TCP1 alpha Antibody (23c) Summary
| Immunogen |
Purified recombinant mouse TCP1 alpha construct encoding the C-terminal half of the 1.8 kb full-length Tcp 1 gene expressed in E. coli.
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| Epitope |
Ab13501 recognises the COOH group, addition of an alanine (LDDA COOH) prevents binding in ELISA assays to immobilized synthetic peptide sequences.
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| Localization |
Cytoplasmic
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| Specificity |
This recognizes other proteins, most notably the p102B COP subunit of Golgi coatomer. It does not react with human Hsp60 protein.
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| Isotype |
IgG2c
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| Clonality |
Monoclonal
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| Host |
Rat
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| Gene |
TCP1
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| Purity |
Protein G purified
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Applications/Dilutions
| Dilutions |
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| Application Notes |
Detects TCP1 alpha in 20 ug of RK13 heat shocked cell lysate. Predicited molecular weight: 60 kDa. Also detects a molecular mass band of approximately 92 kDa.
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Reactivity Notes
Cross-reacts with Mouse, Rat, Cow, Dog, Plants, Rabbit and Sheep. Not yet tested in other species.
Packaging, Storage & Formulations
| Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
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| Buffer |
PBS (pH 7.2)
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| Preservative |
No Preservative
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| Concentration |
1.0 mg/ml
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| Purity |
Protein G purified
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Alternate Names for TCP1 alpha Antibody (23c)
- CCT1T-complex protein 1 subunit alpha
- CCTa
- CCT-alpha
- D6S230E
- tailless complex polypeptide 1
- t-complex 1
- T-complex protein 1, alpha subunit
- TCP-1-alpha
Background
T complex polypeptide 1 (TCP1) is a ~60 kDa protein constitutively expressed in almost all eukaryotic cells, and is upregulated during spermatogenesis. It is found in the cytosol as a subunit of a hetero-oligomeric chaperone that is known to be involved in the folding of actin and tubulin. The family of proteins termed chaperonins act to recognize and stabilize polypeptide intermediates during folding, assembly and disassembly, and share many characteristics with Heat Shock Protein 70 (HSP 70) including high abundance, induction by environmental stress, and ATPase activity. The chaperonin family includes the mitochondrial HSP60, Escherichia coli GroEL, the plastid Rubisco subunit binding protein, and the archaebacterial protein TF55. The TCP1 sequence shows nearly 40% identity to TF55, but only minimal similarity to HSP60 and GroEL.