AB79852

Anti-Hsp70 antibody

Name: Anti-Hsp70 antibody (ab79852) | Abcam
Brand: Abcam Limited
SKU: AB79852
Price: 565 USD
Availability: InStock
Rating: 4 (3 reviews)

(3 Reviews)

(62 Publications)

Rabbit Polyclonal Hsp70 antibody. Suitable for WB, IHC-P, ICC/IF and reacts with Mouse, Human, Rat samples. Cited in 62 publications. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human HSPA1A.

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

Immunocytochemistry/ Immunofluorescence - Anti-Hsp70 antibody (AB79852)

ICC/IF

Supplier Data

Immunocytochemistry/ Immunofluorescence - Anti-Hsp70 antibody (AB79852)

Immunocytochemistry/Immunofluorescence analysis of heat shocked HeLa cells staining Hsp70 using ab79852 at a 1 : 100 dilution. The secondary antibody was a FITC conjugated Goat Anti-Rabbit (green) at a 1 : 200 dilution. Counterstain : DAPI (blue) nuclear stain at 1 : 40000. A) DAPI (blue) nuclear stain. (B) Anti-Hsp70 Antibody. (C) Composite.

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Hsp70 antibody (AB79852)

IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Hsp70 antibody (AB79852)

Immunohistochemistry of human colon carcinoma staining Hsp70 using ab79852 at 1 : 50000. A Biotin conjugated Goat Anti-Rabbit antibody at 1 : 2000 was used as a secondary antibody and Methyl Green at 200uL was used to counter stain.

ICC/IF

Supplier Data

Immunocytochemistry/ Immunofluorescence - Anti-Hsp70 antibody (AB79852)

Immunofluorescent analysis of 2% Formaldehyde-fixed Heat Shocked Cervical cancer cell line (HeLa) labeling Hsp70 with ab79852 at 1/100 dilution. Secondary antibody : APC Goat Anti-Rabbit (red) at 1/200 dilution. (A) DAPI (blue) nuclear stain. (B) Anti-Hsp70 Antibody. (C) Composite. Heat Shocked at 42°C for 1h.

IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Hsp70 antibody (AB79852)

Immunohistochemical analysis of paraffin-embedded formalin fixed (4%) mouse Inflamed colon tissue labelling Hsp70 with ab79852 at 1/1000 dilution for 12 hours at 4°C, followed by secondary antibody Goat Anti-Rabbit (Biotin) at 1/2000 dilution for 1 hour at RT. Counter stained with Methyl Green at 200uL for 2 min at RT.

Supplier Data

Western blot - Anti-Hsp70 antibody (AB79852)

Blocking buffer : 1.5% BSA for 30 minutes at RT.

All lanes:

Western blot - Anti-Hsp70 antibody (ab79852) at 1/10000 dilution

Lane 1:

A431 cell lysate at 2 µg

Lane 2:

A549 cell lysate at 2 µg

Lane 3:

HCT116 cell lysate at 2 µg

Lane 4:

HeLa cell lysate at 2 µg

Lane 5:

HEK293 cell lysate at 2 µg

Lane 6:

HepG2 cell lysate at 2 µg

Lane 7:

HL-60 cell lysate at 2 µg

Lane 8:

HUVEC cell lysate at 2 µg

Lane 9:

Jurkat cell lysate at 2 µg

Lane 10:

MCF7 cell lysate at 2 µg

Lane 11:

PC3 cell lysate at 2 µg

Lane 12:

T98G cell lysate at 2 µg

Lane 13:

Rat brain cell lysate at 2 µg

Secondary

All lanes:

HRP Donkey Anti-Rabbit IgG

Predicted band size: 70 kDa

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Unknown

Western blot - Anti-Hsp70 antibody (AB79852)

Western blot analysis of Mouse Pam212 cells showing detection of HSP70 protein using ab79852 ). Load : 15 µg protein. Block : 1.5% BSA for 30 minutes at RT. Primary Antibody : ab79852 at 1 : 1000 for 2 hours at RT. Secondary Antibody : Donkey Anti-Rabbit IgG : HRP for 1 hour at RT.

All lanes:

Western blot - Anti-Hsp70 antibody (ab79852) at 1/1000 dilution

All lanes:

Cell lysates prepared from mouse Pam212 cells

Observed band size: 70 kDa

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Key facts

Host species

Rabbit

Clonality

Polyclonal

Carrier free

Reacts with

Mouse, Rat, Human

Applications

ICC/IF, WB, IHC-P

applications

Immunogen

Recombinant Full Length Protein corresponding to Human HSPA1A.

P0DMV8

Specificity

Detects a 70kDa protein corresponding to the molecular mass of inducible hsp70. May cross-react with Hsc70 at lower dilutions.

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Alternative Products

Secondary Antibodies

AB150077

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

Immunocytochemistry/ Immunofluorescence - Goat Anti-Rabbit IgG H&L (Alexa Fluor® 488) (AB150077)

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 Immunogen

Storage buffer

pH: 7.4 Preservative: 0.09% 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 (62)

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

Journal for immunotherapy of cancer 13: PubMed40341024

2025

Blocking LIF and PD-L1 enhances the antitumor efficacy of SBRT in murine PDAC models.

