Recombinant Rat Heat shock protein HSP 90-beta (Hsp90ab1)
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Description
Production and Purity
Recombinant rat Hsp90ab1 is typically expressed in yeast or baculovirus systems with affinity tags (e.g., His tag) for purification . Key quality metrics include:
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Purity: >90% as verified by SDS-PAGE and Coomassie staining .
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Activity: ATPase functionality confirmed via enzymatic assays .
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Applications: Used in ELISA, Western blot (WB), and immunoprecipitation (IP) .
Chaperone Mechanism
Hsp90ab1 operates as a dimer, binding client proteins like kinases (e.g., c-Raf) and transcription factors (e.g., p53) in an ATP-dependent cycle. Key co-chaperones include Cdc37 and p23, which regulate client loading and ATPase activity .
Disease Relevance
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Cancer: Upregulated in prostate and laryngeal cancers, where it stabilizes oncoproteins like BIRC2 to inhibit apoptosis .
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Neurodegeneration: Modulates tau aggregation and α-synuclein toxicity in rat models .
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Inflammation: Facilitates IL-1β secretion via TMED10-mediated ERGIC translocation .
Research Tools and Validation
| Reagent | Host | Applications | Specificity Data |
|---|---|---|---|
| Anti-Hsp90ab1 (11405-1-AP) | Rabbit IgG | WB, IHC, IP | KO validation in A431 cells |
| Recombinant Hsp90ab1 | Yeast | ELISA, activity assays | >90% purity |
Evolutionary Conservation
Hsp90ab1 shares >90% sequence identity across mammals, enabling cross-species studies. For example:
| Species | Sequence Identity (vs. Rat) | Molecular Weight (kDa) |
|---|---|---|
| Human | 98% | 83.3 |
| Mouse | 99% | 83.3 |
| Rat | 100% | 83.2 |
Key Challenges
Product Specs
Form
Lyophilized powder. We will ship the format we have in stock. If you have special format requirements, please note them when ordering.
Lead Time
Delivery times vary by purchase method and location. Consult your local distributor for specific delivery times. Proteins are shipped with blue ice packs by default. Request dry ice in advance (extra fees apply).
Notes
Avoid repeated freeze-thaw cycles. Store working aliquots at 4°C for up to one week.
Reconstitution
Briefly centrifuge the vial before opening. Reconstitute protein in sterile deionized water to 0.1-1.0 mg/mL. Add 5-50% glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final glycerol concentration is 50%.
Shelf Life
Shelf life depends on storage conditions, buffer, temperature, and protein stability. Liquid form: 6 months at -20°C/-80°C. Lyophilized form: 12 months at -20°C/-80°C.
Storage Condition
Store at -20°C/-80°C upon receipt. Aliquot for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
Tag type is determined during manufacturing. If you have a specific tag type requirement, please inform us and we will prioritize its development.
Synonyms
Hsp90ab1; Hsp84; Hspcb; Heat shock protein HSP 90-beta; Heat shock 84 kDa; HSP 84; HSP84
Buffer Before Lyophilization
Tris/PBS-based buffer, 6%
Trehalose.
Datasheet
Please contact us to get it.
Expression Region
2-724
Protein Length
Full Length of Mature Protein
Purity
>85% (SDS-PAGE)
Species
Rattus norvegicus (Rat)
Target Names
Target Protein Sequence
PEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA LDKIRYESLT
DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLIN NLGTIAKSGT KAFMEALQAG
ADISMIGQFG VGFYSAYLVA EKVVVITKHN DDEQYAWESS AGGSFTVRAD HGEPIGRGTK
VILHLKEDQT EYLEERRVKE VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE
DKEDEEKPKI EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE
YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK NNIKLYVRRV
FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI LKVIRKNIVK KCLELFSELA
EDKENYKKFY EAFSKNLKLG IHEDSTNRRR LSELLRYHTS QSGDEMTSLS EYVSRMKETQ
KSIYYITGES KEQVANSAFV ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG
LELPEDEEEK KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA
NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA VKDLVVLLFE
TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVTAEEP SAAVPDEIPP LEGDEDASRM
EEVD
Uniprot No.
Target Background
Function
HSP90-beta is a molecular chaperone crucial for the maturation, maintenance, and regulation of target proteins involved in cell cycle control and signal transduction. Its ATPase activity drives a functional cycle, inducing conformational changes in client proteins for activation. HSP90 interacts with co-chaperones that influence substrate recognition and chaperone function. It participates in various cellular processes, including transcriptional regulation by affecting transcription factor levels, epigenetic modifiers, and histone eviction. HSP90-beta also antagonizes STUB1-mediated TGF-beta inhibition, promotes cell differentiation by protecting BIRC2 from degradation, and chaperones JAK2 and PRKCE for STAT1 activation. It is also involved in the ERGIC translocation of leaderless cargo proteins.
Gene References Into Functions
1. Hsp90beta inhibition destabilized upstream mediators in pathogenic signaling, ameliorating nephropathy due to renal hypoxia and oxidative stress. (PMID: 27248656)
2. Hindlimb suspension and spaceflight inhibited HSP27, HSP70, and HSP84 mRNA expression in soleus muscle, but not in plantaris muscle. (PMID: 18845059)
3. Hsp90 beta significantly reduced NO2/NO3 and increased O2- generation. (PMID: 21063103)
4. Bcl-2's antiapoptotic activity was significantly affected by Hsp90beta knockout via RNA interference. (PMID: 16166581)
5. Morphine differentially regulates hsp90beta expression in the nucleus accumbens of Lewis and Fischer 344 rats. (PMID: 17562399)
6. Geldanamycin regulates hsp90alpha and hsp90beta transactivation in rat gliosarcoma 9L cells through transcription elements, including heat-shock elements and TATA boxes. (PMID: 18320580) [Show More/Hide All functionality implied]
Database Links
Protein Families
Heat shock protein 90 family
Subcellular Location
Cytoplasm. Melanosome. Nucleus. Secreted. Cell membrane. Dynein axonemal particle.
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