HNRNPC Recombinant Monoclonal Antibody

Code CSB-RA010605A0HU
Size US$210
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  • Western Blot
    Positive WB detected in: Hela whole cell lysate, 293 whole cell lysate, JK whole cell lysate, Raji whole cell lysate, MCF7 whole cell lysate
    All lanes: HNRNPC antibody at 1:1000
    Secondary
    Goat polyclonal to rabbit IgG at 1/50000 dilution
    Predicted band size: 34, 33, 36, 28 kDa
    Observed band size: 42 kDa
  • IHC image of CSB-RA010605A0HU diluted at 1:300 and staining in paraffin-embedded human braintissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a Goat anti-rabbit polymer IgG labeled by HRP and visualized using 0.05% DAB. Secondary antibody only control: uses 1% BSA instead of primary antibody
  • IHC image of CSB-RA010605A0HU diluted at 1:300 and staining in paraffin-embedded human breast cancer performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a Goat anti-rabbit polymer IgG labeled by HRP and visualized using 0.05% DAB. Secondary antibody only control: uses 1% BSA instead of primary antibody
  • IHC image of CSB-RA010605A0HU diluted at 1:300 and staining in paraffin-embedded human kidney tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a Goat anti-rabbit polymer IgG labeled by HRP and visualized using 0.05% DAB. Secondary antibody only control: uses 1% BSA instead of primary antibody
  • Immunofluorescence staining of Hela cell with CSB-RA010605A0HU at 1:30, counter-stained with DAPI. The cells were fixed in 4% formaldehyde and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4C. The secondary antibody was Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L).
  • Immunofluorescence staining of Hela cell with 5% goat serum, counter-stained with DAPI. The cells were fixed in 4% formaldehyde and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4C. The secondary antibody was Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L).
  • Immunofluorescence staining of HepG2 cell with CSB-RA010605A0HU at 1:30, counter-stained with DAPI. The cells were fixed in 4% formaldehyde and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4C. The secondary antibody was Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L).
  • Immunofluorescence staining of HepG2 cell with 5% goat serum, counter-stained with DAPI. The cells were fixed in 4% formaldehyde and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4C. The secondary antibody was Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L).
  • Overlay Peak curve showing MCF7 cells stained with CSB-RA010605A0HU (red line) at 1:50. The cells were fixed in 4% formaldehyde and permeated by 0.2% TritonX-100. Then 10% normal goat serum to block non-specific protein-protein interactions followed by the antibody (1ug/1*106cells) for 45min at 4℃. The secondary antibody used was FITC-conjugated Goat Anti-rabbit IgG(H+L) at 1:200 dilution for 35min at 4℃.Control antibody (green line) was Rabit IgG (1ug/1*106cells) used under the same conditions. Acquisition of >10,000 events was performed.
  • Immunoprecipitating HNRNPC in Hela whole cell lysate
    Lane 1: Rabbit control IgG instead of CSB-RA010605A0HU  in Hela whole cell lysate.  Lane 2:CSB-RA010605A0HU(3µg)+ Hela whole cell lysate(500µg)
    Lane 3: Hela whole cell lysate(20µg)
    For western blotting, Goat polyclonal to rabbit IgG antibody was used as the secondary antibody (1/50000)
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Product Details

Uniprot No.
Target Names
HNRNPC
Alternative Names
C1 antibody; C2 antibody; Heterogeneous nuclear ribonucleoprotein C (C1/C2) antibody; Heterogeneous nuclear ribonucleoprotein C antibody; Heterogeneous nuclear ribonucleoproteins C1/C2 antibody; HNRNP antibody; hnRNP C1 / hnRNP C2 antibody; hnRNP C1/C2 antibody; Hnrnpc antibody; HNRPC antibody; HNRPC_HUMAN antibody; MGC104306 antibody; MGC105117 antibody; MGC117353 antibody; MGC131677 antibody; Nuclear ribonucleoprotein particle C1 protein antibody; Nuclear ribonucleoprotein particle C2 protein antibody; SNRPC antibody
Species Reactivity
Human
Immunogen
A synthesized peptide derived from human HNRNPC
Immunogen Species
Homo sapiens (Human)
Conjugate
Non-conjugated
Clonality
Monoclonal
Isotype
Rabbit IgG
Clone No.
9G1
Purification Method
Affinity-chromatography
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Form
Liquid
Tested Applications
ELISA, WB, IHC, IF, FC, IP
Recommended Dilution
Application Recommended Dilution
WB 1:500-1:5000
IHC 1:200-1:500
IF 1:20-1:200
IP 1:200-1:1000
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Description

