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Rat Anti-CCT2 Recombinant Antibody (CBYJT-1069) (CBMAB-T0079-YJ)

Provided herein is a Rat monoclonal antibody, which binds to CCT2 (Chaperonin Containing TCP1 Subunit 2). The antibody can be used for immunoassay techniques, such as WB.
See all CCT2 antibodies

Summary

Host Animal
Rat
Specificity
Human, Mouse, Rat, Sheep, Rabbit, Chicken, Hamster, Cattle, Dog, Pig, Monkey
Clone
CBYJT-1069
Antibody Isotype
IgG2b
Application
WB

Basic Information

Immunogen
CCT beta peptide conjugated to PPD.
Specificity
Human, Mouse, Rat, Sheep, Rabbit, Chicken, Hamster, Cattle, Dog, Pig, Monkey
Antibody Isotype
IgG2b
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!]

Buffer
PBS, pH 7.4
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
chaperonin containing TCP1, subunit 2 (beta)
Introduction
CCT2 (Chaperonin Containing TCP1 Subunit 2) is a component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex it may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable).
Entrez Gene ID
Human10576
Mouse12461
Rat299809
Monkey717182
Cattle505313
Dog474445
Sheep101102222
Hamster100759253
Rabbit100216334
Pig100157776
Chicken417846
UniProt ID
HumanP78371
MouseP80314
RatQ5XIM9
MonkeyF6PJP5
CattleQ3ZBH0
DogF6V0D8
SheepW5QGG6
HamsterP86245
PigF6Q936
RabbitB6V9S9
ChickenQ5F424
Alternative Names
Chaperonin Containing TCP1 Subunit 2; Chaperonin Containing TCP1, Subunit 2 (Beta); TCP-1-Beta; CCT-Beta; 99D8.1; CCTB; Chaperonin Containing T-Complex Polypeptide 1, Beta Subunit
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444).
The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444).
As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638).
The TRiC complex plays a role in the folding of actin and tubulin (Probable).
Biological Process
Binding of sperm to zona pellucida Source: Ensembl
Chaperone-mediated protein complex assembly Source: MGI
Chaperone mediated protein folding independent of cofactor Source: BHF-UCL
Neutrophil degranulation Source: Reactome
Positive regulation of establishment of protein localization to telomere Source: BHF-UCL
Positive regulation of protein localization to Cajal body Source: BHF-UCL
Positive regulation of telomerase activity Source: BHF-UCL
Positive regulation of telomerase RNA localization to Cajal body Source: BHF-UCL
Positive regulation of telomere maintenance via telomerase Source: BHF-UCL
Protein folding Source: FlyBase
Protein stabilization Source: BHF-UCL
scaRNA localization to Cajal body Source: BHF-UCL
Toxin transport Source: Ensembl
Cellular Location
Cytoplasm

Ghozlan, H., Showalter, A., Lee, E., Zhu, X., & Khaled, A. R. (2021). Chaperonin-Containing TCP1 complex (CCT) promotes breast cancer growth through correlations with key cell cycle regulators. Frontiers in oncology, 11.

Li, W., Liu, J., & Zhao, H. (2021). Prognostic Power of a Chaperonin Containing TCP-1 Subunit Genes Panel for Hepatocellular Carcinoma. Frontiers in genetics, 12, 502.

Ghozlan, H. H., Showalter, A., & Khaled, A. R. (2021). Chaperonin-Containing TCP1 complex (CCT) promotes breast cancer by targeting key cell cycle regulators.

Cox, A., Martini, A., Lee, E., Moroose, R., Khaled, A., & Khaled, A. R. (2021). Using chaperonin containing TCP1 as a marker to track clinically relevant circulating tumor cells.

Liu, Q., Qi, Y., Kong, X., Wang, X., Zhang, W., Zhai, J., ... & Wang, J. (2021). Molecular and Clinical Characterization of CCT2 Expression and Prognosis via Large-Scale Transcriptome Profile of Breast Cancer. Frontiers in oncology, 11.

Showalter, A. E., Martini, A. C., Nierenberg, D., Hosang, K., Fahmi, N. A., Gopalan, P., ... & Khaled, A. R. (2020). Investigating chaperonin-containing TCP-1 subunit 2 as an essential component of the chaperonin complex for tumorigenesis. Scientific reports, 10(1), 1-14.

Hallal, S., Russell, B. P., Wei, H., Lee, M. Y. T., Toon, C. W., Sy, J., ... & Kaufman, K. L. (2019). Extracellular vesicles from neurosurgical aspirates identifies chaperonin containing TCP1 subunit 6A as a potential glioblastoma biomarker with prognostic significance. Proteomics, 19(1-2), 1800157.

Carr, A. C., Khaled, A. S., Bassiouni, R., Flores, O., Nierenberg, D., Bhatti, H., ... & Khaled, A. R. (2017). Targeting chaperonin containing TCP1 (CCT) as a molecular therapeutic for small cell lung cancer. Oncotarget, 8(66), 110273.

Li, L. J., Zhang, L. S., Han, Z. J., He, Z. Y., Chen, H., & Li, Y. M. (2017). Chaperonin containing TCP-1 subunit 3 is critical for gastric cancer growth. Oncotarget, 8(67), 111470.

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

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