PNN Antibody (Center)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
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Application ![]()
| WB, IHC-P, IF, E |
---|---|
Primary Accession | Q9H307 |
Other Accession | O35691, P79122, NP_002678.2 |
Reactivity | Human |
Predicted | Bovine, Mouse |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 81628 Da |
Antigen Region | 209-239 aa |
Gene ID | 5411 |
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Other Names | Pinin, 140 kDa nuclear and cell adhesion-related phosphoprotein, Desmosome-associated protein, Domain-rich serine protein, DRS protein, DRSP, Melanoma metastasis clone A protein, Nuclear protein SDK3, SR-like protein, PNN, DRS, MEMA |
Target/Specificity | This PNN antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 209-239 amino acids from the Central region of human PNN. |
Dilution | WB~~1:250 IHC-P~~1:100~500 IF~~1:10~50 E~~Use at an assay dependent concentration. |
Format | Purified polyclonal antibody supplied in PBS with 0.05% (V/V) Proclin 300. This antibody is purified through a protein A column, followed by peptide affinity purification. |
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 | PNN Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | PNN |
---|---|
Synonyms | DRS, MEMA |
Function | Transcriptional activator binding to the E-box 1 core sequence of the E-cadherin promoter gene; the core-binding sequence is 5'CAGGTG-3'. Capable of reversing CTBP1-mediated transcription repression. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Participates in the regulation of alternative pre-mRNA splicing. Associates to spliced mRNA within 60 nt upstream of the 5'-splice sites. Component of the PSAP complex which binds RNA in a sequence-independent manner and is proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. Involved in the establishment and maintenance of epithelia cell-cell adhesion. Potential tumor suppressor for renal cell carcinoma. |
Cellular Location | Nucleus speckle. Cell junction, desmosome. Note=Cell-cell contact area, predominantly desmosome of intercellular adherens junction. Not a nucleocytoplasmic shuttling protein |
Tissue Location | Expressed in placenta, lung, liver, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon, heart, epidermis, esophagus, brain and smooth and skeletal muscle. Expressed strongly in melanoma metastasis lesions and advanced primary tumors. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Transcriptional activator binding to the E-box 1 core sequence of the E-cadherin promoter gene; the core-binding sequence is 5'CAGGTG-3'. Capable of reversing CTBP1-mediated transcription repression. Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Participates in the regulation of alternative pre-mRNA splicing. Associates to spliced mRNA within 60 nt upstream of the 5'-splice sites. Involved in the establishment and maintenance of epithelia cell-cell adhesion. Potential tumor suppressor for renal cell carcinoma.
REFERENCES
Bailey, S.D., et al. Diabetes Care (2010) In press :
Talmud, P.J., et al. Am. J. Hum. Genet. 85(5):628-642(2009)
Alpatov, R., et al. Mol. Cell. Biol. 28(5):1584-1595(2008)
Sugiyama, N., et al. Mol. Cell Proteomics 6(6):1103-1109(2007)
Matsuoka, S., et al. Science 316(5828):1160-1166(2007)

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