CUSABIO administered a human HNRNPC-derived peptide to an animal to elicit an immune response. B cells were subsequently isolated from the immunized animal and fused with myeloma cells, generating hybridoma cells. Through screening, a single hybridoma cell clone that produces the desired HNRNPC-specific antibody was identified and selected. RNA was extracted from the chosen hybridoma cells, and the variable regions of the HNRNPC antibody's heavy and light chains were isolated and amplified using reverse transcription PCR. These amplified HNRNPC antibody variable regions were then cloned into an expression vector and transfected into a host cell line for expression purposes. The resulting HNRNPC recombinant monoclonal antibodies were purified from the cell culture supernatant using affinity chromatography. Six applications including ELISA, WB, IHC, IF, FC, and IP were employed to confirm the binding specificity and affinity of this antibody. Notably, this antibody exhibits recognition specifically for human HNRNPC protein.

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Target Background

Function
Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. N6-methyladenosine (m6A) has been shown to alter the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch', facilitating binding of HNRNPC, leading to regulation of mRNA splicing.
Gene References into Functions
  1. APP levels then decrease progressively as a function of age in close relationship with the gradual normalization of FMRP and hnRNP C levels. PMID: 26048669
  2. Endoplasmic reticulum resident chaperone GRP78, mitochondrial protein Prohibitin and heterogeneous nuclear ribonucleoprotein hnRNPC (C1/C2) have been shown to interact with viral RNA. Hence it is proposed that these are the principle candidates governing endoplasmic reticulum stress-induced apoptosis in JEV infection. PMID: 28102850
  3. Our results indicate that a balance between lncRNA SNHG1 and hnRNPC regulates p53 activity and p53-dependent apoptosis upon doxorubicin treatment, and further indicate that a change in lncRNA subcellular localization under specific circumstances is biologically significant. PMID: 28264987
  4. These data suggest an interplay between CELF2 and hnRNP C as the mechanistic basis for activation-dependent alternative splicing of TRAF3 exon 8. PMID: 28031331
  5. These data indicate that hnRNPC1/C2 binds to both DNA and RNA and influences both gene expression and RNA splicing, but these actions do not appear to be linked through 1,25(OH)2D-mediated induction of transcription. PMID: 27672039
  6. These findings suggest that hnRNP C1/C2 is involved in dengue virus replication at the stage of viral RNA synthesis. PMID: 25890165
  7. HnRNP C, YB-1 and hnRNP L coordinately enhance skipping of human MUSK exon 10 to generate a Wnt-insensitive MuSK isoform. PMID: 25354590
  8. Our results suggested that hnRNP C1 controls HPV16 late gene expression. PMID: 25878250
  9. m(6)A-switch-regulated HNRNPC-binding activities affect the abundance as well as alternative splicing of target mRNAs, demonstrating the regulatory role of m(6)A-switches on gene expression and RNA maturation PMID: 25719671
  10. PTBP1 and hnRNP C repress exon 3 inclusion, and that downregulation of PTBP1 inhibited BIM-mediated apoptosis. PMID: 24743263
  11. down-regulation of MALAT-1 expression compromised the cytoplasmic translocation of hnRNP C in the G2/M phase and resulted in G2/M arrest PMID: 23973260
  12. Heterogeneous nuclear ribonucleoprotein C is a key regulator of BRCA gene expression and homologous recombination-based DNA repair. PMID: 23585894
  13. By preventing U2AF65 binding to Alu elements, hnRNP C plays a critical role as a genome-wide sentinel protecting the transcriptome. PMID: 23374342
  14. The data indicated that hnRNPC controls the aggressiveness of glioblastoma cells through the regulation of PDCD4. Silencing of hnRNPC lowered miR-21 levels, in turn increasing the expression of PDCD4, suppressing Akt and p70S6K activation. PMID: 22907752
  15. p27kip1 upregulated by hnRNPC1/2 antagonizes CagA-mediated pathogenesis. PMID: 22404445
  16. study shows mechanism by which Pol II transcripts are classified according to length; heterotetramer of hnRNP C1/C2 measures the length of the transcripts like a molecular ruler, by binding to unstructured RNA regions longer than 200 to 300 nucleotides PMID: 22461616
  17. One of the identified proteins, hnRNPC, was found to interact with small hepatitis delta virus antigen in vitro and in vivo in human liver cells. PMID: 21774814
