The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/1000. Detects a band of approximately 87 kDa (predicted molecular weight: 81 kDa).
Use at an assay dependent concentration.
Use at an assay dependent concentration. PubMed: 17576689
FunctionRegulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin-T1) complex, also called positive transcription elongation factor B (P-TEFb), which is proposed to facilitate the transition from abortive to productive elongation by phosphorylating the CTD (carboxy-terminal domain) of the large subunit of RNA polymerase II (RNA Pol II). In case of HIV or SIV infections, binds to the transactivation domain of the viral nuclear transcriptional activator, Tat, thereby increasing Tat's affinity for the transactivating response RNA element (TAR RNA). Serves as an essential cofactor for Tat, by promoting RNA Pol II activation, allowing transcription of viral genes.
Tissue specificityUbiquitously expressed.
Sequence similaritiesBelongs to the cyclin family. Cyclin C subfamily.
Human immunodeficiency virus 1 expression antibody
Human immunodeficiency virus type 1 (HIV 1) expression (elevated) 1 antibody
pTEFb subunit antibody
Subunit of positive elongation transcription factor b antibody
Anti-Cyclin T1 antibody images
Western blot - Cyclin T1 antibody (ab27963)
All lanes : Anti-Cyclin T1 antibody (ab27963) at 1/1000 dilution
Lane 1 : HeLa whole cell lysate Lane 2 : HeLa cell nuclear lysate Lane 3 : monkey Vero cell lysate Lane 4 : mouse kidney cell lysate Lane 5 : Drosophila S2 cell lysate Lane 6 : horse dermal cell lysate
Secondary donkey anti-sheep peroxidase conjugate at 1/20000 dilution
Krueger BJ et al. LARP7 is a stable component of the 7SK snRNP while P-TEFb, HEXIM1 and hnRNP A1 are reversibly associated. Nucleic Acids Res : (2008).
Read more (PubMed: 18281698) »
Sedore SC et al. Manipulation of P-TEFb control machinery by HIV: recruitment of P-TEFb from the large form by Tat and binding of HEXIM1 to TAR. Nucleic Acids Res35:4347-58 (2007).
Read more (PubMed: 17576689) »