Recombinant Human His6-HSP40/DNAJB1 Protein, CF Summary
Contains a C-terminal 6-His tag
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||X mg/ml (X μM) in 50 mM HEPES pH 7.5, 100 mM NaCl, 1 mM TCEP|
|Shipping||The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Heat shock protein 40 (HSP40, also known as DNAJB1) is the human homologue of the bacterial DnaJ heat shock protein. Heat shock proteins (HSPs) are a highly conserved family of stress response proteins. HSPs function primarily as molecular chaperones, facilitating the folding of other cellular proteins, preventing protein aggregation, or targeting improperly folded proteins to specific degradative pathways. Heat Shock Proteins are ubiquitously expressed in all organisms, and they are induced in response to various types of environmental stresses like heat, cold, and oxygen deprivation. HSP40 is a stress inducible chaperone that colocalizes with HSP70 and can bind unfolded proteins and prevent protein denaturation and aggregation. The conserved amino terminal J domain can interact with HSP70 and stimulate its ATPase activity. HSP40 and HSP70 are required to target some misfolded proteins to the Ubiquitin E3 ligase CHIP (Stub1) for subsequent ubiquitination. This recombinant human protein contains a C-terminal His6 tag.
- Chien V., et. al. (2010) Biochem J. 432: 113-121
- Hinault M.P., et. al. (2010) J Biol. Chem. 285: 38173-38182
- Minami Y., et. al. (1996) J Biol. Chem. 271: 19617-19624
- Qiu X.B., et. al. (2006) Cell Mol. Life. Sci. 63: 2560-2570
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