Rabbit Anti-E2F5 Polyclonal Antibody
Purified Rabbit Polyclonal Antibody (Pab)
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Application ![]()
| WB, IHC-P, IHC-F, IF, E |
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Primary Accession | Q15329 |
Reactivity | Human, Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 37610 Da |
Physical State | Liquid |
Immunogen | KLH conjugated synthetic peptide derived from human E2F5 |
Epitope Specificity | 101-200/346 |
Isotype | IgG |
Purity | affinity purified by Protein A |
Buffer | 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol. |
SUBCELLULAR LOCATION | Nucleus. |
SIMILARITY | Belongs to the E2F/DP family. |
SUBUNIT | Component of the DRTF1/E2F transcription factor complex. Binds cooperatively with DP-1 to E2F sites. Interaction with retinoblastoma protein RB1 or proteins RBL1 and RBL2 inhibits the E2F transactivation domain. Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2. |
Important Note | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
Background Descriptions | The protein encoded by this gene is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transforming proteins of small DNA tumor viruses. The E2F proteins contain several evolutionarily conserved domains that are present in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein is differentially phosphorylated and is expressed in a wide variety of human tissues. It has higher identity to E2F4 than to other family members. Both this protein and E2F4 interact with tumor suppressor proteins p130 and p107, but not with pRB. Alternative splicing results in multiple variants encoding different isoforms. |
Gene ID | 1875 |
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Other Names | E2F-5; Transcription factor E2F5; E2F5 |
Dilution | WB=1:500-2000,IHC-P=1:100-500,IHC-F=1:100-500,IF=1:100-500,Flow-Cyt=1 µg /test,ELISA=1:5000-10000 |
Format | 0.01M TBS(pH7.4) with 1% BSA, 0.09% (W/V) sodium azide and 50% Glyce |
Storage | Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C. |
Name | E2F5 |
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Function | Transcriptional activator that binds to E2F sites, these sites are present in the promoter of many genes whose products are involved in cell proliferation. May mediate growth factor-initiated signal transduction. It is likely involved in the early responses of resting cells to growth factor stimulation. Specifically required for multiciliate cell differentiation: together with MCIDAS and E2F5, binds and activate genes required for centriole biogenesis. |
Cellular Location | Nucleus. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Transcriptional activator that binds to E2F sites, these sites are present in the promoter of many genes whose products are involved in cell proliferation. May mediate growth factor- initiated signal transduction. It is likely involved in the early responses of resting cells to growth factor stimulation.
REFERENCES
Itoh A.,et al.Cell. Mol. Biol. Res. 41:147-154(1995).
Hijmans E.M.,et al.Mol. Cell. Biol. 15:3082-3089(1995).
Sardet C.,et al.Proc. Natl. Acad. Sci. U.S.A. 92:2403-2407(1995).
Vaishnav Y.N.,et al.Biochem. Biophys. Res. Commun. 242:586-592(1998).
Li W.B.,et al.Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.

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