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Chaperonin Containing TCP1, Subunit 2 (Beta) (CCT2) (C-Term) antibody

Details for Product No. ABIN650525
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Antigen
Synonyms fa26a01, fc58a11, CHUNP6883, wu:fa26a01, wu:fc58a11, cct2, MGC89448, CCT2, 99D8.1, CCT-beta, CCTB, PRO1633, TCP-1-beta, Cctb
Epitope
C-Term
(13), (2), (2), (1), (1), (1), (1), (1), (1)
Reactivity
Human, Rat (Rattus)
(43), (23), (21), (14), (14), (14), (14), (5), (3), (2), (2), (2), (1), (1)
Host
Rabbit
(23), (18), (8)
Clonality
Monoclonal
Conjugate
Un-conjugated
(1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Western Blotting (WB), Immunohistochemistry (IHC), Immunofluorescence (IF)
(39), (13), (10), (10), (5), (4), (3), (2), (2), (1), (1)
Pubmed 5 references available
Quantity 100 µL
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Catalog No. ABIN650525
450.00 $
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Immunogen A synthetic peptide corresponding to residues on the C-terminus in human TCP1 Beta was used as an immunogen.
Specificity A synthetic peptide corresponding to residues on the C-terminus in human TCP1 Beta was used as an immunogen.
Alternative Name TCP1 beta
Background T-complex polypeptide 1 subunit beta (TCP1 beta) is a cytosolic molecular chaperone that belongs to the chaperonin-containing TCP1 (CCT) complex (1). The CCT complex is composed of eight subunits that assist in the folding of actin, tubulin, and other cytosolic proteins (1). The sequence differences among the CCT subunits are located mainly in their apical domains, suggesting some degree of specificity towards substrate binding (2). TCP1 beta plays a role in the folding of newly translated proteins in the cytosol (3). Major cytoskeletal proteins such as actin and tubulin, depend on CCT to maintain the integrity of the microfilament and microtubule-based cytoskeletal systems (4). The beta-tubulin/TCP1 beta complex may serve as an effective chemotherapeutic target for treating tumors overexpressing TCP1 beta (5).
Molecular Weight 50 kDA
Gene ID 3718
UniProt P78371
Research Area Signaling, Protein Modifications, Chromatin, Cell Structure
Application Notes The suggested dilution is: WB: = 1:2000 , IHC: = 1: 100-250
Comment

Background: T-complex polypeptide 1 subunit beta (TCP1 beta) is a cytosolic molecular chaperone that belongs to the chaperonin-containing TCP1 (CCT) complex (1). The CCT complex is composed of eight subunits that assist in the folding of actin, tubulin, and other cytosolic proteins (1). The sequence differences among the CCT subunits are located mainly in their apical domains, suggesting some degree of specificity towards substrate binding (2). TCP1 beta plays a role in the folding of newly translated proteins in the cytosol (3). Major cytoskeletal proteins such as actin and tubulin, depend on CCT to maintain the integrity of the microfilament and microtubule-based cytoskeletal systems (4). The beta-tubulin/TCP1 beta complex may serve as an effective chemotherapeutic target for treating tumors overexpressing TCP1 beta (5).

Restrictions For Research Use only
Format Liquid
Buffer 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Storage Comment TCP1 beta Antibody can be stored at -20°C for up to 12 months from time of receipt.
Expiry Date 12 months
Background publications Llorca, Martín-Benito, Grantham et al.: "The 'sequential allosteric ring' mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin." in: The EMBO journal, Vol. 20, Issue 15, pp. 4065-75, 2001 (PubMed).

Yokota, Yanagi, Yura et al.: "Cytosolic chaperonin-containing t-complex polypeptide 1 changes the content of a particular subunit species concomitant with substrate binding and folding activities during the cell cycle." in: European journal of biochemistry / FEBS, Vol. 268, Issue 17, pp. 4664-73, 2001 (PubMed).

Brackley, Grantham: "Activities of the chaperonin containing TCP-1 (CCT): implications for cell cycle progression and cytoskeletal organisation." in: Cell stress & chaperones, Vol. 14, Issue 1, pp. 23-31, 2008 (PubMed).

Lin, Tsai, Liu et al.: "Intracellular beta-tubulin/chaperonin containing TCP1-beta complex serves as a novel chemotherapeutic target against drug-resistant tumors." in: Cancer research, Vol. 69, Issue 17, pp. 6879-88, 2009 (PubMed).

Bichet: "V2R mutations and nephrogenic diabetes insipidus." in: Progress in molecular biology and translational science, Vol. 89, pp. 15-29, 2010 (PubMed).

Validation Images
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