AB47455

Anti-Hsp70 antibody [C92F3A-5]

Name: Anti-Hsp70 antibody [C92F3A-5] (ab47455) | Abcam
Brand: Abcam Limited
SKU: AB47455
Rating: 4 (3 reviews)

(3 Reviews)

(47 Publications)

Mouse Monoclonal Hsp70 antibody. Suitable for Flow Cyt, WB, IHC-P and reacts with Human, Mouse, Rat samples. Cited in 47 publications. Immunogen corresponding to Recombinant Fragment Protein within Human HSPA1A aa 400-550.

View Alternative Names

HSP72, HSPA1, HSX70, HSPA1A, Heat shock 70 kDa protein 1A, Heat shock 70 kDa protein 1, Heat shock protein family A member 1A, HSP70-1, HSP70.1, HSP72, HSPA1B, Heat shock 70 kDa protein 1B, Heat shock 70 kDa protein 2, Heat shock protein family A member 1B, HSP70-2, HSP70.2

6 Images

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Hsp70 antibody [C92F3A-5] (AB47455)

IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Hsp70 antibody [C92F3A-5] (AB47455)

Formalin-fixed, paraffin-embedded human colon carcinoma tissue stained for Hsp70 using ab47455 at 1/1000 dilution in immunohistochemical analysis. Counter stained with hematoxylin.

IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Hsp70 antibody [C92F3A-5] (AB47455)

ab47455 staining Hsp70 in mouse colon cancer tissue section by Immunohistochemistry (Bouin's fixed paraffin embedded tissue sections). The primary antibody was diluted at 1/100,000. A Fluorophore conjugated goat anti mouse was used as secondary. An antibody amplifier™ system was used for staining.

Unknown

Western blot - Anti-Hsp70 antibody [C92F3A-5] (AB47455)

All are cancer cell lines.

All lanes:

Western blot - Anti-Hsp70 antibody [C92F3A-5] (ab47455) at 1 µg/mL

Lane 1:

Cell lysate prepared from human A431 cell line

Lane 2:

Cell lysate prepared from human A549 cell line

Lane 3:

Cell lysate prepared from human HCT116 cells line

Lane 4:

Cell lysate prepared from human Hela cell line

Lane 5:

Cell lysate prepared from human HEK293 cell line

Lane 6:

Cell lysate prepared from human HepG2 cell line

Lane 7:

Cell lysate prepared from human HL-60 cell line

Lane 8:

Cell lysate prepared from human HUVEC cell line

Lane 9:

Cell lysate prepared from human Jurkat cell line

Lane 10:

Cell lysate prepared from human MCF7 cell line

Lane 11:

Cell lysate prepared from human PC3 cell line

Lane 12:

Cell lysate prepared from human T98G cell line

Lane 13:

Rat brain tissue lysates

Predicted band size: 70 kDa

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AbReview50309****

Western blot - Anti-Hsp70 antibody [C92F3A-5] (AB47455)

All lanes:

Western blot - Anti-Hsp70 antibody [C92F3A-5] (ab47455) at 1/500 dilution

All lanes:

Rat bone (tibia) whole cell lysate at 50 µg

Predicted band size: 70 kDa

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Image courtesy of an anonymous AbReview

Flow Cytometry - Anti-Hsp70 antibody [C92F3A-5] (AB47455)

Flow Cyt

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Flow Cytometry - Anti-Hsp70 antibody [C92F3A-5] (AB47455)

FACS analysis using ab47455 staining heat shock treated CD3 + CD8 + T cells.

CiteAb

Western blot - Anti-Hsp70 antibody [C92F3A-5] (AB47455)

Hsp70 western blot using anti-Hsp70 antibody [C92F3A-5] ab47455. Publication image and figure legend from Cheng, Y. C., Huang, C. J., et al., 2016, Sci Rep, PubMed 27444754.

ab47455 was used in this publication in western blot. This may not be the same as the application(s) guaranteed by Abcam. For a full list of applications guaranteed by Abcam for ab47455 please see the product overview.

Cell model and expression profiles of HSP27 in neurons differentiated from PDMCs.(A) Cell morphology showing the differentiation of neurons derived from PDMCs. Phase contrast images of PDMCs (left upper panel) and neuron-like cells induced by IBMX (left lower panel). Immunocytochemistry analysis of PDMCs (right upper panel) and differentiated neuron-like cells using anti-NSE antibody (right lower panel). Induced neurons extended neurites and formed synaptic connections with each other (red arrowheads). Scale bar = 100 μm. (B) Temporal expression of HSP27 protein in the study model was profiled using 2D-PAGE. PDMCs were harvested at the indicated time points after treatment with IBMX. The proteins at each time point were profiled using 2-DE-PAGE. Cell extracts (300 μg) from each time point were separately subjected to the 2-DE procedure, and protein spots were visualized with silver staining. The rectangle represents the location of HSP27 in 2D-PAGE images. The HSP27 expression level in each 2-DE-PAGE was selected, marked by a cross and indicated with arrows, showing that the protein expression of HSP27 at different time points decreased after IBMX induction (right panel). (C) qPCR analysis of mRNA expression in the PDMCs after IBMX induction. Each time point was evaluated in five independent experiments. The star indicates statistical significance with p value < 0.05. (D) Immunoblots for HSP27, HSP90, HSP70 and HSPA5 after IBMX induction of PDMCs. Cell extracts (30 μg) were prepared from induced PDMCs at the indicated time points (0, 12, 24 and 48 h). GAPDH was used as an internal control.

