Anti-PCBP2 (AB1) antibody produced in rabbit

Poly(rC) binding protein 2 (PCBP2) is a poly(rC)-binding protein that regulate of RNA processing. PCBP2 is believed to be involved in the shuttling of nascent mRNPs to processing bodies (P-bodies) which are involved in mRNA degradation and siRNA- or miRNA-mediated gene silencing. PCBP2 promotes the processing of various microRNAs (miRNA) via its association with Dicer. MicroRNA processing may be regulated by cytosolic iron via the PCBP2:Dicer-dependent processes. The PCBP2-AIP4 axis defines a signaling cascade for MAVS degradation and ′fine tuning′ of antiviral innate immunity. PCBP2 stabilization of mRNA increases the expression of STAT1 and STAT2 which enhances the antiviral effect of IFN-α.

Anti-PCBP2 (AB1) polyclonal antibody reacts with poly(rC) binding protein 2 proteins.

Synthetic peptide directed towards the middle region of human PCBP2

Anti-PCBP2 (AB1) polyclonal antibody is used to tag poly(rC) binding protein 2 for detection and quantitation by Western blotting and in plasma by immunohistochemical (IHC) techniques. It is used as a probe to determine the roles of poly(rC) binding protein 2 in RNA trafficking and processing.

PCBP2 appears to be multifunctional. It along with PCBP-1 and hnRNPK corresponds to the major cellular poly(rC)-binding proteins. This protein together with PCBP-1 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 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 gene and PCBP-1 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-1 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-1 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 multiexon structural mRNA is thought to be retrotransposed to generate PCBP-1 intronless gene which has similar functions. This gene and PCBP-1 has paralogues PCBP3 and PCBP4 which is thought to arose as a result of duplication events of entire genes. It also has two processed pseudogenes PCBP2P1 and PCBP2P2. There are presently two alternatively spliced transcript variants described for this gene.

Synthetic peptide located within the following region: VIFAGGQDRYSTGSDSASFPHTTPSMCLNPDLEGPPLEAYTIQGQYAIPQ

Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

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