Anti-TCPb [F39P7F11]
Invented by Ayham Alnabulsi from Vertebrate Antibodies Limited
Invented at Vertebrate Antibodies Limited
- Datasheet
- References (2)
- Inventor Info
Info
![Image for Anti-TCPb [F39P7F11]](https://res.cloudinary.com/ximbio/image/upload/c_fit,fl_lossy,q_auto/89174927-e4aa-4eb1-b695-bb498d6b5824.jpg)
![Image for Anti-TCPb [F39P7F11]](https://res.cloudinary.com/ximbio/image/upload/c_fit,fl_lossy,q_auto/c85cd6c1-b003-4c79-9a8d-a89cc443df6c.jpg)
![BLAST analysis has shown that the peptide immunogen used to develop Anti-TCPb antibody [F39P7F11] is 100% identical in most vertebrates including fish. Immunohistochemistry was performed on Atlantic Salmon gill filament. (A) positive immunostaining, predominately cytoplasmic, is observed in gill filament cells. Strong staining is detected in undifferentiated basal and epithelial cells. (B) negative control (no primary antibody).](https://res.cloudinary.com/ximbio/image/upload/c_fit,fl_lossy,q_auto/ad5e9014-d957-41e2-ae2b-a88bc84cb855.png)
![Immunohistochemistry image showing positive staining of Anti-TCPb [F39P7F11] in Gilthead Sea Bream (Sparus aurata). BLAST analysis has shown that peptide immunogen used to develop Anti-TCPb [F39P7F11] is 100% identical in most vertebrates including fish. Immunohistochemistry was performed on the anterior intestine of Gilthead Sea Bream (Sparus aurata). Positive staining was observed in the base of the epithelium (the brush border).](https://res.cloudinary.com/ximbio/image/upload/c_fit,fl_lossy,q_auto/526acef7-d81f-4b51-8f16-d212cc1b670a.png)
![Image for Anti-TCPb [F39P7F11]](https://res.cloudinary.com/ximbio/image/upload/c_limit,fl_lossy,h_282,q_auto,w_368/89174927-e4aa-4eb1-b695-bb498d6b5824.jpg)
![Image for Anti-TCPb [F39P7F11]](https://res.cloudinary.com/ximbio/image/upload/c_limit,fl_lossy,h_282,q_auto,w_368/c85cd6c1-b003-4c79-9a8d-a89cc443df6c.jpg)
![BLAST analysis has shown that the peptide immunogen used to develop Anti-TCPb antibody [F39P7F11] is 100% identical in most vertebrates including fish. Immunohistochemistry was performed on Atlantic Salmon gill filament. (A) positive immunostaining, predominately cytoplasmic, is observed in gill filament cells. Strong staining is detected in undifferentiated basal and epithelial cells. (B) negative control (no primary antibody).](https://res.cloudinary.com/ximbio/image/upload/c_limit,fl_lossy,h_282,q_auto,w_368/ad5e9014-d957-41e2-ae2b-a88bc84cb855.png)
![Immunohistochemistry image showing positive staining of Anti-TCPb [F39P7F11] in Gilthead Sea Bream (Sparus aurata). BLAST analysis has shown that peptide immunogen used to develop Anti-TCPb [F39P7F11] is 100% identical in most vertebrates including fish. Immunohistochemistry was performed on the anterior intestine of Gilthead Sea Bream (Sparus aurata). Positive staining was observed in the base of the epithelium (the brush border).](https://res.cloudinary.com/ximbio/image/upload/c_limit,fl_lossy,h_282,q_auto,w_368/526acef7-d81f-4b51-8f16-d212cc1b670a.png)
![Image thumbnail for Anti-TCPb [F39P7F11]](https://res.cloudinary.com/ximbio/image/upload/c_fit,fl_lossy,h_45,q_auto/89174927-e4aa-4eb1-b695-bb498d6b5824.jpg)
![Image thumbnail for Anti-TCPb [F39P7F11]](https://res.cloudinary.com/ximbio/image/upload/c_fit,fl_lossy,h_45,q_auto/c85cd6c1-b003-4c79-9a8d-a89cc443df6c.jpg)
![Image thumbnail for Anti-TCPb [F39P7F11]](https://res.cloudinary.com/ximbio/image/upload/c_fit,fl_lossy,h_45,q_auto/ad5e9014-d957-41e2-ae2b-a88bc84cb855.png)
![Image thumbnail for Anti-TCPb [F39P7F11]](https://res.cloudinary.com/ximbio/image/upload/c_fit,fl_lossy,h_45,q_auto/526acef7-d81f-4b51-8f16-d212cc1b670a.png)
| Catalogue Number | 151868 |
| Applications | ELISA IHC WB |
| Antigen/Gene or Protein Targets | T-complex protein 1, beta subunit |
| Reactivity | Human, Mouse, Rat, Xenopus laevis and Salmon |
| Relevance | The chaperonins are key molecular complexes, which are essential in the folding of proteins to produce stable and functionally competent protein conformations. One member of the chaperonin group of proteins is TCP1 (chaperonin containing t-complex polypeptide 1, or CCT), but little is known about this protein in tumours. |
| Host | Mouse |
| Immunogen | C-terminal peptide with sequence RKRVPDHHPC conjugated to ovalbumin |
| Subclass | IgG2a kappa |
| Myeloma Used | P3X63Ag8.653 |
| Strain | Balb/c |
| Notes | BLAST analysis revealed 100% identity to the following: Human, Gorilla, Monkey, Marmoset, Mouse, Rat, Dog, Bovine, Hamster, Horse, Pig, Opossum, Platypus, Xenopus, Salmon, Pufferfish, Zebrafish and Stickleback. |
| Research Area | Apoptosis and Programmed Cell Death, Cancer, Cell Cycle |
References: 2 entries
Coghlin et al. 2006. J Pathol. 210(3):351-7. PMID: 16981251.
ELISA
Characterization and over-expression of chaperonin t-complex proteins in colorectal cancer.
Europe PMC ID: 16981251
Add a reference
References: 2 entries
Coghlin et al. 2006. J Pathol. 210(3):351-7. PMID: 16981251.
ELISA
Characterization and over-expression of chaperonin t-complex proteins in colorectal cancer.
Add a reference
