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Goat Anti-TCP1 Antibody
Peptide-affinity purified goat antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC, E |
|---|---|
| Primary Accession | P17987 |
| Other Accession | NP_001008897, 6950 |
| Reactivity | Human |
| Host | Goat |
| Clonality | Polyclonal |
| Concentration | 100ug/200ul |
| Isotype | IgG |
| Calculated MW | 60344 Da |
| Gene ID | 6950 |
|---|---|
| Other Names | T-complex protein 1 subunit alpha, TCP-1-alpha, CCT-alpha, TCP1, CCT1, CCTA |
| Format | 0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Goat Anti-TCP1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | TCP1 |
|---|---|
| Synonyms | CCT1, CCTA |
| 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). |
| Cellular Location | Cytoplasm, cytosol. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
The protein encoded by this gene is a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Alternate transcriptional splice variants of this gene, encoding different isoforms, have been characterized. In addition, three pseudogenes that appear to be derived from this gene have been found.
References
Variation at the NFATC2 Locus Increases the Risk of Thiazolinedinedione-Induced Edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) Study. Bailey SD, et al. Diabetes Care, 2010 Jul 13. PMID 20628086.
Chaperonin genes on the rise: new divergent classes and intense duplication in human and other vertebrate genomes. Mukherjee K, et al. BMC Evol Biol, 2010 Mar 1. PMID 20193073.
Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip. Talmud PJ, et al. Am J Hum Genet, 2009 Nov. PMID 19913121.
Functions of membrane binding domain of CTP:phosphocholine cytidylyltransferase in alveolar type II cells. Ridsdale R, et al. Am J Respir Cell Mol Biol, 2010 Jul. PMID 19684306.
A genome-wide association study identifies novel and functionally related susceptibility Loci for Kawasaki disease. Burgner D, et al. PLoS Genet, 2009 Jan. PMID 19132087.
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