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>   首页   >   产品   >   一抗   >   癌症   >   RNF139 Antibody (C-Term)   

RNF139 Antibody (C-Term)

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - RNF139 Antibody (C-Term) AP21873b
    All lanes : Anti-RNF139 Antibody (C-Term) at 1:2000 dilution Lane 1: Caki-1 whole cell lysate Lane 2: human brain lysate Lane 3: human heart lysate Lane 4: human kidney lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 76 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession Q8WU17
Other Accession Q5RBT7
Reactivity Human, Mouse
Host Rabbit
Clonality polyclonal
Isotype Rabbit IgG
Calculated MW 75994 Da
Additional Information
Gene ID 11236
Other Names E3 ubiquitin-protein ligase RNF139, 632-, RING finger protein 139, Translocation in renal carcinoma on chromosome 8 protein, RNF139 (HGNC:17023)
Target/Specificity This RNF139 antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 604-636 amino acids from human RNF139.
Dilution WB~~1:2000
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain 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.
PrecautionsRNF139 Antibody (C-Term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name RNF139 (HGNC:17023)
Function E3-ubiquitin ligase; acts as a negative regulator of cell proliferation through mechanisms involving G2/M arrest and cell death (PubMed:10500182, PubMed:12032852, PubMed:17016439). Required for MHC class I ubiquitination in cells expressing the cytomegalovirus protein US2 before dislocation from the endoplasmic reticulum (ER) (PubMed:19720873). Affects SREBP processing by hindering the SREBP-SCAP complex translocation from the ER to the Golgi, thereby reducing SREBF2 target gene expression (PubMed:19706601, PubMed:20068067). Involved in the sterol-accelerated degradation of HMGCR (PubMed:22143767, PubMed:23223569). This is achieved through binding of RNF139 to INSIG1 and/or INSIG2 at the ER membrane (PubMed:22143767). In addition, interaction of RNF139 with AUP1 facilitates interaction of RNF139 with ubiquitin-conjugating enzyme UBE2G2 and ubiquitin ligase AMFR, leading to ubiquitination of HMGCR (PubMed:23223569). The ubiquitinated HMGCR is then released from the ER into the cytosol for subsequent destruction (PubMed:22143767, PubMed:23223569). Required for INSIG1 ubiquitination (PubMed:20068067). May be required for EIF3 complex ubiquitination (PubMed:20068067).
Cellular Location Endoplasmic reticulum membrane; Multi-pass membrane protein
Tissue Location Highly expressed in testis, placenta and adrenal gland. Moderate expression in heart, brain, liver, skeletal muscle and pancreas, and low expression in lung and kidney
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

E3-ubiquitin ligase; acts as a negative regulator of the cell proliferation through mechanisms involving G2/M arrest and cell death. Required for MHC class I ubiquitination in cells expressing the cytomegalovirus protein US2 before dislocation from the endoplasmic reticulum (ER). Affects SREBP processing by hindering the SREBP/SCAP complex translocation from the ER to the Golgi, thereby reducing SREBF2 target gene expression. Required for INSIG1 ubiquitination. May be required for EIF3 complex ubiquitination. May function as a signaling receptor.

REFERENCES

Gemmill R.M.,et al.Proc. Natl. Acad. Sci. U.S.A. 95:9572-9577(1998).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
Lorick K.L.,et al.Proc. Natl. Acad. Sci. U.S.A. 96:11364-11369(1999).
Gemmill R.M.,et al.Oncogene 21:3507-3516(2002).

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