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Immunocytochemistry/Immunofluorescence analysis using Rabbit Anti-Hsp70 Polyclonal Antibody (STPA00002). Tissue: Heat Shocked Cervical cancer cell line (HeLa). Species: Human. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Rabbit Anti-Hsp70 Polyclonal Antibody (STPA00002) at 1:100 for 12 hours at 4°C. Secondary Antibody: FITC Goat Anti-Rabbit (green) at 1:200 for 2 hours at RT.
Key Features

Anti-HSP70 Antibody

SKU STPA00002
Antibody Type Polyclonal
Applications WB
Applications IHC
Applications ICC/IF
Applications IP
Applications ELISA
Applications FCM
Reactivity Human
Reactivity Mouse
Reactivity Rat
Reactivity Beluga (Delphinapterus leucas)
Reactivity Bovine
Reactivity Dog
Reactivity Fish
Reactivity Carp (Cypriniformes)
Reactivity Guinea Pig (Cavia porcellus)
Reactivity Hamster
Reactivity Monkey
Reactivity Pig
Reactivity Sheep
Reactivity Coral (Anthozoa)
Reactivity Plant
Reactivity Tomato
Reactivity Tobacco
Reactivity Shark
Reactivity Spiny Dogfish Shark (Squalus acanthias)
Reactivity Atlantic Hagfish (Myxine glutinosa)
Reactivity Leishmania amazonensis
Host Species Rabbit
€642

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Description

HSP70 Antibody

HSP70 Antibody is a rabbit polyclonal antibody directed against HSP70, offered by Assay Genie for research applications. Reported applications include WB, IHC, ICC/IF, IP, ELISA and FCM. Reported reactivity: Human, Mouse, Rat, Beluga (Delphinapterus leucas), Bovine, Dog, Fish, Carp (Cypriniformes), Guinea Pig (Cavia porcellus), Hamster, Monkey, Pig, Sheep, Coral (Anthozoa), Plant, Tomato, Tobacco, Shark, Spiny Dogfish Shark (Squalus acanthias), Atlantic Hagfish (Myxine glutinosa) and Leishmania amazonensis. Purified by Peptide Affinity.

HSP70 proteins are a highly conserved family of 70-kDa molecular chaperones encoded by a multigene family in most eukaryotes and prokaryotes. Found in nearly all cellular compartments—including the cytosol, nucleus, mitochondria, endoplasmic reticulum, and chloroplasts—HSP70s are constitutively expressed and strongly upregulated in response to cellular stress. These chaperones play a vital role in protein homeostasis by binding to nascent polypeptides and partially folded or misfolded proteins, preventing aggregation and facilitating proper folding. HSP70s exhibit high-affinity ATP binding and weak ATPase activity, which is stimulated upon interaction with unfolded substrates. ATP hydrolysis triggers conformational changes that regulate substrate binding and release, enabling dynamic cycles of protein folding and refolding. Structurally, the N-terminal domain of HSP70 is responsible for ATP binding, while the C-terminal domain mediates substrate interaction. This modular design allows HSP70s to coordinate with co-chaperones such as HSP40, HIP, HOP, and BAG-1, integrating folding with degradation and transport pathways. In neurodegenerative disease research, HSP70 is of particular interest due to its ability to counteract protein misfolding and aggregation—hallmarks of disorders like Alzheimer’s, Parkinson’s, and Huntington’s disease. By stabilizing toxic intermediates and promoting their clearance, HSP70 enhances neuronal survival and resilience under proteotoxic stress. This antibody is also available conjugated to ATTO 390, ATTO 488, ATTO 594, APC, Biotin, FITC, HRP, PerCP and RPE. Supplied in 100 µg. For research use only; not for diagnostic or therapeutic procedures.

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