In molecular biology, chaperone DnaJ, also known as Hsp40 (heat shock protein 40 kDa), is a molecular chaperone protein. It is expressed in a wide variety of organisms from bacteria to humans. Molecular chaperones are a diverse family of proteins that function to protect proteins from irreversible aggregation during synthesis and in times of cellular stress. The bacterial molecular chaperone DnaK is an enzyme that couples cycles of ATP binding, hydrolysis, and ADP release by an N-terminal ATP-hydrolyzing domain to cycles of sequestration and release of unfolded proteins by a C-terminal substrate binding domain. Dimeric GrpE is the co-chaperone for DnaK, and acts as a nucleotide exchange factor, stimulating the rate of ADP release 5000-fold. DnaK is itself a weak ATPase; ATP hydrolysis by DnaK is stimulated by its interaction with another co-chaperone, DnaJ. Thus the co-chaperones DnaJ and GrpE are capable of tightly regulating the nucleotide-bound and substrate-bound state of DnaK in ways that are necessary for the normal housekeeping functions and stress-related functions of the DnaK molecular chaperone cycle.

DnaJ homolog subfamily B member 1
DnaJ protein homolog 1
Heat shock 40 kDa protein 1 (HSP40; Heat shock protein 40)
Human DnaJ protein 1 (hDj-1)
DNAJB1
DNAJ1, HDJ1, HSPF1

p25685

WB,IHC,IF,ICC,FC

WB 1:5000
IHC 1:200-1:1000
IF 1:100-1:400
ICC 1:100
FC 1:1000

Human,Mouse,Rat,Monkey

Rabbit

Predicted size: 38 kDa

Cytoplasm, Nucleus, nucleolus.

Recombinant Rabbit monoclonal

IgG

Protein A affinity purified.

Liquid

PBS (pH7.4), 0.1% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.

Store at +4°C short term. Store at -20°C long term. Avoid freeze / thaw cycle.