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| Alternative Names | HSPA1A, HSPA1B, HSPA1, HSP70, HSP70-1, HSP70.1, HSP70-2, HSP72, HSP73, HSX70, Heat shock 70 kDa protein 1A, Heat shock 70 kDa protein 1B |
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Background
HSP70 is provided as a recombinant protein reagent for research use only. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.
Protein identity context: HSP70 (source species: Human; native localization: Cytoplasm).
Human Recombinant HSP70 Protein
HSP70 is a highly inducible molecular chaperone that plays a pivotal role in protein quality control across all major cellular compartments. In the brain, HSP70 is essential for preventing the aggregation of misfolded proteins, a key pathological feature of neurodegenerative diseases.
Biological significance and function
Mechanistically, HSP70 functions within the cellular proteostasis network, helping client proteins reach and maintain functional conformations under basal and stress conditions. Many clients are signaling proteins (e.g., kinases) whose stability and activity are sensitive to folding state and chaperone availability. This protein is frequently discussed in research themes such as Cancer and Heat Shock.
Molecular characteristics
Molecular characteristics: Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.
- Source species: Human
- Cellular localization (native): Cytoplasm
- Protein size: ~70 kDa
- Purity: >90%
- Expression system: Baculovirus/Sf9
- Purification: Affinity Purified | Endotoxin-free
- Storage buffer: 50mM Tris/HCl, pH 7.5, 0.15M NaCl, 10% glycerol
Post-translational considerations: Insect-cell expression supports eukaryotic folding and some PTMs, which can be beneficial for structurally complex proteins. Glycan patterns may differ from mammalian cells and can influence certain binding-dependent assays. For molecular chaperones, nucleotide-binding state and co-chaperone interactions often shape functional readouts.
Structural and biochemical features
Structural/biochemical context: Many chaperones cycle through nucleotide-bound conformations that regulate client binding and release. Co-chaperones can tune this cycle and change apparent interaction profiles in reconstituted assays.
Expression and purification strategy
Expression system: Baculovirus/Sf9. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.
Purification strategy: Affinity Purified | Endotoxin-free. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.
Research interpretation
Research interpretation: Changes in chaperone abundance or activity can reflect altered proteostasis demand (e.g., heat shock, oxidative stress, proteotoxic challenge) and may shift the stability landscape of client proteins. Interpreting effects often benefits from pairing chaperone measurements with client-protein stability, stress-response transcriptional markers, and aggregation/solubility readouts.
Certificate of Analysis: This product has been certified >90% pure using SDS-PAGE analysis. The protein tested positive for ATPase activity using a Malachite Green assay.
Tariff Code: 3822.19.0030
UNSPSC Code: 12352202
ADR Code: Non-hazardous
UN Code for transport: Non-hazardous
Cite this Product: Human Recombinant HSP70 Protein (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-115A)
Human Recombinant HSP70 Protein (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-115B)
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Can I request a custom size, tag variant, or formulation?
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.
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