDa Exposure time: 2min IHC image of CSB-RA357302MA1HU diluted at 1:50 and staining in paraffin-embedded human liver cancer performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a Anti-Human lgG, Fcy Fragment Specific labeled by HRP and visualized using 0.05% DAB. Immunofluorescence staining of HepG2 cell with CSB-RA357302MA1HU at 1:30 ,counter-stained with DAPI. The cells were fixed in 4% formaldehyde, permeabilized using 0.2% Triton X-100 and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4°C. The secondary antibody was Alexa Fluor 488-congugated AffiniPure Goat Anti-Human IgG(H+L). Immunofluorescence staining of A549 cell with CSB-RA357302MA1HU at 1:30 ,counter-stained with DAPI. The cells were fixed in 4% formaldehyde, permeabilized using 0.2% Triton X-100 and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4°C. The secondary antibody was Alexa Fluor 488-congugated AffiniPure Goat Anti-Human IgG(H+L). Overlay Peak curve showing Hela cells stained with CSB-RA357302MA1HU (red line) at 1:100. The cells were fixed in 4% formaldehyde and permeated by 0.2% TritonX-100 for 10min. Then 10% normal goat serum to block non-specific protein-protein interactions followed by the antibody (1ug/110⁶cells) for 45min at 4℃. The secondary antibody used was Fluorescein (FITC) AffiniPure Goat Anti-Human IgG, Fcγ fragment specific at 1:200 dilution for 35 min at 4℃.Control antibody (green line) was human IgG1 (1ug/110⁶cells) used under the same conditions. Acquisition of >10,000 events was performed.
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HSPA1A Recombinant Monoclonal Antibody

Product Details

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Target Background