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Mouse Anti-HSPD1 Monoclonal Antibody (CBFYH-3253) (CBMAB-H0140-FY)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYH-3253
Antibody Isotype
IgG1, κ
Application
WB, FC, ELISA, IF, IP, IHC-P, IHC-Fr, CyTOF

Basic Information

Immunogen
Recombinant human HSP60 protein
Specificity
Human
Antibody Isotype
IgG1, κ
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
Concentration
1 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
heat shock protein family D (Hsp60) member 1
Introduction
This gene encodes a member of the chaperonin family. The encoded mitochondrial protein may function as a signaling molecule in the innate immune system. This protein is essential for the folding and assembly of newly imported proteins in the mitochondria. This gene is adjacent to a related family member and the region between the 2 genes functions as a bidirectional promoter. Several pseudogenes have been associated with this gene. Two transcript variants encoding the same protein have been identified for this gene. Mutations associated with this gene cause autosomal recessive spastic paraplegia 13.
Entrez Gene ID
3329
UniProt ID
P10809
Alternative Names
Heat Shock Protein Family D (Hsp60) Member 1; Heat Shock 60kDa Protein 1 (Chaperonin); Mitochondrial Matrix Protein P1; P60 Lymphocyte Protein; 0 KDa Chaperonin; Chaperonin 60; HuCHA60; HSP-60; HSP60; CPN60; Spastic Paraplegia 13 (Autosomal Dominant)
Function
Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:1346131, PubMed:11422376).

The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable).
Biological Process
de novo' protein folding Source: BHF-UCL
Activation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
Apoptotic mitochondrial changes Source: GO_Central
B cell activation Source: BHF-UCL
B cell proliferation Source: BHF-UCL
Biological process involved in interaction with symbiont Source: CAFA
Chaperone-mediated protein complex assembly Source: BHF-UCL
Isotype switching to IgG isotypes Source: BHF-UCL
Mitochondrial unfolded protein response Source: GO_Central
MyD88-dependent toll-like receptor signaling pathway Source: BHF-UCL
Negative regulation of apoptotic process Source: UniProtKB
Positive regulation of apoptotic process Source: BHF-UCL
Positive regulation of interferon-alpha production Source: BHF-UCL
Positive regulation of interferon-gamma production Source: BHF-UCL
Positive regulation of interleukin-10 production Source: BHF-UCL
Positive regulation of interleukin-12 production Source: BHF-UCL
Positive regulation of interleukin-6 production Source: BHF-UCL
Positive regulation of macrophage activation Source: BHF-UCL
Positive regulation of T cell activation Source: BHF-UCL
Positive regulation of T cell mediated immune response to tumor cell Source: BHF-UCL
Protein folding Source: GO_Central
Protein import into mitochondrial intermembrane space Source: GO_Central
Protein maturation Source: BHF-UCL
Protein refolding Source: UniProtKB
Protein stabilization Source: UniProtKB
Response to cold Source: AgBase
Response to unfolded protein Source: BHF-UCL
T cell activation Source: MGI
Cellular Location
Mitochondrion matrix
Involvement in disease
Spastic paraplegia 13, autosomal dominant (SPG13):
A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body.
Leukodystrophy, hypomyelinating, 4 (HLD4):
A severe autosomal recessive hypomyelinating leukodystrophy. Clinically characterized by infantile-onset rotary nystagmus, progressive spastic paraplegia, neurologic regression, motor impairment, profound mental retardation. Death usually occurs within the first two decades of life.
More Infomation

Duan, Y., Yu, J., Chen, M., Lu, Q., Ning, F., Gan, X., ... & Lash, G. E. (2023). Knockdown of heat shock protein family D member 1 (HSPD1) promotes proliferation and migration of ovarian cancer cells via disrupting the stability of mitochondrial 3-oxoacyl-ACP synthase (OXSM). Journal of ovarian research, 16(1), 1-14.

Zheng, X., Chang, S., Liu, Y., Dai, X., & You, C. (2023). Human Mitochondrial Protein HSPD1 Binds to and Regulates the Repair of Deoxyinosine in DNA. Journal of Proteome Research, 22(4), 1339-1346.

Wu, T., Jia, L., Lei, S., Jiang, H., Liu, J., Li, N., ... & Lei, L. (2022). Host HSPD1 Translocation from Mitochondria to the Cytoplasm Induced by Streptococcus suis Serovar 2 Enolase Mediates Apoptosis and Loss of Blood–Brain Barrier Integrity. Cells, 11(13), 2071.

Song, X., Chen, B., Liang, Y., Li, Y., Zhang, H., Han, D., ... & Yang, Q. (2022). CircEIF3H-IGF2BP2-HuR scaffold complex promotes TNBC progression via stabilizing HSPD1/RBM8A/G3BP1 mRNA. Cell Death Discovery, 8(1), 261.

Parma, B., Ramesh, V., Gollavilli, P. N., Siddiqui, A., Pinna, L., Schwab, A., ... & Ceppi, P. (2021). Metabolic impairment of non-small cell lung cancers by mitochondrial HSPD1 targeting. Journal of Experimental & Clinical Cancer Research, 40(1), 1-20.

Klebl, D. P., Feasey, M. C., Hesketh, E. L., Ranson, N. A., Wurdak, H., Sobott, F., ... & Muench, S. P. (2021). Cryo-EM structure of human mitochondrial HSPD1. Iscience, 24(1).

Albadawy, R., Agwa, S. H., Khairy, E., Saad, M., El Touchy, N., Othman, M., & Matboli, M. (2021). Clinical significance of hspd1/mmp14/itgb1/mir-6881-5p/lnc-sparcl1-1: 2 rna panel in nafld/nash diagnosis: Egyptian pilot study. Biomedicines, 9(9), 1248.

Cömert, C., Brick, L., Ang, D., Palmfeldt, J., Meaney, B. F., Kozenko, M., ... & Bross, P. (2020). A recurrent de novo HSPD1 variant is associated with hypomyelinating leukodystrophy. Molecular Case Studies, 6(3), a004879.

Kang, B. H., Shu, C. W., Chao, J. K., Lee, C. H., Fu, T. Y., Liou, H. H., ... & Liu, P. F. (2019). HSPD1 repressed E-cadherin expression to promote cell invasion and migration for poor prognosis in oral squamous cell carcinoma. Scientific reports, 9(1), 8932.

Kim, S. K., Kim, K., Ryu, J. W., Ryu, T. Y., Lim, J. H., Oh, J. H., ... & Cho, H. S. (2019). The novel prognostic marker, EHMT2, is involved in cell proliferation via HSPD1 regulation in breast cancer. International Journal of Oncology, 54(1), 65-76.

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

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