H90-10

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$40.00
SKU: H90-10
View product citations for antibody H90-10 on CiteAb

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DSHB Data Sheet
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Catalog Fields

Antigen: Heat Shock Protein 90 beta
Hybridoma Cells Available: Yes
Antigen Species: Human
Depositor: Freeman, Brian
Isotype: MIgG2a
Antigen Sequence:
Host Species: mouse
Depositors Institution: University of Illinois-Urbana-Champaign
Positive Tested Species Reactivity: Canine, Chicken, Human, Mouse, Rabbit, Rat
Depositors Notes:
Antigen Molecular Weight: 83.3 kDa
Human Protein Atlas:  
Predicted Species Reactivity:  
Gene: HSP90AB1
Immunogen: Recombinant human HSP90beta
Alternate Gene Names: HSPC2, HSPCB
Alternate Antibody Name:
Clonality: Monoclonal
Alternate Antigen Name:
Epitope Mapped: Yes
Myeloma Strain: P3NS-11-AG4-1 (NS-1)
Epitope Location or Sequence:
Uniprot ID: P08238 
Immunogen Sequence: Full length protein
Entrez Gene ID: 3326 
Additional Characterization:  
Antibody Registry ID:  
Additional Information:
Recommended Applications: ELISA, Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blot
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These hybridomas were created by your colleagues. Please acknowledge the hybridoma contributor and the Developmental Studies Hybridoma Bank (DSHB) in the Materials and Methods of your publications. Please email the citation to us.
For your Materials & Methods section:
H90-10 was deposited to the DSHB by Freeman, Brian (DSHB Hybridoma Product H90-10)
Storage and Handling Recommendations
Although many cell products are maintained at 4°C for years without loss of activity, shelf-life at 4°C is highly variable. For immediate use, short term storage at 4°C up to two weeks is recommended. For long term storage, divide the solution into volumes of no less than 20 ul for freezing at -20°C or -80°C. The small volume aliquot should provide sufficient reagent for short term use. Freeze-thaw cycles should be avoided. For concentrate or bioreactor products, an equal volume of glycerol, a cryoprotectant, may be added prior to freezing.
Usage Recommendations
Although the optimal Ig concentration for an application varies for each product and must be optimized for each laboratory, a good starting concentration for immunohistochemistry (IHC), immunofluorescence (IF), and immunocytochemistry (ICC) is 2-5 ug/ml. For western blots, the recommended concentration range is 0.2-0.5 ug/ml.
All cell products contain the antimicrobial ProClin. Click here for additional information.

16 References

  • Initial Publication
  • IF References
  • WB References
  • IP References
  • ELISA References
  • Epitope Map References
  • All References
    • Initial Publication

    Immunological evidence that the nonhormone binding component of avian steroid receptors exists in a wide range of tissues and species.
    Toft DO
    Biochemistry 24.23 (1985 Nov 5): 6586-91.

    IF References

    Immunofluorescence colocalization of the 90-kDa heat-shock protein and microtubules in interphase and mitotic mammalian cells.
    Welsh MJ
    European journal of cell biology 50.1 (1989 Oct): 66-75.

    WB References

    Immunological evidence that the nonhormone binding component of avian steroid receptors exists in a wide range of tissues and species.
    Toft DO
    Biochemistry 24.23 (1985 Nov 5): 6586-91.

    A 90,000-dalton binding protein common to both steroid receptors and the Rous sarcoma virus transforming protein, pp60v-src.
    Toft DO
    The Journal of biological chemistry 260.26 (1985 Nov 15): 14292-6.

    Loss of proliferative potential during terminal differentiation coincides with the decreased abundance of a subset of heterogeneous ribonuclear proteins.
    Scott RE
    The Journal of cell biology 109.5 (1989 Nov): 1937-46.

    Relationship of the 90-kDa murine heat shock protein to the untransformed and transformed states of the L cell glucocorticoid receptor.
    Pratt WB
    The Journal of biological chemistry 262.15 (1987 May 25): 6986-91.

    Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein.
    Pratt WB
    The Journal of biological chemistry 260.23 (1985 Oct 15): 12398-401.

    A 90,000-dalton binding protein common to both steroid receptors and the Rous sarcoma virus transforming protein, pp60v-src.
    Toft DO
    The Journal of biological chemistry 260.26 (1985 Nov 15): 14292-6.

    Reconstitution of progesterone receptor with heat shock proteins.
    Toft DO
    Molecular endocrinology (Baltimore, Md.) 4.11 (1990 Nov): 1704-11.

    Identification of the 90 kDa substrate of rat liver type II casein kinase with the heat shock protein which binds steroid receptors.
    Toft DO
    Biochimica et biophysica acta 927.1 (1987 Jan 19): 74-80.

    FKBP51 promotes assembly of the Hsp90 chaperone complex and regulates androgen receptor signaling in prostate cancer cells.
    Paschal BM
    Molecular and cellular biology 30.5 (2010 Mar): 1243-53.

    Intracellular dynamics of the Hsp90 co-chaperone p23 is dictated by Hsp90.
    Picard D
    Experimental cell research 312.2 (2006 Jan 15): 198-204.

    The Hsp90-binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo.
    Smith DF
    The EMBO journal 22.5 (2003 Mar 3): 1158-67.

    IP References

    A 90,000-dalton binding protein common to both steroid receptors and the Rous sarcoma virus transforming protein, pp60v-src.
    Toft DO
    The Journal of biological chemistry 260.26 (1985 Nov 15): 14292-6.

