Recombinant Human Poly (PCBP2) Protein (His&Myc)

Name: Recombinant Human Poly (PCBP2) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-01531P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Poly (PCBP2) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q15366
Target Symbol	PCBP2
Synonyms	Alpha-CP2;Heterogeneous nuclear ribonucleoprotein E2;hnRNP E2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MDTGVIEGGLNVTLTIRLLMHGKEVGSIIGKKGESVKKMREESGARINISEGNCPERIITLAGPTNAIFKAFAMIIDKLEEDISSSMTNSTAASRPPVTLRLVVPASQCGSLIGKGGCKIKEIRESTGAQVQVAGDMLPNSTERAITIAGIPQSIIECVKQICVVMLETLSQSPPKGVTIPYRPKPSSSPVIFAGGQDRYSTGSDSASFPHTTPSMCLNPDLEGPPLEAYTIQGQYAIPQPDLTKLHQLAMQQSHFPMTHGNTGFSGIESSSPEVKGYWGLDASAQTTSHELTIPNDLIGCIIGRQGAKINEIRQMSGAQIKIANPVEGSTDRQVTITGSAASISLAQYLINVRLSSETGGMGSS
Expression Range	1-365aa
Protein Length	Full Length
Mol. Weight	46.0 kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. Major cellular poly(rC)-binding protein. Binds also poly(rU). Negatively regulates cellular antiviral responses mediated by MAVS signaling. It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitination and degradation.; (Microbial infection) In case of infection by poliovirus, binds to the viral internal ribosome entry site (IRES) and stimulates the IRES-mediated translation. Also plays a role in initiation of viral RNA replication in concert with the viral protein 3CD.
Subcellular Location	Nucleus. Cytoplasm. Note=Loosely bound in the nucleus. May shuttle between the nucleus and the cytoplasm.
Database References	HGNC: 8648 OMIM: 601210 KEGG: hsa:5094 STRING: 9606.ENSP00000352438 UniGene: PMID: 28787701 Double immunofluorescence for hnRNP E2 and TDP-43 showed most TDP-43 immunopositive dystrophic neuritis within frontal and temporal cortex, and the neuronal cytoplasmic inclusions seen in dentate gyrus granule cells, to contain hnRNP E2. Present findings indicate an association between TDP-43 and hnRNP E2 which might underlie the pathogenetic mechanism of Semantic Dementia Frontotemporal Lobar Degeneration. PMID: 28666471 Data suggest that the interaction between PCBP2 and the 3'UTR of the ARHGDIA mRNA may induce a local change in RNA structure that favors subsequent binding of miR-151-5p and miR-16, thus leading to the suppression of ARHGDIA expression. PMID: 26761212 To promote intracellular iron flux, an iron chaperone appears to be essential for receiving iron from heme catabolism. Data suggest that PCBP2 competes with CPR for binding HO1; PCBP2 K homology 3 domain is important for HO1/PCBP2 interaction; heme prompts HO1/CPR multimer and decreases HO1/PCBP2 multimer. [PCBP2 = poly(rC) binding protein 2; CPR = cytochrome P450 reductase; HO1 = heme oxidase 1] PMID: 28655775 Study determined that PCBP2 specifically associates with components of this kinase cascade and regulates the activities of its downstream transcriptional coactivators. PMID: 27215387 These results suggest that FPN1 exports iron received from the iron chaperone PCBP2. Therefore, it was found that PCBP2 modulates cellular iron export, which is an important physiological process. PMID: 27302059 PCBP2 was overexpressed in esophageal squamous cell carcinoma tissues and cell lines. PCBP2 expression promoted proliferation of ESCC cells. We also found that reduced PCBP2 expression might induce ESCC cell apoptosis with increased cleaved caspase3 expression. Overall, our findings indicated that PCBP2 might be involved in the ESCC progression and be considered as a new treatment target in ESCC. PMID: 27461833 High expression of PCBP2 may contribute to sorafenib resistance in hepatocellular carcinoma cells. PMID: 27748915 our data indicate that miR-214 may function as tumor suppressor in glioma by targeting PCBP2 PMID: 26722446 PCBP2 knockdown promoted angiotensin II-induced hypertrophy (increase in cell size, protein synthesis and activation of fetal genes) of cardiomyocytes, while PCBP2 overexpression obtained oppose effects. PMID: 26116532 Protein and mRNA levels of PCBP2 were down-regulated under insulin-resistant conditions. Over-expression of PCBP2 inhibits HIF1alpha and STAT3 pathway. PMID: 26002461 STAT3 functions via cellular PCBP2 to regulate B-cell lytic susceptibility by restraining Epstein-Barr Virus lytic activation. PMID: 25717101 PCBP2-depletion induces apoptosis in gastric cancer cells via up-regulating expression of pro-apoptotic proteins and down-regulating anti-apoptotic proteins. miR-34a is a target of PCBP2, and miR-34a is critically essential for the function of PCBP2. PMID: 24796666 SIRT6 inhibits glioma cell proliferation and colony formation in vitro and glioma cell growth in vivo in a PCBP2 dependent manner. SIRT6 inhibits