Poly(rC) Binding Protein 1 (PCBP1) antibody

Antigen: Poly(rC) Binding Protein 1 (PCBP1)

Synonyms: HNRPX, HNRPE1, hnRNP-X, hnRNP-E1, WBP17, [a]CP-1, alphaCP-1, PCBP1, RGD1561319, MGC140822

Clonality: Polyclonal

Host: Rabbit

Reactivity: Cow (Bovine), Dog (Canine), Human, Mouse (Murine), Rabbit, Rat (Rattus)

Application: Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Western Blotting (WB)

Catalog no.: ABIN310056

Additional Information

Alternative name: PCBP1

Description: PCBP1 appears to be multifunctional. It along with PCBP-2 and hnRNPK corresponds to the major cellular poly(rC)-binding protein. It contains three K-homologous (KH) domains which may be involved in RNA binding. This protein together with PCBP-2 also functions as translational coactivators of poliovirus RNA via a sequence-specific interaction with stem-loop IV of the IRES and promote poliovirus RNA replication by binding to its 5'-terminal cloverleaf structure. It has also been implicated in translational control of the 15-lipoxygenase mRNA, human Papillomavirus type 16 L2 mRNA, and hepatitis A virus RNA. PCBP1 is also suggested to play a part in formation of a sequence-specific alpha-globin mRNP complex which is associated with alpha-globin mRNA stability.This intronless gene is thought to be generated by retrotransposition of a fully processed PCBP-2 mRNA. This gene and PCBP-2 has paralogues PCBP3 and PCBP4 which is thought to arose as a result of duplication events of entire genes. The protein encoded by this gene appears to be multifunctional. It along with PCBP-2 and hnRNPK corresponds to the major cellular poly(rC)-binding proteins. It contains three K-homologous (KH) domains which may be involved in RNA binding. This encoded protein together with PCBP-2 also functions as translational coactivators of poliovirus RNA via a sequence-specific interaction with stem-loop IV of the IRES and promote poliovirus RNA replication by binding to its 5'-terminal cloverleaf structure. It has also been implicated in translational control of the 15-lipoxygenase mRNA, human Papillomavirus type 16 L2 mRNA, and hepatitis A virus RNA. The encoded protein is also suggested to play a part in formation of a sequence-specific alpha-globin mRNP complex which is associated with alpha-globin mRNA stability.This intronless gene is thought to have been generated by retrotransposition of a fully processed PCBP-2 mRNA. This gene and PCBP-2 have paralogues (PCBP3 and PCBP4) which are thought to have arisen as a result of duplication events of entire genes. The protein encoded by this gene appears to be multifunctional. It along with PCBP-2 and hnRNPK corresponds to the major cellular poly(rC)-binding protein. It contains three K-homologous (KH) domains which may be involved in RNA binding. This encoded protein together with PCBP-2 also functions as translational coactivators of poliovirus RNA via a sequence-specific interaction with stem-loop IV of the IRES and promote poliovirus RNA replication by binding to its 5'-terminal cloverleaf structure. It has also been implicated in translational control of the 15-lipoxygenase mRNA, human Papillomavirus type 16 L2 mRNA, and hepatitis A virus RNA. The encoded protein is also suggested to play a part in formation of a sequence-specific alpha-globin mRNP complex which is associated with alpha-globin mRNA stability. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications. Keywords: PCBP1, NM_006196, NP_006187, Q15365

Application Details

Application Notes: ELISA titre: 1:62500 . Western Blotting: Suggested dilution at 1 u ug/ml in 5% skim milk / PBS buffer, and HRP conjugated anti-Rabbit IgG should be diluted in 1: 50,000 - 100,000 as second antibody.

Research Area: Chromatin and Nuclear Signaling, DNA/RNA

Restrictions: For Research Use only

Images

anti-Poly(rC) Binding Protein 1 (PCBP1) antibody

Publications

Publications: Shi, Bencze, Stemmler et al.: "A cytosolic iron chaperone that delivers iron to ferritin." in: Science (New York, N.Y.), Vol. 320, Issue 5880, pp. 1207-10, 2008 (PubMed).