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519 FITC

FITC Anti-Hsp70 antibody [C92F3A-5]

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

C92F3A-5

Isotype

IgG1

Carrier free

Reacts with

Mouse, Rat, Human

Applications

IHC-P, Flow Cyt, WB

applications

Immunogen

Recombinant Fragment Protein within Human HSPA1A aa 400-550. The exact immunogen used to generate this antibody is proprietary information.

P0DMV8

Epitope

The mapped epitope is in the region of amino acid residues 436-503.

Specificity

Detects a 70kDa protein corresponding to the molecular mass of Hsp70 of SDS PAGE immunoblots. There is no cross-reactivity to Hsc70 (Hsp73).

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Alternative Products

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AB150077

Goat Anti-Rabbit IgG H&L (Alexa Fluor® 488)

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Primary Antibodies

AB9485

Anti-GAPDH antibody - Loading Control

BOND RX™ Validated|Lab Essentials

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Reactivity data

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Properties and storage information

Form

Liquid

Purification technique

Affinity purification Protein G

Storage buffer

Preservative: 0.1% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine)

Shipped at conditions

Blue Ice

Appropriate short-term storage duration

1-2 weeks

Appropriate short-term storage conditions

+4°C

Appropriate long-term storage conditions

-20°C

Aliquoting information

Upon delivery aliquot

Storage information

Avoid freeze / thaw cycle

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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Hsp70 also known as Heat Shock Protein 70 or HSPA1B is a molecular chaperone with a mass of approximately 70 kDa. It plays a mechanical role by assisting in the proper folding of nascent polypeptide chains and the refolding of misfolded proteins. Researchers often detect Hsp70 using Western blot and immunohistochemistry (IHC) techniques. Hsp70 is widely expressed in many tissues particularly during stress conditions like heat shock where its expression level increases significantly.

Biological function summary

Hsp70 operates by stabilizing intermediate states of folding proteins preventing aggregation and facilitating the correct folding process. It often forms a complex with co-chaperones such as Hsp40 and nucleotide exchange factors. This complex is essential for the protein's activity and function. Additionally Hsp70 participates in protein degradation pathways by guiding misfolded proteins to the proteasome for degradation maintaining cellular homeostasis.

Pathways

This molecular chaperone plays significant roles in the heat shock response and unfolded protein response pathways. Hsp70 interacts closely with proteins such as Hsp90 and co-chaperones which together help protect cells from stress-induced damage. The protein also participates in the JAK/STAT signaling pathway influencing cell proliferation and apoptosis. These interactions suggest an integral role in maintaining cellular integrity during stress conditions.

Overexpression of Hsp70 has been associated with various cancers and neurodegenerative diseases. In cancer Hsp70 helps tumor cells survive the hostile tumor microenvironment partly by interacting with anti-apoptotic proteins such as Bcl-2. In neurodegenerative disorders such as Alzheimer's disease Hsp70 associates with amyloid-beta peptides potentially mitigating their aggregation toxicity. These interactions highlight Hsp70's importance in both protective and pathological cellular processes.

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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Visit the General protocols
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Target data

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 (PubMed : 24012426, PubMed : 24318877, PubMed : 26865365). 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 (PubMed : 27708256). 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 (PubMed : 27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed : 24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed : 23973223). Required as a co-chaperone for optimal STUB1/CHIP ubiquitination of NFATC3 (By similarity). Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed : 9499401). 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 (PubMed : 28842558).. (Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell.

See full target information HSPA1A

Additional targets

HSPA1B

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Publications (47)

Recent publications for all applications. Explore the full list and refine your search

Journal of cancer research and clinical oncology 151:264 PubMed40971071

2025

Low expression of HSP27 and HSP70 predicts poor prognosis in laryngeal squamous cell carcinoma.

Applications

Unspecified application

Species

Unspecified reactive species

Jędrzej Borowczak,Dariusz Łaszczych,Adrianna Czyżnikiewicz,Andrzej Marszałek,Łukasz Szylberg,Magdalena Bodnar

Molecular microbiology 121:1127-1147 PubMed38629786

2024

Chaperones Hsc70 and Hsp70 play distinct roles in the replication of bocaparvovirus minute virus of canines.

