New Products from StressMarq
StressMarq have released 5 new antisera:
- 2 Mouse monoclonal against Aha1, clones 25F2-D9 and clones25F2-D10
- Mouse monoclonal anti-phosphotyrosine, clone G104
- Rabbit polyclonal against HSPB2, also known as MKBP
- Rabbit polyclonal against Hsp110
Aha1
Aha1 is a member of the Hsp90 cochaperone family, and is thought to stimulate Hsp90 ATPase activity by competing with p23 and other co-chaperones for Hsp90 binding. It may affect a step in the endoplasmic reticulum to Golgi trafficking. Aha1 also interacts with HSPCA/Hsp90 and with the cytoplasmic tail of the vesicular stomatistis virus glycoproteins (VSV G). Aha1 is expressed in numerous tissues, including the brain, heart, skeletal muscle, and kidney, and at low levels, the liver and placenta. Aha1 might be a potential therapeutic strategy to increase sensitivity to HSP inhibitors .
HSPB2, alias MKBP
HSPB2, also known as MKBP is the most divergent member of the sHSP family with only 30% sequence identity to all other mammalian sHSPS. MKBP is known to associate specifically with myotonic dystrophy protein kinase (DMPK) in skeletal muscle. MKBP enhances the kinase activity of DMPK and protects it from heat-induced activation. MKBP also shows a unique nature compared to other sHSps, in that the expression of MKBP is not induced by heat shock. In unstressed skeletal muscle, MKBP forms large oligomeric complexes with HSPB3 in the cytosol which are localized on
mitochondria and the neuromuscular junction. During stress, these complexes dissolve and MKBP’s localization to mitochondria increases, leading to increased cell survival. Pinz et al. tried to find a distinct role for MKBP in terms of cardiac mechanics and finds that it is required for normal systolic performance and normal cardiac energetic. HSPB2 has also been found to be expressed in several cancer cell lines, including human breast cancer, suggesting that MKBP may be an important factor in tumor transformation and metastasis.
Hsp110
Hsp110 belongs to a family of large stress proteins known as the Hsp110/SSE Family. The proteins in this family are the most distantly known relatives of the well studied Hsp70 family. They share 30-33% amino acid identity, mostly in the conserved ATP-binding domain. Hsp110 cooperates with Hsp70 in protein folding in the eukaryotic cytosol. In mammals, Hsp110 is constitutively expressed, but exhibits particularly high levels in the brain. Both Hsp70 and Hsp110 are elevated after cerebral ischemia. Recent studies demonstrate that the protective effects of Hsp110 deficiency in cerebral ischemia may partly be mediated by an increase in the chaperone activity of Hsp70. Studies also suggest that Hsp110 can be used in heat shock protein-based cancer immunotherapy.
