C57BL/6JCya-Hspbp1em1flox/Cya
Common Name
Hspbp1-flox
Product ID
S-CKO-19187
Backgroud
C57BL/6JCya
Strain ID
CKOCMP-66245-Hspbp1-B6J-VB
When using this mouse strain in a publication, please cite “Hspbp1-flox Mouse (Catalog S-CKO-19187) were purchased from Cyagen.”
Product Type
Age
Genotype
Sex
Quantity
Basic Information
Strain Name
Hspbp1-flox
Strain ID
CKOCMP-66245-Hspbp1-B6J-VB
Gene Name
Product ID
S-CKO-19187
Gene Alias
1500019G21Rik
Background
C57BL/6JCya
NCBI ID
Modification
Conditional knockout
Chromosome
Chr 7
Phenotype
Datasheet
Application
--
Strain Description
Ensembl Number
ENSMUST00000079970
NCBI RefSeq
NM_024172
Target Region
Exon 3
Size of Effective Region
~0.7 kb
Overview of Gene Research
Hspbp1, also known as Hsp70-binding protein 1, is a co-chaperone belonging to a family that regulates Hsp70 activity [1,3,6]. It plays a crucial role in multiple cellular processes, such as protein folding, as it functions as a nucleotide exchange factor for Hsp70 molecular chaperones, facilitating the conversion from the ADP-bound to the ATP-bound state of Hsp70, thus closing the chaperone folding cycle [3,6]. It is involved in DNA repair, apoptosis, antiviral response, and the formation of stress granules, and is associated with diseases like breast cancer and HIV infection [1,2,4,5,7].
In breast cancer, in BRCA1-proficient cells, knocking down or overexpressing HspBP1 leads to profound changes in tumorigenesis, including in vitro anchorage-independent cell growth and in vivo tumor formation in xenograft models. It promotes BRCA1-mediated homologous recombination DNA repair by interacting with BRCA1, contributing to breast cancer suppression and genomic stability maintenance. However, it does not affect the tumorigenic properties in BRCA1-deficient cells. Additionally, regardless of BRCA1 status, HspBP1 facilitates cell survival in response to ionizing radiation by interfering with the association of Hsp70 and apoptotic protease-activating factor-1 [1]. In the antiviral response, knockdown and knockout of HSPBP1 lead to down-regulation of virus-induced RIG-I expression, inhibiting IRF3 activation and reducing the production of IFNB1, indicating that HSPBP1 positively regulates the antiviral signal pathway by inhibiting the K48-linked ubiquitination of RIG-I [2].
In conclusion, Hspbp1 is a multifunctional co-chaperone. Its role in DNA repair, apoptosis, and the antiviral response has been revealed through studies including gene-knockdown and knockout models. In breast cancer, it is closely related to BRCA1-associated tumorigenesis regulation, and in the antiviral field, it plays a positive role in the RLR-mediated antiviral response. These findings contribute to understanding the underlying mechanisms of related diseases and may provide potential therapeutic targets.
References：
1. Youn, Cha Kyung, Lee, Jung-Hee, Hariharasudhan, Gurusamy, Chang, In-Youb, You, Ho Jin. 2022. HspBP1 is a dual function regulatory protein that controls both DNA repair and apoptosis in breast cancer cells. In Cell death & disease, 13, 309. doi:10.1038/s41419-022-04766-0. https://pubmed.ncbi.nlm.nih.gov/35387978/
2. Yang, Ya-Xian, Huang, Jing-Ping, Li, Sheng-Na, Xie, Tao, Xu, Liang-Guo. 2021. HSPBP1 facilitates cellular RLR-mediated antiviral response by inhibiting the K48-linked ubiquitination of RIG-I. In Molecular immunology, 134, 62-71. doi:10.1016/j.molimm.2021.03.002. https://pubmed.ncbi.nlm.nih.gov/33713958/
3. Bracher, Andreas, Verghese, Jacob. . Nucleotide Exchange Factors for Hsp70 Molecular Chaperones: GrpE, Hsp110/Grp170, HspBP1/Sil1, and BAG Domain Proteins. In Sub-cellular biochemistry, 101, 1-39. doi:10.1007/978-3-031-14740-1_1. https://pubmed.ncbi.nlm.nih.gov/36520302/
4. Mahboubi, Hicham, Moujaber, Ossama, Kodiha, Mohamed, Stochaj, Ursula. 2020. The Co-Chaperone HspBP1 Is a Novel Component of Stress Granules that Regulates Their Formation. In Cells, 9, . doi:10.3390/cells9040825. https://pubmed.ncbi.nlm.nih.gov/32235396/
5. Ceccin, A D F, Souza, A P D, Hilário, G T, Romão, P R T, Rodrigues Junior, L C. 2019. HspBP1 and anti-HspBP1 levels in the serum of HIV-infected individuals are associated to the disease progression. In Journal of applied microbiology, 127, 576-585. doi:10.1111/jam.14230. https://pubmed.ncbi.nlm.nih.gov/30786116/
6. Bracher, Andreas, Verghese, Jacob. . GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: nucleotide exchange factors for Hsp70 molecular chaperones. In Sub-cellular biochemistry, 78, 1-33. doi:10.1007/978-3-319-11731-7_1. https://pubmed.ncbi.nlm.nih.gov/25487014/
7. Iyer, Kruthika, Mitra, Alapani, Mitra, Debashis. 2022. Identification of 5' upstream sequence involved in HSPBP1 gene transcription and its downregulation during HIV-1 infection. In Virus research, 324, 199034. doi:10.1016/j.virusres.2022.199034. https://pubmed.ncbi.nlm.nih.gov/36581045/
Quality Control Standard
Sperm Test
Pre-cryopreservation: Measurement of sperm concentration, determination of sperm viability.
Post-cryopreservation: A vial of cryopreserved sperms is selected for in-vitro fertilization from each batch.
Environmental Standards:SPF
Available Region:Global
Source:Cyagen
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