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Mouse Anti-CCT2 Recombinant Antibody (CBYJT-1064) (CBMAB-T0074-YJ)

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Published Data

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat, Dog, Cattle, Pig
Clone
CBYJT-1064
Antibody Isotype
IgG1, κ
Application
ELISA, IF, IP, WB

Basic Information

Immunogen
Amino acids 509-534 at the C-terminus of TCP-1 β of human origin.
Host Species
Mouse
Specificity
Human, Mouse, Rat, Dog, Cattle, Pig
Antibody Isotype
IgG1, κ
Clonality
Monoclonal Antibody
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)1:50-1:500
ELISA1:100-1:1,000

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

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.2 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
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
UniProt ID
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
More Infomation

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.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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