Anti-Hsp70 HSPA1A Antibody Picoband® (monoclonal, 3H5)

Overview

This antibody is intended for detection of HSPA1A (CD59 molecule, complement regulatory protein) in biological samples using common immunoassay formats. It is typically selected based on target identity, species reactivity, clonality/clone information, and detection modality.

Vendor notes: Boster Bio Anti-Hsp70 HSPA1A Antibody Picoband® (monoclonal, 3H5) catalog # M00949-2. Tested in Flow Cytometry, IF, IHC, ICC, WB applications. This antibody reacts with Human. The brand Picoband indicates this is a premium antibody that guarantees superior quality, high affinity, and strong signals with minimal background in Western blot applications. Only our best-performing antibodies are designated as Picoband, ensuring unmatched performance.

Key elements and design rationale

• Antibody format: Mouse Monoclonal Mouse IgG1
• Clone number: Clone: 3H5
• Immunogen / epitope context: A synthetic peptide corresponding to a sequence at the C-terminus of human Hsp70, different from the related mouse sequence by five amino acids, and from the related rat sequence by three amino acids.
• Molecular weight context: reported MW: 70 kDa; calculated MW: nan
• Reactivity: Human
• Applications: Flow Cytometry, IF, IHC, ICC, WB

As a monoclonal antibody, the reagent targets a defined epitope, supporting consistency across experiments; epitope masking by PTMs or conformational changes can affect signal.

Biological background

CD59 molecule, complement regulatory protein; heat shock protein family A (Hsp70) member 1A/1B. HSPA1 (heat shock 70kDa protein 1A) also known as HSP70-1, HSPA1A, HSP70-1A, HSP72 or HSP70I, is a protein that in humans is encoded by the HSPA1A gene. This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 family. The HSPA1A gene encodes a predicted 641-amino acid protein. The HSPA1 gene is mapped on 6p21.33. Shimizu et al. (1999) found that peripheral blood mononuclear cells of 18 major depression patients expressed a short HSPA1A transcript that utilized exon 1 rather than exon 2, which is found in the more common HSPA1A transcript. No protein was associated with expression of this short HSPA1A mRNA, possibly due to lack of a TATA box or loss of internal ribosome binding sites. Treatment with BGP-15, a pharmacologic inducer of Hsp72 that can protect against obesity-induced insulin resistance, improved muscular architecture, strength, and contractile function in severely affected diaphragm muscles in mdx dystrophic mice. Functional note: 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:26865365, PubMed:24318877). 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). Negatively regulates heat shock- induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401). Reported localization: Cytoplasm Expression/tissue context: Ubiquitous.

Research relevance and current trends

• Cancer: Researchers commonly examine how HSPA1A (CD59 molecule, complement regulatory protein) relates to this theme using model systems and orthogonal readouts.
• Chaperones: Researchers commonly examine how HSPA1A (CD59 molecule, complement regulatory protein) relates to this theme using model systems and orthogonal readouts.
• Heat Shock Proteins: Researchers commonly examine how HSPA1A (CD59 molecule, complement regulatory protein) relates to this theme using model systems and orthogonal readouts.

Common research applications

• Western blotting: compare relative HSPA1A (CD59 molecule, complement regulatory protein) levels across conditions; band patterns may reflect isoforms and processing.
• IHC/IHC-F: assess spatial distribution of HSPA1A (CD59 molecule, complement regulatory protein) across tissue regions and cell types using matched controls.
• IF/ICC: evaluate subcellular localization and co-localization patterns; signal can depend on fixation/permeabilization and epitope accessibility.
• Flow cytometry: quantify target-positive populations and shifts in expression; gating strategy and background staining controls are essential.

Notes for experimental interpretation

• Specificity notes: No cross reactivity with other proteins.
• Cross-reactivity: No cross-reactivity with other proteins.
• Isoforms and PTMs: Apparent size and signal patterns can differ across splice isoforms, proteolytic processing, and post-translational modifications.
• Controls: Include an isotype control (as relevant), no-primary control for imaging, and orthogonal validation such as KD/KO samples when available.

Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.