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HSPB1 Matched Antibody Pair (577) (APMAB-577LY)


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Specifications

ApplIcation
Sandwich ELISA
Specificity
Human
Capture Antibody
Mouse anti-HSPB1 monoclonal antibody, 100 ug
Detection Antibody
Anti-HSPB1 Rabbit polyclonal antibody, 50 ug
Dilutions
10 ng/ml-100 ng/ml
Format
Liquid
Storage
Aliquot and store at -20°Cor -80°C. Avoid freeze-thaw cycles.
Introduction
This gene encodes a member of the small heat shock protein (HSP20) family of proteins. In response to environmental stress, the encoded protein translocates from the cytoplasm to the nucleus and functions as a molecular chaperone that promotes the correct folding of other proteins. This protein plays an important role in the differentiation of a wide variety of cell types. Expression of this gene is correlated with poor clinical outcome in multiple human cancers, and the encoded protein may promote cancer cell proliferation and metastasis, while protecting cancer cells from apoptosis. Mutations in this gene have been identified in human patients with Charcot-Marie-Tooth disease and distal hereditary motor neuropathy. [provided by RefSeq, Aug 2017]
Alternative Names
CMT2F; HMN2B; HSP27; HSP28; Hsp25; SRP27; HS.76067; HEL-S-102
Entrez Gene ID
3315
UniProt ID
P04792
More Infomation

Wang, L., Wu, S., He, H., Ai, K., Xu, R., Zhang, L., & Zhu, X. (2022). CircRNA-ST6GALNAC6 increases the sensitivity of bladder cancer cells to erastin-induced ferroptosis by regulating the HSPB1/P38 axis. Laboratory Investigation, 102(12), 1323-1334.

Lu, S., Hu, J., Arogundade, O. A., Goginashvili, A., Vazquez-Sanchez, S., Diedrich, J. K., ... & Cleveland, D. W. (2022). Heat-shock chaperone HSPB1 regulates cytoplasmic TDP-43 phase separation and liquid-to-gel transition. Nature cell biology, 24(9), 1378-1393.

Alexander, C. C., Munkáscy, E., Tillmon, H., Fraker, T., Scheirer, J., Holstein, D., ... & Rodriguez, K. A. (2022). HspB1 overexpression improves life span and stress resistance in an invertebrate model. The Journals of Gerontology: Series A, 77(2), 268-275.

Liu, X., Xiao, W., Jiang, Y., Zou, L., Chen, F., Xiao, W., ... & Zhu, Y. (2021). Bmal1 regulates the redox rhythm of HSPB1, and homooxidized HSPB1 attenuates the oxidative stress injury of cardiomyocytes. Oxidative Medicine and Cellular Longevity, 2021, 1-16.

Gonçalves, C. C., Sharon, I., Schmeing, T. M., Ramos, C. H., & Young, J. C. (2021). The chaperone HSPB1 prepares protein aggregates for resolubilization by HSP70. Scientific reports, 11(1), 17139.

Muranova, L. K., Sudnitsyna, M. V., Strelkov, S. V., & Gusev, N. B. (2020). Mutations in HspB1 and hereditary neuropathies. Cell Stress and Chaperones, 25, 655-665.

Baughman, H. E., Pham, T. H. T., Adams, C. S., Nath, A., & Klevit, R. E. (2020). Release of a disordered domain enhances HspB1 chaperone activity toward tau. Proceedings of the National Academy of Sciences, 117(6), 2923-2929.

Haidar, M., Asselbergh, B., Adriaenssens, E., De Winter, V., Timmermans, J. P., Auer-Grumbach, M., ... & Timmerman, V. (2019). Neuropathy-causing mutations in HSPB1 impair autophagy by disturbing the formation of SQSTM1/p62 bodies. Autophagy, 15(6), 1051-1068.

Wang, Y., Liu, J., Kong, Q., Cheng, H., Tu, F., Yu, P., ... & Liu, L. (2019). Cardiomyocyte-specific deficiency of HSPB1 worsens cardiac dysfunction by activating NFκB-mediated leucocyte recruitment after myocardial infarction. Cardiovascular research, 115(1), 154-167.

Baughman, H. E., Clouser, A. F., Klevit, R. E., & Nath, A. (2018). HspB1 and Hsc70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation. Journal of Biological Chemistry, 293(8), 2687-2700.

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For research use only. Not intended for any clinical use.

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