HSP90 (total) Antibody

SKU:BHA11900680
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StressMarq Biosciences Inc.
StressMarq Biosciences Inc.
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    Overview
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    Mouse Anti-Human HSP90 (total) Monoclonal IgG2a
    Target HSP90 (total)
    Clone number 4F3.E8
    Clonality Monoclonal
    Application(s) WB, IHC, ICC/IF, IP, ELISA
    Host Mouse
    Available Options

    Select the variant that best fits your experiment. Availability and lead time may vary by option.

    • Options: Size (2) — 200 ug, 12 ug; Conjugate(s) (10) — Unconjugated, ATTO 390, ATTO 488, ATTO 594, APC, BI, FITC, HRP, PCP, RPE
    • Lead time: options listed as “in stock at manufacturer” typically ship in 2–3 business days; other statuses may take longer.
    • Storage: -20ºC, Conjugated antibodies should be stored according to the product label
    • Shipping: cold-chain shipment (typically with ice packs).
    • Upon receipt: store at the recommended temperature as soon as possible.
    • Sales terms and conditions: Please review prior to ordering.
    Options selector
    Catalog no. Size Conjugate(s)
    SMC-149B 200 ug
    SMC-149S 12 ug
    Field Specification
    Accession Number NP_001017963.2
    Alternative Names HSP90, HSP90AB1, HSP90-beta, HSPCB, HSPC2, Heat shock protein HSP 90-beta, Heat shock 84 kDa protein, HSP84, HSP90B
    Cellular Localization Cytoplasm | Melanosome
    Clonality
    • Monoclonal
    Concentration 1 mg/ml
    Host Mouse
    Immunogen Recombinant Human HSP90 purified from E.coli
    Isotype
    • IgG2a
    Product Type
    • Antibodies
    • Primary Antibodies
    Reactivity
    • Human
    • Mouse
    • Rat
    • Plant
    Shipping Blue Ice or 4ºC
    Storage -20ºC, Conjugated antibodies should be stored according to the product label
    Target HSP90 (total)

    HSP90 is a highly conserved and abundantly expressed molecular chaperone that plays a central role in maintaining protein homeostasis, particularly in the nervous system. Present in all eukaryotic cells, HSP90 exists in two major cytosolic isoforms—HSP90α and HSP90β—which share 85% sequence identity but differ in oligomeric state and regulatory function.

    Despite its classification as a heat shock protein, HSP90 is constitutively expressed at high levels, comprising up to 2% of total cytosolic protein in unstressed cells. It is essential for the folding, maturation, and stabilization of a wide range of client proteins, many of which are involved in neuronal signaling, synaptic plasticity, and stress response. These include kinases (e.g., c-Raf), transcription factors (e.g., p53), and steroid hormone receptors.

    In neurodegenerative diseases such as Alzheimer’s, Parkinson’s, and Huntington’s, HSP90 is implicated in both protective and pathological processes. It stabilizes misfolded proteins and prevents aggregation, but can also shield aberrant proteins from degradation, contributing to disease progression. HSP90’s interaction with co-chaperones like Cdc37 and p23 forms complexes that regulate the fate of client proteins, making it a key node in proteostasis networks.

    Pharmacological inhibition of HSP90—using compounds like geldanamycin—has shown promise in modulating protein quality control pathways and reducing toxic protein accumulation in neurodegenerative models.

    0.5 µg/ml of SMC-149 was sufficient for detection of HSP90alpha in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

    Cite this product varies by variant:

    • SMC-149B — Size: 200 ug: HSP90 (total) Antibody (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-149B, RRID: AB_2233312)
    • SMC-149B-A390 — Size: 200 ug: HSP90 (total) Antibody: ATTO 390 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-149B-A390, RRID: AB_2698381)
    • SMC-149B-A488 — Size: 200 ug: HSP90 (total) Antibody: ATTO 488 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-149B-A488, RRID: AB_2698382)
    • SMC-149B-A594 — Size: 200 ug: HSP90 (total) Antibody: ATTO 594 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-149B-A594, RRID: AB_2698384)
    • SMC-149B-APC — Size: 200 ug: HSP90 (total) Antibody: APC (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-149B-APC, RRID: AB_2698390)
    • SMC-149B-BI — Size: 200 ug: HSP90 (total) Antibody: Biotin (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-149B-BI, RRID: AB_2698391)
    • SMC-149B-FITC — Size: 200 ug: HSP90 (total) Antibody: FITC (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-149B-FITC, RRID: AB_2698392)
    • SMC-149B-HRP — Size: 200 ug: HSP90 (total) Antibody: HRP (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-149B-HRP, RRID: AB_2698393)
    • SMC-149B-PCP — Size: 200 ug: HSP90 (total) Antibody: PerCP (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-149B-PCP, RRID: AB_2698395)
    • SMC-149B-RPE — Size: 200 ug: HSP90 (total) Antibody: RPE (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-149B-RPE, RRID: AB_2698396)
    • SMC-149S — Size: 12 ug: HSP90 (total) Antibody (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-149S, RRID: AB_2233312)

    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.

    1. Nemoto T. et al. (1997) J.Biol Chem. 272: 26179-26187.
    2. Minami, Y, et al. (1991), J.Biol Chem. 266: 10099-10103.
    3. Arlander SJH, et al. (2003) J Biol Chem 278: 52572-52577.
    4. Pearl H, et al. (2001) Adv Protein Chem 59: 157-186.
    5. Neckers L, et al. (2002) Trends Mol Med 8: S55-S61.
    6. Pratt W, Toft D. (2003) Exp Biol Med 228: 111-133.
    7. Pratt W, Toft D. (1997) Endocr Rev 18: 306–360.
    8. Pratt WB. (1998) Proc Soc Exptl Biol Med 217: 420–434.
    9. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91: 8324–8328.
    10. Nemoto, T. (1997) Biochem and Mol. Bio Intl. 42 (5): 881-889.

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