PCBP2 expression through deacetylating H3K9ac and SIRT6 acts as a tumor suppressor in glioma. PMID: 24607900 Inhibition of poliovirus-induced cleavage of cellular PCBP2 protein reduces the viral RNA replication. PMID: 24371074 PCBP2 and PTB are differentially cleaved by human rhinovirus proteinase in infected cells. PMID: 24418535 PCBP2 controls the 3' processing of its own transcript. PMID: 23629627 PCBP2 is an RNA-binding protein that modulates glioma growth by regulating FHL3 PMID: 23585479 Cytosolic iron may modulate the association between PCBP2 and Dicer, as well as the multimerization of PCBP2 and its ability to bind to miRNA precursors PMID: 22633452 PCBP2 specifically and selectively interacts with rabies virus glycoprotein mRNA and this interaction may contribute to the post-transcriptional regulation of glycoprotein expression PMID: 22438951 PCBP2 stabilizes the mRNA of STAT1 and STAT2 through binding the 3'Untranslated Region (UTR) of these two molecules. PMID: 22022391 SRp75 inhibits splicing of tau exon 10 by binding to the CA repeat in the intronic splicing silencer downstream of the exon, and requires hnRNPG to exert its full regulatory effect on tau exon 10. PMID: 21723381 study demonstrates the mechanism of the participation of PCBP2 in hepatitis C virus translation and replication PMID: 21632751 Study reports that loss of miR-328 occurs in blast crisis chronic myelogenous leukemia (CML-BC) in a BCR/ABL dose- and kinase-dependent manner through the MAPK-hnRNP E2 pathway. PMID: 20211135 The authors established that the 5'CL-PCBP complex is required for optimal poliovirus viral RNA translation and identified the KH3 domain of PCBP2 as the functional region. PMID: 19945132 specific PCBP2 domains may have distinct roles for differential picornavirus template utilization during viral translation and RNA replication PMID: 12414943 Data suggest that poly(C)-binding protein 2 KH domain 1 interactions with telomeric DNA and telomerase RNA may be involved in the regulation of telomere/telomerase functions. PMID: 15331611 PCBP2 KH1 binds to C-rich strand of human telomeric DNA, indicating that that PCBPs may participate in mechanisms involved in the regulation of telomere/telomerase functions PMID: 16186123 2',5'-oligoadenylate synthetase activation may occur in prostate cancer cells stimulated by cellular mRNAs for PCBP2. PMID: 17145707 Downregulation of HnRNP E2 is associated with oral cancer PMID: 17219427 molecular model of the interaction of the third KH domain of human poly(C)-binding protein-2 in complex with a C-rich strand of human telomeric DNA. PMID: 17426136 Crystal structures of PCBP2 KH1 domain in complex with a 12-nucleotide DNA corresponding to two repeats of the human C-rich strand telomeric DNA and its RNA equivalent. PMID: 17526645 Study shows that through the loss of the KH3 domain, and therefore loss of its ability to function in translation, PCBP2 can mediate the switch from viral translation to RNA replication. PMID: 17581994 The interaction of PCBP2 with RNA target sequences at the 5' end of the coxsackievirus B3 genome was investigated. PMID: 18086560 PCBP2 may be involved in stress-induced remodeling of mRNP complexes and that it may also play a role in the rapid transition of certain silenced mRNAs into a translationally active state. PMID: 18174314 Using a novel protein-RNA tethering system, We establish PCBP2 as an essential co-factor in the initiation of poliovirus negative-strand synthesis. PMID: 18252259 The authors showed that the PCBP2 linker domain modulates binding to poliovirus stem-loop IV RNA via a mechanism that is not inhibited by the antibody. PMID: 18656221 SIN1 and PCBP2 are generally coregulated with large numbers of genes implicated in both cell survival and death and in cellular stress responses, including RNA translation and processing PMID: 18687895 analysis of the human poly(C)-binding protein containing the first and second KH domains reveals insights into its regulatory mechanisms PMID: 18701464 The data demonstrate interaction of isolated PCBP2 KH1 and KH3 domains to four distinct target sites within the 5'-nontranslated region of the CVB3 genomic RNA. PMID: 18929541 Results establish the compositional diversity among P-bodies, and that PCBP2, probably in complex with other mRNP factors, may dynamically recognize such differences and accumulate to specific P-bodies. PMID: 19230839 PCBP2-AIP4 axis defines a new signaling cascade for MAVS degradation and 'fine tuning' of antiviral innate immunity. PMID: 19881509 validated occurrence of an unusual TG 3' splice site in intron 7 PMID: 17672918

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.