    Immunological evidence that the nonhormone binding component of avian steroid receptors exists in a wide range of tissues and species.
    Toft DO
    Biochemistry 24.23 (1985 Nov 5): 6586-91.

    Relationship of the 90-kDa murine heat shock protein to the untransformed and transformed states of the L cell glucocorticoid receptor.
    Pratt WB
    The Journal of biological chemistry 262.15 (1987 May 25): 6986-91.

    Reconstitution of progesterone receptor with heat shock proteins.
    Toft DO
    Molecular endocrinology (Baltimore, Md.) 4.11 (1990 Nov): 1704-11.

    Mutational analysis of hsp90 binding to the progesterone receptor.
    Toft DO
    The Journal of biological chemistry 268.27 (1993 Sep 25): 20373-9.

    Analysis of FKBP51/FKBP52 chimeras and mutants for Hsp90 binding and association with progesterone receptor complexes.
    Smith DF
    Molecular endocrinology (Baltimore, Md.) 12.3 (1998 Mar): 342-54.

    The biochemical role of the heat shock protein 90 chaperone complex in establishing human telomerase activity.
    Jarstfer MB
    The Journal of biological chemistry 281.29 (2006 Jul 21): 19840-8.

    Intracellular dynamics of the Hsp90 co-chaperone p23 is dictated by Hsp90.
    Picard D
    Experimental cell research 312.2 (2006 Jan 15): 198-204.

    The Hsp90-binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo.
    Smith DF
    The EMBO journal 22.5 (2003 Mar 3): 1158-67.

    A Remodeled Hsp90 Molecular Chaperone Ensemble with the Novel Cochaperone Aarsd1 Is Required for Muscle Differentiation.
    Picard D
    Molecular and cellular biology 36.8 (2016 Apr): 1310-21.

    Multiple domains of the co-chaperone Hop are important for Hsp70 binding.
    Smith DF
    The Journal of biological chemistry 279.16 (2004 Apr 16): 16185-93.

    ELISA References

    Identification of the 90 kDa substrate of rat liver type II casein kinase with the heat shock protein which binds steroid receptors.
    Toft DO
    Biochimica et biophysica acta 927.1 (1987 Jan 19): 74-80.

    Epitope Map References

    Mutational analysis of hsp90 binding to the progesterone receptor.
    Toft DO
    The Journal of biological chemistry 268.27 (1993 Sep 25): 20373-9.

    All References

    Immunofluorescence colocalization of the 90-kDa heat-shock protein and microtubules in interphase and mitotic mammalian cells.
    Welsh MJ
    European journal of cell biology 50.1 (1989 Oct): 66-75.

    Immunological evidence that the nonhormone binding component of avian steroid receptors exists in a wide range of tissues and species.
    Toft DO
    Biochemistry 24.23 (1985 Nov 5): 6586-91.

    A 90,000-dalton binding protein common to both steroid receptors and the Rous sarcoma virus transforming protein, pp60v-src.
    Toft DO
    The Journal of biological chemistry 260.26 (1985 Nov 15): 14292-6.

    Loss of proliferative potential during terminal differentiation coincides with the decreased abundance of a subset of heterogeneous ribonuclear proteins.
    Scott RE
    The Journal of cell biology 109.5 (1989 Nov): 1937-46.

    Relationship of the 90-kDa murine heat shock protein to the untransformed and transformed states of the L cell glucocorticoid receptor.
    Pratt WB
    The Journal of biological chemistry 262.15 (1987 May 25): 6986-91.

    Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein.
    Pratt WB
    The Journal of biological chemistry 260.23 (1985 Oct 15): 12398-401.

    Reconstitution of progesterone receptor with heat shock proteins.
    Toft DO
    Molecular endocrinology (Baltimore, Md.) 4.11 (1990 Nov): 1704-11.

    Identification of the 90 kDa substrate of rat liver type II casein kinase with the heat shock protein which binds steroid receptors.
    Toft DO
    Biochimica et biophysica acta 927.1 (1987 Jan 19): 74-80.

    FKBP51 promotes assembly of the Hsp90 chaperone complex and regulates androgen receptor signaling in prostate cancer cells.
    Paschal BM
    Molecular and cellular biology 30.5 (2010 Mar): 1243-53.

    Intracellular dynamics of the Hsp90 co-chaperone p23 is dictated by Hsp90.
    Picard D
    Experimental cell research 312.2 (2006 Jan 15): 198-204.

    The Hsp90-binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo.
    Smith DF
    The EMBO journal 22.5 (2003 Mar 3): 1158-67.

    Mutational analysis of hsp90 binding to the progesterone receptor.
    Toft DO
    The Journal of biological chemistry 268.27 (1993 Sep 25): 20373-9.

    Analysis of FKBP51/FKBP52 chimeras and mutants for Hsp90 binding and association with progesterone receptor complexes.
    Smith DF
    Molecular endocrinology (Baltimore, Md.) 12.3 (1998 Mar): 342-54.

    The biochemical role of the heat shock protein 90 chaperone complex in establishing human telomerase activity.
    Jarstfer MB
    The Journal of biological chemistry 281.29 (2006 Jul 21): 19840-8.

    A Remodeled Hsp90 Molecular Chaperone Ensemble with the Novel Cochaperone Aarsd1 Is Required for Muscle Differentiation.
    Picard D
    Molecular and cellular biology 36.8 (2016 Apr): 1310-21.

    Multiple domains of the co-chaperone Hop are important for Hsp70 binding.
    Smith DF
    The Journal of biological chemistry 279.16 (2004 Apr 16): 16185-93.

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