- Tel: 858.663.9055
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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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HDJ2 Antibody recognizes DNAJA1, a molecular co-chaperone belonging to the HSP40/DnaJ family of heat shock proteins. Also known as HDJ2, HSDJ, DJA1, and HSPF4, DNAJA1 works closely with HSP70 proteins to regulate protein folding, stabilization, and degradation. Molecular chaperones maintain protein homeostasis, particularly during cellular stress when proteins become susceptible to misfolding or aggregation. DNAJA1 directs HSP70 activity toward specific client proteins and supports the maintenance of functional protein structures.
The human DNAJA1 gene is located on chromosome 9 and encodes a protein of approximately 397 amino acids with a calculated molecular weight near 45 kDa. DNAJA1 contains an N-terminal J domain with a conserved HPD motif that stimulates HSP70 ATPase activity. Additional regions include a glycine/phenylalanine-rich segment, a zinc finger-like domain involved in substrate interactions, and a C-terminal region that contributes to client protein binding and dimerization. These structural features enable DNAJA1 to recognize unfolded proteins and coordinate their transfer to HSP70.
DNAJA1 participates in cellular responses to heat shock, oxidative stress, and other conditions that disrupt protein stability. By stimulating HSP70 ATP hydrolysis, it promotes interactions between HSP70 and its substrates. DNAJA1 also contributes to protein quality control by helping determine whether damaged proteins undergo refolding or degradation. The DNAJA1 Polyclonal Antibody is relevant to research investigating these chaperone-dependent mechanisms and cellular adaptation to stress.
Beyond protein folding, DNAJA1 influences the stability of regulatory proteins involved in cell proliferation, survival, and signaling. Its interactions with HSP70 and other components of the proteostasis network have attracted interest in cancer biology, neurodegenerative disorders, and diseases characterized by protein aggregation. DNAJA1 has also been implicated in the regulation of certain oncogenic proteins, making it relevant to studies of tumor cell survival and therapeutic resistance.
DNAJA1 is closely related to other HSP40 family members, including DNAJA2 and DNAJA3, but these proteins differ in cellular localization, client specificity, and biological functions. Distinguishing individual co-chaperones is important when investigating stress responses and protein quality control. NSJ Bioreagents offers antibodies targeting DNAJA1 for research into molecular chaperone function. An HDJ2 Antibody provides a tool for examining DNAJA1 expression and its involvement in HSP70-mediated protein folding, cellular stress responses, and protein homeostasis.
Explore our Autophagy Antibodies collection for additional antibodies targeting cellular protein quality control, degradation pathways, and mechanisms involved in maintaining protein homeostasis.
The stated application concentrations are suggested starting amounts. Titration of the HDJ2 Antibody / DNAJA1 Polyclonal Antibody may be required due to differences in protocols and secondary/substrate sensitivity.
An amino acid sequence from the C-terminus of human HDJ2 (NQERRRHYNGEAYEDD) was used as the immunogen for this HDJ2 antibody (100% homologous in human, mouse and rat).
After reconstitution, the HDJ2 antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
DNAJA1 antibody, HSP40 antibody, DnaJ Homolog Subfamily A Member 1 antibody, Heat Shock Protein 40 antibody, HSP40 Family Member A1 antibody, DnaJ Protein Homolog 1 antibody
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