HSP90B1 Antibody Cat. No.: 61-702

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psi-iconSpecifications
HOST SPECIES:Rabbit
SPECIES REACTIVITY: Hamster, Human, Mouse
HOMOLOGY: Predicted species reactivity based on immunogen sequence: Bovine, Chicken, Monkey, Pig, Rat
IMMUNOGEN: This HSP90B1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 16-43 amino acids from the N-terminal region of human HSP90B1.
TESTED APPLICATIONS: Flow, IF, IHC-P, WB
APPLICATIONS: For WB starting dilution is: 1:1000

For IHC-P starting dilution is: 1:50~100

For FACS starting dilution is: 1:10~50

For IF starting dilution is: 1:10~50
PREDICTED MOLECULAR WEIGHT: 92 kDa

psi-iconProperties
PURIFICATION:This antibody is purified through a protein A column, followed by peptide affinity purification.
CLONALITY:Polyclonal
ISOTYPE:Rabbit Ig
CONJUGATE:Unconjugated
PHYSICAL STATE:Liquid
BUFFER:Supplied in PBS with 0.09% (W/V) sodium azide.
CONCENTRATION:batch dependent
STORAGE CONDITIONS:Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.

psi-iconAdditional Info
OFFICIAL SYMBOL:HSP90B1
ALTERNATE NAMES:Endoplasmin, 94 kDa glucose-regulated protein, GRP-94, Heat shock protein 90 kDa beta member 1, Tumor rejection antigen 1, gp96 homolog, HSP90B1, GRP94, TRA1
ACCESSION NO.:P14625
PROTEIN GI NO.:119360
GENE ID:7184
USER NOTE:Optimal dilutions for each application to be determined by the researcher.
psi-iconBackground and References
BACKGROUND:HSP90B1 is highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90B1 is an endoplasmic reticulum HSP90 protein. Other HSP90 proteins are found in cytosol.
REFERENCES:1) Koo, B.H., et al. J. Biol. Chem. 285(1):197-205(2010) Suriano, R., et al. Glycobiology 19(12):1427-1435(2009) Lev, A., et al. J. Immunol. 183(7):4205-4210(2009)

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