HSP70 (78kD Glucose-regulated Protein, GRP 78, Heat Shock 70kD Protein 5, Immunoglobulin Heavy Chain-binding Protein, BiP, Endoplasmic Reticulum Lumenal Ca(2+)-binding Protein grp78, HSPA5, GRP78) (Biotin)

In cooperation with other chaperones, HSP70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. The HSP70s in mitochondria and the endoplasmic reticulum play an additional role by providing a driving force for protein translocation. They are involved in signal transduction pathways in cooperation with HSP90. They participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. \n\nApplications: \nSuitable for use in ELISA, Western Blot, and Immunohistochemistry. Other applications not tested.\n\nRecommended Dilution:\nELISA: 1:1000\nWestern Blot: 1:100-1:500\nImmunohistochemistry: 1:50-1:100\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for at least 6 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

H1830-97D-Biotin

Size

200ul

Applications

ELISA, IHC, WB

Hosts

Rabbit

Reactivities

Hum, Mouse

Conjugates

Biotin

Form

Supplied as a liquid in PBS, pH 7.2. Contains ~0.09% sodium azide. Conjugated to Biotin.

P Type

Pab

Purity

Purified by Protein G affinity chromatography.

Isotype

IgG

References

1. Strausberg, R.L., et al., Proc. Natl. Acad. Sci. USA 99(26):16899-16903 (2002). 2. Milner, C.M., et al., Immunogenetics 32(4):242-251 (1990). 3. Sargent, C.A., et al., Proc. Natl. Acad. Sci. USA 86(6):1968-1972 (1989). 4. Drabent, B., et al., Nucleic Acids Res. 14(22):8933-8948 (1986). 5. Hunt, C., et al., Proc. Natl. Acad. Sci. USA 82(19):6455-6459 (1985). 6. Nicholas J. Buchkovich, et al. J. Virol. published 9 September 2009, 10.1128/JVI.00762-09. (E-pub)

Additional Info

Recognizes human HSP70. Species Crossreactivity: mouse.