HSP90 beta Protein

SKU:BHP11900004
Overview
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HSP90 beta recombinant protein (Human) for research use. Supplied as a defined reagent (expressed in Baculovirus/Sf9; purity >85%) to support controlled biochemical studies and assay development.
Target HSP90 beta
Species Human
Expression System Baculovirus/Sf9
Conjugate No tag
Purity >85%
Protein Length Full Length
Options selector
Catalog no. Size
SPR-102A 50 ug
SPR-102B 100 ug
Available Options

Select from the available variant options shown for this product. Review lead time and shipping expectations before ordering.

  • Options: Size (100 ug, 50 ug).
  • Lead time: in-stock options typically ship in 2–3 business days.
  • Storage: store at -20°C; cold-chain shipment (typically with dry ice) is expected.
  • Please ensure someone is available to receive and store the shipment promptly.
  • Sales terms and conditions: Please review prior to ordering.
Field Specification
Mfr No SPR-102
Accession Number NP_031381.2
Alternative Names FLJ26984, HSP84, HSP90, HSP90B, HSPC2, HSPCB
Biological Activity ATPase active
Cellular Localization Cytoplasm | Melanosome
Concentration Lot/batch specific. See included datasheet.
Conjugate
  • No tag
Expression System
  • Baculovirus/Sf9
Gene ID 3326
Product Type
  • Proteins & Peptide
  • Recombinant Protein
  • Chaperone & Stress Protein
Protein Length Full Length
Protein Size ~90 kDa
Purity >85%
Shipping Blue Ice or 4ºC
Species Human
Storage -20ºC
Target HSP90 beta

Background

HSP90 beta 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: HSP90 beta (source species: Human; native localization: Cytoplasm | Melanosome).

Human Recombinant HSP90 beta Full Length Protein

HSP90 beta is the constitutively expressed isoform of the HSP90 family and is essential for the maintenance of cellular protein networks. In the nervous system, HSP90 beta supports the folding and maturation of proteins involved in synaptic transmission, cytoskeletal dynamics, and neuronal survival.

Biological significance and function

Mechanistically, HSP90 beta 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 | Melanosome
  • Protein length: Full Length
  • Protein size: ~90 kDa
  • Purity: >85%
  • Expression system: Baculovirus/Sf9
  • Purification: Affinity Purified | Low Endotoxin
  • Storage buffer: 20mM Tris, pH7.5, 175 mM NaCl, 0.1 mM EDTA, 10% glycerol, 1 mM DTT

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 | Low Endotoxin. 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.

Tariff Code: 3822.19.0030

UNSPSC Code: 12352202

ADR Code: Non-hazardous

UN Code for transport: Non-hazardous

Cite this Product: Human Recombinant HSP90 beta Protein (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-102A)
Human Recombinant HSP90 beta Protein (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-102B)

What is the purity of HSP90 beta Protein (Human)?
>85% BioHippo includes a Certificate of Analysis (CoA) confirming purity per lot with every order.
How should HSP90 beta Protein (Human) be stored?
-20ºC Prepare single-use aliquots after reconstitution to avoid repeated freeze–thaw cycles.
What expression system was used to produce this protein?
This recombinant protein was expressed in Baculovirus/Sf9. The system was selected to achieve high yield, correct folding, and appropriate post-translational modifications.
Is this protein biologically active?
ATPase active Refer to the product datasheet for recommended assay conditions and controls.
What are the shipping conditions?
Blue Ice or 4ºC Upon receipt, immediately transfer to recommended storage conditions.
Is this protein approved for clinical or in vitro diagnostic use?
No. Supplied for Research Use Only (RUO) — not intended for therapeutic applications or in vitro diagnostic procedures.
Can I request a custom size, tag variant, or formulation?
Yes. BioHippo can accommodate custom requests including alternative sizes, His/GST/Fc tag variants, bulk quantities, and custom formulations. See the Customization & Add-ons tab or email support@biohippo.com.

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.

1. Arlander S.J.H., et al. (2003) J Biol Chem. 278: 52572-52577.
2. Pearl H., et al. (2001) Adv Protein Chem. 59:157-186.
3. Neckers L., et al. (2002) Trends Mol Med. 8:S55-S61.
4. Pratt W., Toft D. (2003) Exp Biol Med. 228:111-133.
5. Pratt W., Toft D. (1997) Endocr Rev. 18: 306–360.
6. Pratt W.B. (1998) Proc Soc Exptl Biol Med. 217: 420–434.
7. Whitesell L., et al. (1994) Proc Natl Acad Sci USA. 91: 8324– 8328.
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