- Tel: 858.663.9055
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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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HSP105 Antibody / HSP70 Co-Chaperone Antibody recognizes heat shock protein 105, a large molecular chaperone encoded by the HSPH1 gene. HSP105 belongs to the HSP110/HSPH family of heat shock proteins and is closely associated with cellular protein quality control and stress responses. Unlike classical HSP70 proteins, HSP105 functions prominently as a co-chaperone and nucleotide exchange factor for HSP70-family proteins, helping regulate the chaperone cycle responsible for maintaining protein folding and proteostasis.
HSP105 interacts with HSP70 and related chaperones to promote the release of ADP from HSP70, facilitating nucleotide exchange and progression through the HSP70 protein-folding cycle. Through this activity, HSP105 contributes to the handling of unfolded and misfolded proteins and helps protect cells against proteotoxic stress. Members of the HSP110 family can also cooperate with HSP70 machinery in protein disaggregation, providing an important mechanism for recovering proteins from stress-induced aggregates and maintaining cellular protein homeostasis.
Expression of HSP105 can increase in response to heat shock and other forms of cellular stress. Its molecular chaperone activity has therefore made HSP105 an important target for studies of stress adaptation, protein folding, protein aggregation and proteostasis. An HSP105 Antibody can be useful for investigating changes in HSPH1 expression under conditions that challenge protein homeostasis and for examining the relationship between HSP105 and the broader HSP70 chaperone network.
HSP105 is also studied in cancer biology, where altered expression of molecular chaperones can support cellular survival under the stressful conditions associated with tumor growth. Elevated HSP105 expression has been reported in multiple malignancies, and research has examined its relationships with tumor cell survival, proliferation, stress resistance and treatment response. These observations have generated interest in HSP105 as a marker of cellular stress adaptation and as a component of chaperone networks involved in cancer-associated proteostasis.
NSJ Bioreagents offers mouse monoclonal HSP105 Antibody clone 3D10 for research into HSPH1 expression and molecular chaperone biology. An HSP70 Co-Chaperone Antibody can support studies of HSP70-associated protein folding, nucleotide exchange, proteostasis, cellular stress responses and cancer biology.
Researchers investigating HSP105 within cellular stress and protein homeostasis pathways can explore our Signal Transduction Antibodies page for additional reagents targeting proteins involved in stress-responsive cellular signaling.
Optimal dilution of the HSP105 Antibody / HSP70 Co-Chaperone Antibody should be determined by the researcher.
A human recombinant protein (amino acids Y653-D858) was used as the immunogen for the HSP105 antibody.
After reconstitution, the HSP105 antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
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