HNRPQ Antibody (Center)
Purified Rabbit Polyclonal Antibody (Pab)
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- 文献引用 : 1
- 实验流程
- 背景知识
Application
| WB, IHC-P, FC, E |
|---|---|
| Primary Accession | O60506 |
| Other Accession | Q7TP47, Q7TMK9 |
| Reactivity | Human |
| Predicted | Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 69603 Da |
| Antigen Region | 392-420 aa |
| Gene ID | 10492 |
|---|---|
| Other Names | Heterogeneous nuclear ribonucleoprotein Q, hnRNP Q, Glycine- and tyrosine-rich RNA-binding protein, GRY-RBP, NS1-associated protein 1, Synaptotagmin-binding, cytoplasmic RNA-interacting protein, SYNCRIP, HNRPQ, NSAP1 |
| Target/Specificity | This HNRPQ antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 392-420 amino acids from the Central region of human HNRPQ. |
| Dilution | WB~~1:1000 IHC-P~~1:100~500 FC~~1:10~50 E~~Use at an assay dependent concentration. |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | HNRPQ Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | SYNCRIP |
|---|---|
| Synonyms | HNRPQ, NSAP1 |
| Function | Heterogenous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD-mediated complex that promotes MYC mRNA stability. Isoform 1, isoform 2 and isoform 3 are associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Isoform 1 binds to apoB mRNA AU-rich sequences. Isoform 1 is part of the APOB mRNA editosome complex and may modulate the postranscriptional C to U RNA-editing of the APOB mRNA through either by binding to A1CF (APOBEC1 complementation factor), to APOBEC1 or to RNA itself. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Interacts in vitro preferentially with poly(A) and poly(U) RNA sequences. Isoform 3 may be involved in cytoplasmic vesicle-based mRNA transport through interaction with synaptotagmins. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation assembles into the GAIT complex which binds to stem loop- containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation; seems not to be essential for GAIT complex function. |
| Cellular Location | Cytoplasm. Microsome {ECO:0000250|UniProtKB:Q7TMK9} Endoplasmic reticulum. Nucleus {ECO:0000250|UniProtKB:Q7TMK9}. Note=The tyrosine phosphorylated form bound to RNA is found in microsomes (By similarity). Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity). {ECO:0000250|UniProtKB:O43390, ECO:0000250|UniProtKB:Q7TMK9} [Isoform 2]: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q7TMK9}. Note=Expressed predominantly in the nucleoplasm. {ECO:0000250|UniProtKB:Q7TMK9} |
| Tissue Location | Ubiquitously expressed. Detected in heart, brain, pancreas, placenta, spleen, lung, liver, skeletal muscle, kidney, thymus, prostate, uterus, small intestine, colon, peripheral blood and testis. |
Research Areas
For Research Use Only. Not For Use In Diagnostic Procedures.

Application Protocols
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Heterogenous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms.
REFERENCES
Yoo,B.C., Cell. Mol. Life Sci. 66 (2), 350-364 (2009) Chen,H.H., Mol. Cell. Biol. 28 (22), 6929-6938 (2008) Quaresma,A.J., Biochem. Biophys. Res. Commun. 350 (2), 288-297 (2006)
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