  18. Studies indicated that DDX21, HNRNPC, and RCC2 were isolated from Ku86 multicomponent complex in response to DNA damage. PMID: 20873769
  19. HNRNP C recognizes uridine tracts with a defined long-range spacing consistent with HNRNP particle organization. PMID: 20601959
  20. FMRP represses translation by recruiting APP mRNA to processing bodies, whereas hnRNP C promotes APP translation by displacing FMRP, thereby relieving the translational block. PMID: 20473314
  21. The authors report here that the 5' end of poliovirus negative-strand RNA is capable of interacting with endogenous hnRNP C, as well as with poliovirus nonstructural proteins. PMID: 20164237
  22. The authors propose that hnRNP C interacts with poliovirus RNA and replication proteins to increase the efficiency of viral genomic RNA synthesis. PMID: 20189623
  23. phosphorylation of heterogeneous nuclear ribonucleoprotein C1/C2 in response to physiologic levels of hydrogen peroxide in endothelial cells PMID: 11877401
  24. nuclear ribonucleoproteins C1 and C2 are part of the RNP complex that forms on XIAP IRES, the cellular levels of hnRNPC1 and -C2 parallel the activity of XIAP IRES and the overexpression of hnRNPC1-C2 specifically enhanced translation of XIAP IRES PMID: 12482981
  25. hnRNP C, via internal ribosomal entry site binding, modulates translation of c-myc mRNA in a cell cycle phase-dependent manner PMID: 12509468
  26. the acidic C-terminal domain of hnRNP-C1/C2 could be a regulatory domain and may play an important role in the regulation of mRNA binding by hnRNP-C1/C2. PMID: 12564933
  27. a novel nuclear export is activated by the ROCK signaling pathway to exclude hnRNP C1/C2 from nucleus, by which the compartmentalization of specific hnRNP components is disturbed in apoptotic cells PMID: 15494373
  28. CK1alpha-mediated phosphorylation modulates the mRNA binding ability of hnRNP-C PMID: 15687492
  29. findings suggest that hnRNP C1 has a role in positive-strand RNA synthesis in poliovirus-infected cells, possibly at the level of initiation PMID: 15731220
  30. upstream element in human papillomavirus type 16 interacted specifically with CstF-64, hnRNP C1/C2 & polypyrimidine tract binding protein, suggesting these factors were enhancing or regulating polyadenylation at the HPV-16 early polyadenylation signal PMID: 15767428
  31. Direct in vivo interaction of hnRNPC with the urokinase receptor mRNA 3'UTR was demonstrated. PMID: 16010978
  32. Results describe the purification of a locus control region-associated remodeling complex consisting of heterogeneous nuclear ribonucleoprotein C1/C2, SWI/SNF, and MeCP1 as a single homogeneous complex. PMID: 16217013
  33. These results demonstrate that hnRNP C1/C2 is involved in maintenance of cellular homeostasis besides cellular differentiation and proliferation. PMID: 16960656
  34. in addition to its RNA-processing functions, hnRNP C1/C2 may be a key determinant of the temporal patterns of VDRE occupancy PMID: 17071612
  35. regulation of IRES-mediated translation by hnRNP C1/C2 and Unr might be important in mitosis PMID: 17159903
  36. A novel cis-element in the 5' coding region of p53 mRNA and its interaction with heterogeneous nuclear ribonucleoprotein (hnRNP)C1/C2, is described. PMID: 18296503
  37. Intracellular NS1 protein of dengue virus interacts with hnRNP C1/C2. PMID: 18471994
  38. The RNA binding domain of heterogeneous nuclear ribonuclear protein C binds and stabilizes urokinase-type plasminogen activator receptor (uPAR) mRNA, attributing the key role of this domain in hnRNPC-mediated uPAR regulation in lung epithelial cells. PMID: 18494499
  39. The H(2)O(2) responsive pre-mRNA binding protein hnRNP-C is up-regulated in atherosclerosis. PMID: 18508286
  40. anti-hnRNP C1/C2 antibody hampered splicing of SMN1 exon 7, but did not affect splicing of SMN2 exon 7 PMID: 19628962
  41. endogenous hnRNP C and PTEN interact and co-localize within the nucleus PMID: 19740742
  42. This protein has been found differentially expressed in the Wernicke's Area from patients with schizophrenia. PMID: 19405953

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Subcellular Location
Nucleus. Note=Component of ribonucleosomes.
Protein Families
RRM HNRPC family, RALY subfamily
Database Links

HGNC: 5035

OMIM: 164020

KEGG: hsa:3183

STRING: 9606.ENSP00000319690

UniGene: Hs.508848

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