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HSP40 Antibody: Biotin

Rabbit Anti-Human HSP40 Polyclonal

Product Specifications

Background

DnaJ/HSP40 proteins have been preserved throughout evolution and are important for protein translation, folding, unfolding, translocation, and degradation, primarily by stimulating the ATPase activity of chaperone proteins, HSP70s. Because the ATP hydrolysis is essential for the activity of HSP70s, DnaJ/HSP40 proteins actually determine the activity of HSP70s by stabilizing their interaction with substrate proteins. DnaJ/HSP40 proteins all contain the J domain through which they bind to HSP70s. HSP40, also known as HDJ1 (6), is a basic mammalian 40kDa heat shock protein which is not only homologous to the bacterial heat shock protein (DnaJ), but also yeast DnaJ-related proteins such as SCJ1, Sec63/Npl1, YDJ1 and SIS1 (2-5). HSP 40 is inducible by stress including heat after which is moves from the cytoplasm to the nucleus and nucleoli; an intracellular pattern similar to HSC70/HSP70, the mammalian homologues of the bacterial heat shock protein, DnaK (2).

Specifications

Detects ~40kDa.

Product Name Alternative

Cancer, Heat Shock, Cell Signaling, Protein Trafficking, Chaperone Proteins

UNSPSC

12352203

Gene ID

3337

Swiss Prot

P25685

Accession Number

NP_006136.1

Cellular Locus

Cytoplasm | Nucleus

Host

Rabbit

Species Reactivity

Human

Immunogen

Recombinant purified full-length human HSP40 (no tags)

Target

HSP40

Clonality

Polyclonal

Conjugation

Biotin

Validated Applications

WB,IHC,ICC/IF |ELISA

Purification

Rabbit Antiserum

Dilution

WB (1:2000), ICC/IF (1:100); optimal dilutions for assays should be determined by the user.

Weight

0.1

Buffer

136.36mM Ethanolamine, and 9.55mM Sodium Bicarbonate in 95.45% PBS

Precautions

Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.

References & Citations

1. Melville, M. W. et al. (1997) PNAS USA, 94: 97-102. 2. Hattori, H., Liu, Y-C., Tohnai, I., Ueda, M., Kaneda, T., Kobayashi, T., Tanabe, K., and Ohtsuka, K. (1992) Cell Structure and Function 17: 77-86. 3. Ohtsuka, K. Masuda, A., Nakai, A., and Nagata, K. (1990) Biochem. Biophys. Res. Commun. 166: 642-647. 4. Bardwell, J.C.A., Tilly, K., Craig, E., King, J., Zylicz, M. and Georgopoulos, C. (1986) J. Biol. Chem. 261: 1782-1785. 5. Ohku, M., Tamura, F., Nishimura, S., and Uchida, H. (1986) J. Biol. Chem. 261: 1778-1781. 6. Ohtsuka, K. (1993) Biochem. Biophys. Res. Commun. 197: 235-240.

Product Datasheet

https://cdn.gentaur.com/products/400/4412053/datasheet/spc-100d-bi.pdf

Product MSDS

https://cdn.gentaur.com/products/400/4412053/msds/spc-100d-bi.pdf

CAS Number

9007-83-4

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