|Other Names||DnaJ homolog subfamily B member 2, DnaJ protein homolog 1, Heat shock 40 kDa protein 3, Heat shock protein J1, HSJ-1, DNAJB2, HSJ1, HSPF3|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Functions as a co-chaperone, regulating the substrate binding and activating the ATPase activity of chaperones of the HSP70/heat shock protein 70 family (PubMed:7957263, PubMed:22219199). In parallel, also contributes to the ubiquitin- dependent proteasomal degradation of misfolded proteins (PubMed:15936278, PubMed:21625540). Thereby, may regulate the aggregation and promote the functional recovery of misfolded proteins like HTT, MC4R, PARK2, RHO and SOD1 and be crucial for many biological processes (PubMed:12754272, PubMed:20889486, PubMed:21719532, PubMed:22396390, PubMed:24023695). Isoform 1 which is localized to the endoplasmic reticulum membranes may specifically function in ER-associated protein degradation of misfolded proteins (PubMed:15936278).|
|Cellular Location||Isoform 2: Cytoplasm Nucleus|
|Tissue Location||More abundantly expressed in neocortex, cerebellum, spinal cord and retina where it is expressed by neuronal cells (at protein level) (PubMed:1599432, PubMed:12754272). Detected at much lower level in non-neuronal tissues including kidney, lung, heart, skeletal muscle, spleen and testis (at protein level) (PubMed:12754272, PubMed:1599432) Isoform 1 is more abundant in neocortex and cerebellum compared to isoform 2 (at protein level) (PubMed:12754272)|
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Provided below are standard protocols that you may find useful for product applications.
DNAJB2 is involved in heat shock protein and unfolded protein binding.
Claeys, K.G., et al. Am. J. Pathol. 176(6):2901-2910(2010)Starr, J.M., et al. Mech. Ageing Dev. 129(12):745-751(2008)Mahoney, D.J., et al. Am. J. Physiol. Regul. Integr. Comp. Physiol. 294 (6), R1901-R1910 (2008) :Adaimy, L., et al. Am. J. Hum. Genet. 81(4):821-828(2007)Sugiyama, N., et al. Mol. Cell Proteomics 6(6):1103-1109(2007)
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