Applications

Unspecified application

Species

Unspecified reactive species

Jianhui Guo,Yan Yan,Jinhan Sun,Kai Ji,Zhiping Hei,Liang Zeng,Huanzhou Xu,Xiang Ren,Yuning Sun

International journal of molecular sciences 25: PubMed38203414

2024

Elevated Expression of HSP72 in the Prefrontal Cortex and Hippocampus of Rats Subjected to Chronic Mild Stress and Treated with Imipramine.

Applications

Unspecified application

Species

Unspecified reactive species

Adam Bielawski,Agnieszka Zelek-Molik,Katarzyna Rafa-Zabłocka,Marta Kowalska,Piotr Gruca,Mariusz Papp,Irena Nalepa

BMC cancer 23:972 PubMed37828458

2023

Hyperthermia inhibits cellular function and induces immunogenic cell death in renal cell carcinoma.

Applications

Unspecified application

Species

Unspecified reactive species

Yin Huaqi,Dong Bingqi,Zhao Yanhui,Ma Yongkang,Zhao Shiming,Sun Zhenghui,Du Zheng,Peng Jiangshan,Yang Tiejun

International journal of molecular sciences 24: PubMed37834400

2023

Diaphragm Fatigue in SMNΔ7 Mice and Its Molecular Determinants: An Underestimated Issue.

Applications

Unspecified application

Species

Unspecified reactive species

Francesca Cadile,Deborah Recchia,Massimiliano Ansaldo,Paola Rossi,Giorgia Rastelli,Simona Boncompagni,Lorenza Brocca,Maria Antonietta Pellegrino,Monica Canepari

EMBO reports 24:e53408 PubMed37530743

2023

The cell cycle protein MAD2 facilitates endocytosis of the serotonin transporter in the neuronal soma.

Applications

Unspecified application

Species

Unspecified reactive species

Florian Koban,Michael Freissmuth

Journal of cell science 135: PubMed35543156

2022

Mitochondrial antiviral-signalling protein is a client of the BAG6 protein quality control complex.

Applications

Unspecified application

Species

Unspecified reactive species

Peristera Roboti,Craig Lawless,Stephen High

Journal of cell science 134: PubMed34085697

2021

Genome-wide imaging screen uncovers molecular determinants of arsenite-induced protein aggregation and toxicity.

Applications

Unspecified application

Species

Unspecified reactive species

Stefanie Andersson,Antonia Romero,Joana Isabel Rodrigues,Sansan Hua,Xinxin Hao,Therese Jacobson,Vivien Karl,Nathalie Becker,Arghavan Ashouri,Sebastien Rauch,Thomas Nyström,Beidong Liu,Markus J Tamás

Journal of cell science 134: PubMed33674449

2021

DNAJB chaperones suppress destabilised protein aggregation via a region distinct from that used to inhibit amyloidogenesis.

Applications

Unspecified application

Species

Unspecified reactive species

Shannon McMahon,Steven Bergink,Harm H Kampinga,Heath Ecroyd

PLoS genetics 17:e1008951 PubMed33428620

2021

Differential role of cytosolic Hsp70s in longevity assurance and protein quality control.

Applications

Unspecified application

Species

Unspecified reactive species

Rebecca Andersson,Anna Maria Eisele-Bürger,Sarah Hanzén,Katarina Vielfort,David Öling,Frederik Eisele,Gustav Johansson,Tobias Gustafsson,Kristian Kvint,Thomas Nyström

View all publications

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Product promise

We are committed to supporting your work with high-quality reagents, and we're here for you every step of the way. In the unlikely event that one of our products does not perform as expected, you're protected by our Product Promise.

For full details, please see our Terms & Conditions

Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

For licensing inquiries, please contact partnerships@abcam.com

Anti-Hsp70 antibody [C92F3A-5]

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Hsp70 antibody [C92F3A-5] (AB47455)

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Hsp70 antibody [C92F3A-5] (AB47455)

Western blot - Anti-Hsp70 antibody [C92F3A-5] (AB47455)

Western blot - Anti-Hsp70 antibody [C92F3A-5] (AB47455)

Flow Cytometry - Anti-Hsp70 antibody [C92F3A-5] (AB47455)

Western blot - Anti-Hsp70 antibody [C92F3A-5] (AB47455)

Related conjugates and formulations (1)

Key facts

Host species

Clonality

Clone number

Isotype

Carrier free

Reacts with

Applications

Immunogen

Epitope

Specificity

Alternative Products

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Primary Antibodies

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Primary Antibodies

Complementary Products

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Primary Antibodies

Primary Antibodies

Secondary Antibodies

Primary Antibodies

Reactivity data

Properties and storage information

Form

Purification technique

Storage buffer

Shipped at conditions

Appropriate short-term storage duration

Appropriate short-term storage conditions

Appropriate long-term storage conditions

Aliquoting information

Storage information

Supplementary information

Biological function summary

Pathways

Product protocols

Target data

Additional targets

Publications (47)

Product promise