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Mouse Anti-HSPA1L Recombinant Antibody (CAP896) (CBMAB-AP2709LY)


See all HSPA1L antibodies

Summary

Host Animal
Mouse
Specificity
Rat
Clone
CAP896
Antibody Isotype
IgG
Application
ICC, IHC, IP, WB

Basic Information

Immunogen
Met1~Asp641
Specificity
Rat
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
heat shock protein family A (Hsp70) member 1 like
Introduction
This gene encodes a 70kDa heat shock protein. In conjunction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which also encode isoforms of the 70kDa heat shock protein. [provided by RefSeq, Jul 2008]
Entrez Gene ID
24963
UniProt ID
P55063
Alternative Names
Heat Shock Protein Family A (Hsp70) Member 1 Like; Heat Shock 70kDa Protein 1-Like; Heat Shock 70 KDa Protein 1-Hom; Heat Shock 70kD Protein-Like 1; Heat Shock 70 KDa Protein 1L; HSP70-HOM;
Function
Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release (PubMed:26865365).

Positive regulator of PRKN translocation to damaged mitochondria (PubMed:24270810).
Biological Process
Binding of sperm to zona pellucida Source: Ensembl
Cellular response to unfolded protein Source: GO_Central
Chaperone cofactor-dependent protein refolding Source: GO_Central
Positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
Protein refolding Source: UniProtKB
Response to unfolded protein Source: ProtInc
Vesicle-mediated transport Source: GO_Central
Cellular Location
Cytosol; Blood microparticle; Mitochondrial matrix; Nucleoplasm; Nucleus; Plasma membrane; Cell body; Cytoplasm; Zona pellucida receptor complex

Liu, X., Teng, Z., Wang, Z., Zhu, P., Song, Z., & Liu, F. (2022). Expressions of HSPA1L and HSPA9 are associated with poor sperm quality of low‐motility spermatozoa in fertile men. Andrologia, 54(2), e14321.

Muhammad, J. S., Saheb Sharif-Askari, N., Cui, Z. G., Hamad, M., & Halwani, R. (2021). SARS-CoV-2 infection-induced promoter hypomethylation as an epigenetic modulator of heat shock protein A1L (HSPA1L) gene. Frontiers in Genetics, 12, 622271.

Nakatsuka, A., Yamaguchi, S., Eguchi, J., Kakuta, S., Iwakura, Y., Sugiyama, H., & Wada, J. (2021). A Vaspin–HSPA1L complex protects proximal tubular cells from organelle stress in diabetic kidney disease. Communications Biology, 4(1), 373.

Lee, J. H., Yoon, Y. M., Song, K. H., Noh, H., & Lee, S. H. (2020). Melatonin suppresses senescence‐derived mitochondrial dysfunction in mesenchymal stem cells via the HSPA1L–mitophagy pathway. Aging cell, 19(3), e13111.

Wang, X., Xie, W., Yao, Y., Zhu, Y., Zhou, J., Cui, Y., ... & Liu, M. (2020). The heat shock protein family gene Hspa1l in male mice is dispensable for fertility. PeerJ, 8, e8702.

De Andrade, W. P., Braga, L. D. C., Goncales, N. G., Silva, L. M., & Da Silva Filho, A. L. (2020). HSPA1A, HSPA1L and TRAP1 heat shock genes may be associated with prognosis in ovarian epithelial cancer. Oncology Letters, 19(1), 359-367.

Choi, S. I., Lee, J. H., Kim, R. K., Jung, U., Kahm, Y. J., Cho, E. W., & Kim, I. G. (2020). HSPA1L enhances cancer stem cell-like properties by activating IGF1Rβ and regulating β-catenin transcription. International Journal of Molecular Sciences, 21(18), 6957.

Williams, P. A., Kobilnyk, H. E., McMillan, E. A., & Strochlic, T. I. (2019). MAPKAP kinase 2–mediated phosphorylation of HspA1L protects male germ cells from heat stress–induced apoptosis. Cell Stress and Chaperones, 24, 1127-1136.

Kohan, L., Tabiee, O., & Sepahi, N. (2019). HSPA1L and HSPA1B gene polymorphisms and haplotypes are associated with idiopathic male infertility in Iranian population. European Journal of Obstetrics & Gynecology and Reproductive Biology, 240, 57-61.

Huusko, J. M., Karjalainen, M. K., Graham, B. E., Zhang, G., Farrow, E. G., Miller, N. A., ... & Muglia, L. J. (2018). Whole exome sequencing reveals HSPA1L as a genetic risk factor for spontaneous preterm birth. PLoS genetics, 14(7), e1007394.

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

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