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p107 antibody (Retinoblastoma-Like 1 (p107)) (full length)

Details for Product anti-RBL1 Antibody No. ABIN967438, Supplier: Log in to see
Antigen
  • AW547426
  • CP107
  • fj58e06
  • p107
  • PRB1
  • prb1
  • wu:fj58e06
Alternatives
anti-Human p107 antibody for Western Blotting
Epitope
full length
20
18
15
11
6
4
2
2
2
2
2
2
1
1
1
1
1
1
1
Reactivity
Human
106
48
40
2
2
1
Host
Mouse
99
7
Clonality (Clone)
Monoclonal ()
Conjugate
This p107 antibody is un-conjugated
7
6
6
4
4
4
2
2
2
2
2
2
2
2
2
Application
Immunoprecipitation (IP), Western Blotting (WB)
68
50
24
23
16
11
6
2
2
2
1
1
Supplier
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Brand BD Pharmingen™
Immunogen Human Full-length p107 Recombinant Protein
Clone SD9
Isotype IgG1
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
Purification The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name p107 (RBL1 Antibody Abstract)
Background P107 is a cellular protein that, like the retinoblastoma protein (Rb), can bind SV40 large T antigen and adenovirus E1A. It was originally described as an E1A-associated protein that was detected in extracts of the 293 adenovirus transformed human kidney cell line. p107 and Rb share sequence homology which mainly extends throughout their large T/E1A binding pockets. In cells that do not contain the viral oncogenes, p107 and Rb associate, independently, with cellular E2F. E2F, originally identified as an activator of the adenovirus E1A promoter, is a transcription factor. It is believed that E2F plays a role in the control of cellular genes that respond to proliferation signals. In vivo, the large T/E1A binding pocket of Rb, associates with E2F primarily in G1 and S phase. p107 forms two complexes with E2F, one in S phase with cdk2 and cyclin A, and one in G1 phase with cdk2 and cyclin E. In vitro, the pocket regions of p107 and Rb associate with the same set of proteins, except that p107 also associates with two additional proteins, one of which is cyclin A. Since p107 shares structural and biochemical features with Rb it has been suggested that p107, like Rb, is a tumor suppressor gene product, however, the biological function of p107 remains speculative. The SD9 clone has been reported to be crossreactive on monkey and mouse p107. It reportedly does not crossreact with Rb. Reports of epitope mapping have shown that SD9 recognizes a region between amino acids 414-653 of human p107.
Molecular Weight 107 kDa
Research Area Transcription Factors
Pathways Cell Division Cycle
Application Notes The following cell lines have been reported to be positive for p107 expression: (1) 293 (ATCC CRL-1573), (2) CEM (ATCC CCL-119), (3) Saos-2 (ATCC HTB-85), and (4) KHOS-240S (ATCC CRL-1545).
For the immunoprecipitation application, cyclin A (55 kDa) and cdk2 (33 kDa) have been reported to co-immunoprecipitate with p107.
Comment

Related Products: ABIN967389

Restrictions For Research Use only
Format Liquid
Concentration 0.5 mg/mL
Buffer Aqueous buffered solution containing ≤0.09 % sodium azide.
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 4 °C
Storage Comment Store undiluted at 4° C.
Product cited in: Lee, Galvin, See, Eckner, Livingston, Moran, Shi: "Relief of YY1 transcriptional repression by adenovirus E1A is mediated by E1A-associated protein p300." in: Genes & development, Vol. 9, Issue 10, pp. 1188-98, 1995 (PubMed).

Wu, Zukerberg, Ngwu, Harlow, Lees: "In vivo association of E2F and DP family proteins." in: Molecular and cellular biology, Vol. 15, Issue 5, pp. 2536-46, 1995 (PubMed).

Beijersbergen, Hijmans, Zhu, Bernards: "Interaction of c-Myc with the pRb-related protein p107 results in inhibition of c-Myc-mediated transactivation." in: The EMBO journal, Vol. 13, Issue 17, pp. 4080-6, 1994 (PubMed).

Fattaey, Harlow, Helin: "Independent regions of adenovirus E1A are required for binding to and dissociation of E2F-protein complexes." in: Molecular and cellular biology, Vol. 13, Issue 12, pp. 7267-77, 1994 (PubMed).

Lees, Saito, Vidal, Valentine, Look, Harlow, Dyson, Helin: "The retinoblastoma protein binds to a family of E2F transcription factors." in: Molecular and cellular biology, Vol. 13, Issue 12, pp. 7813-25, 1994 (PubMed).

Schneider, Gu, Zhu, Mahdavi, Nadal-Ginard: "Reversal of terminal differentiation mediated by p107 in Rb-/- muscle cells." in: Science (New York, N.Y.), Vol. 264, Issue 5164, pp. 1467-71, 1994 (PubMed).

Dyson, Dembski, Fattaey, Ngwu, Ewen, Helin: "Analysis of p107-associated proteins: p107 associates with a form of E2F that differs from pRB-associated E2F-1." in: Journal of virology, Vol. 67, Issue 12, pp. 7641-7, 1993 (PubMed).

Zhu, van den Heuvel, Helin, Fattaey, Ewen, Livingston, Dyson, Harlow: "Inhibition of cell proliferation by p107, a relative of the retinoblastoma protein." in: Genes & development, Vol. 7, Issue 7A, pp. 1111-25, 1993 (PubMed).

Cao, Faha, Dembski, Tsai, Harlow, Dyson: "Independent binding of the retinoblastoma protein and p107 to the transcription factor E2F." in: Nature, Vol. 355, Issue 6356, pp. 176-9, 1992 (PubMed).

Background publications Chittenden, Livingston, DeCaprio: "Cell cycle analysis of E2F in primary human T cells reveals novel E2F complexes and biochemically distinct forms of free E2F." in: Molecular and cellular biology, Vol. 13, Issue 7, pp. 3975-83, 1993 (PubMed).