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HSPB1 / HSP27

heat shock 27kDa protein 1

Heat shock protein 27 (Hsp27) also known as heat shock protein beta-1 (HSPB1) is a protein that in humans is encoded by the HSPB1 gene. Hsp27 is a chaperone of the sHsp (small heat shock protein) group among ubiquitin, a-crystallin, Hsp20 and others. The common functions of sHsps are chaperone activity, thermotolerance, inhibition of apoptosis, regulation of cell development, and cell differentiation. They also take part in signal transduction.

Gene Name: heat shock 27kDa protein 1
Synonyms: HSPB1, 28 kDa heat shock protein, Heat shock 27 kDa protein, Heat shock 27kD protein 1, Heat shock 27kDa protein 1, HSP27, HSP28, HSP 27, Hsp25, SRP27, Stress-responsive protein 27, CMT2F, Heat shock 27 kd protein, Heat shock protein beta-1, HMN2B, HS.76067
Target Sequences: NM_001540 NP_001531.1 P04792

Publications (10)

1
Chromosomal assignments of human 27-kDa heat shock protein gene family. McGuire SE, Fuqua SA, Naylor SL, Helin-Davis DA, McGuire WL. Somatic cell and molecular genetics. 1989 15:167-71. [PubMed:2538929] Related Antibodies: LS-B383.
2
Multi-kinase inhibitors can associate with heat shock proteins through their NH2-termini by which they suppress chaperone function. Booth L, Shuch B, Albers T, Roberts JL, Tavallai M, Proniuk S, Zukiwski A, Wang D, Chen CS, Bottaro D, Ecroyd H, Lebedyeva IO, Dent P. Oncotarget. 2016 7:12975-96. (WB; Human) [Full Text Article] [PubMed:26887051] [PMC:PMC4914336] Related Antibodies: LS-C31836.
3
Translocation of molecular chaperones to the titin springs is common in skeletal myopathy patients and affects sarcomere function. Unger A, Beckendorf L, Böhme P, Kley R, von Frieling-Salewsky M, Lochmüller H, Schröder R, Fürst DO, Vorgerd M, Linke WA. Acta neuropathologica communications. 2017 5:72. (WB; Human) [Full Text Article] [PubMed:28915917] [PMC:PMC5603016]
4
A cDNA for the estradiol-regulated 24K protein: control of mRNA levels in MCF-7 cells. Moretti-Rojas I, Fuqua SA, Montgomery RA, McGuire WL. Breast cancer research and treatment. 1988 11:155-63. [PubMed:3401605] Related Antibodies: LS-B383.
5
Estradiol stimulates synthesis of a major intracellular protein in a human breast cancer cell line (MCF-7). Edwards DP, Adams DJ, McGuire WL. Breast cancer research and treatment. 1981 1:209-23. [PubMed:7348573] Related Antibodies: LS-B383.
6
Rationally Repurposing Ruxolitinib (Jakafi (®)) as a Solid Tumor Therapeutic. Tavallai M, Booth L, Roberts JL, Poklepovic A, Dent P. Frontiers in oncology. 2016 6:142. (WB; Human) [Full Text Article] [PubMed:27379204] [PMC:PMC4904019] Related Antibodies: LS-C31836.
7
[Pemetrexed + Sorafenib] lethality is increased by inhibition of ERBB1/2/3-PI3K-NF?B compensatory survival signaling. Booth L, Roberts JL, Tavallai M, Chuckalovcak J, Stringer DK, Koromilas AE, Boone DL, McGuire WP, Poklepovic A, Dent P. Oncotarget. 2016 7:23608-32. (WB; Human) [Full Text Article] [PubMed:27015562] [PMC:PMC5029651] Related Antibodies: LS-C31836.
8
Multi-kinase inhibitors interact with sildenafil and ERBB1/2/4 inhibitors to kill tumor cells in vitro and in vivo. Booth L, Albers T, Roberts JL, Tavallai M, Poklepovic A, Lebedyeva IO, Dent P. Oncotarget. 2016 7:40398-40417. (WB; Human) [Full Text Article] [PubMed:27259258] [PMC:PMC5130016] Related Antibodies: LS-C31836.
9
PDE5 inhibitors enhance the lethality of pemetrexed through inhibition of multiple chaperone proteins and via the actions of cyclic GMP and nitric oxide. Booth L, Roberts JL, Poklepovic A, Gordon S, Dent P. Oncotarget. 2017 8:1449-1468. (WB; Human) [Full Text Article] [PubMed:27903966] [PMC:PMC5352068] Related Antibodies: LS-C31836.
10
The HDAC inhibitor AR42 interacts with pazopanib to kill trametinib/dabrafenib-resistant melanoma cells in vitro and in vivo. Booth L, Roberts JL, Sander C, Lee J, Kirkwood JM, Poklepovic A, Dent P. Oncotarget. 2017 8:16367-16386. (WB; Human) [Full Text Article] [PubMed:28146421] [PMC:PMC5369969] Related Antibodies: LS-C31836.
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For RESEARCH USE ONLY. Intended for use by laboratory professionals. Not intended for human diagnostic or therapeutic purposes.

The data on this page has been compiled from LifeSpan internal sources, the National Center for Biotechnology Information (NCBI), and The Universal Protein Resource (UniProt).