Applications

Unspecified application

Species

Unspecified reactive species

Jian Ye,Shuyang S Qin,Angela L Hughson,Gary Hannon,Noah A Salama,Tara G Vrooman,Maggie L Lesch,Sidney Lesser,Sarah L Eckl,Rachel Jewell,Lauren Benoodt,Bradley N Mills,Carl J Johnston,Edith Lord,Brian A Belt,Laura M Calvi,David Linehan,Nadia Luheshi,Jim Eyles,Scott A Gerber

Cell communication and signaling : CCS 23:178 PubMed40205436

2025

Zinc finger DHHC-type palmitoyltransferase 13-mediated S-palmitoylation of GNA13 from Sertoli cell-derived extracellular vesicles inhibits autophagy in spermatogonial stem cells.

Applications

Unspecified application

Species

Unspecified reactive species

Heran Cao,Huihui Gao,Yan Li,Long Li,Shujuan Liu,Tianqi Jin,Yang Wang,Ye Gong,Shuiqiao Yuan,Wuzi Dong

Journal for immunotherapy of cancer 11: PubMed37142292

2023

CD73 and PD-L1 dual blockade amplifies antitumor efficacy of SBRT in murine PDAC models.

Applications

Unspecified application

Species

Unspecified reactive species

Jian Ye,Nicholas W Gavras,David C Keeley,Angela L Hughson,Gary Hannon,Tara G Vrooman,Maggie L Lesch,Carl J Johnston,Edith M Lord,Brian A Belt,David C Linehan,Jim Eyles,Scott A Gerber

Nature communications 13:7860 PubMed36543770

2022

SOX17-positive rete testis epithelium is required for Sertoli valve formation and normal spermiogenesis in the male mouse.

Applications

Unspecified application

Species

Unspecified reactive species

Aya Uchida,Kenya Imaimatsu,Honoka Suzuki,Xiao Han,Hiroki Ushioda,Mami Uemura,Kasane Imura-Kishi,Ryuji Hiramatsu,Hinako M Takase,Yoshikazu Hirate,Atsuo Ogura,Masami Kanai-Azuma,Akihiko Kudo,Yoshiakira Kanai

Journal of extracellular vesicles 11:e12291 PubMed36468940

2022

Comparison of viral inactivation methods on the characteristics of extracellular vesicles from SARS-CoV-2 infected human lung epithelial cells.

Applications

Unspecified application

Species

Unspecified reactive species

Supasek Kongsomros,Nutkridta Pongsakul,Jirawan Panachan,Ladawan Khowawisetsut,Jinjuta Somkird,Chak Sangma,Tapanee Kanjanapruthipong,Patompon Wongtrakoongate,Arthit Chairoungdua,Kovit Pattanapanyasat,David S Newburg,Ardythe L Morrow,Suradej Hongeng,Arunee Thitithanyanont,Somchai Chutipongtanate

Burns & trauma 10:tkac043 PubMed36439706

2022

HSP70 alleviates sepsis-induced cardiomyopathy by attenuating mitochondrial dysfunction-initiated NLRP3 inflammasome-mediated pyroptosis in cardiomyocytes.

Applications

Unspecified application

Species

Unspecified reactive species

Chenlu Song,Yiqiu Zhang,Qing Pei,Li Zheng,Meiyu Wang,Youzhen Shi,Shan Wu,Wei Ni,Xiujun Fu,Yinbo Peng,Wen Zhang,Min Yao

Adipocyte 11:572-587 PubMed36093813

2022

Adipose-derived mesenchymal stem cell-secreted extracellular vesicles alleviate non-alcoholic fatty liver disease delivering miR-223-3p.

Applications

Unspecified application

Species

Unspecified reactive species

Qinghui Niu,Ting Wang,Zhiqiang Wang,Feng Wang,Deyu Huang,Huali Sun,Hanyun Liu

Cancers 14: PubMed35681607

2022

Extracellular Vesicle-Based Method for Detecting Amplification Status of Pediatric Neuroblastoma.

Applications

Unspecified application

Species

Unspecified reactive species

Jirawan Panachan,Napat Rojsirikulchai,Nutkridta Pongsakul,Ladawan Khowawisetsut,Pongpak Pongphitcha,Teerapong Siriboonpiputtana,Takol Chareonsirisuthigul,Pitichai Phornsarayuth,Nisakorn Klinkulab,Natini Jinawath,Wararat Chiangjong,Usanarat Anurathapan,Kovit Pattanapanyasat,Suradej Hongeng,Somchai Chutipongtanate

Journal of inflammation research 15:2213-2228 PubMed35411167

2022

HSP70 Ameliorates Septic Acute Kidney Injury via Binding with TRAF6 to Inhibit of Inflammation-Mediated Apoptosis.

Applications

Unspecified application

Species

Unspecified reactive species

Yiqiu Zhang,Chenlu Song,Wei Ni,Qing Pei,Caixia Wang,Youguo Ying,Min Yao

Biomolecules 12: PubMed35327602

2022

HSP70 Ameliorates Septic Lung Injury via Inhibition of Apoptosis by Interacting with KANK2.

Applications

Unspecified application

Species

Unspecified reactive species

Qing Pei,Wei Ni,Yihang Yuan,Jing Yuan,Xiong Zhang,Min Yao

View all publications

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