P6246
Anti-PABP antibody, Mouse monoclonal
clone 10E10, purified from hybridoma cell culture
Synonyme(s) :
Anti-Poly(A)-Binding Protein
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A propos de cet article
Conjugate:
unconjugated
Clone:
10E10, monoclonal
Application:
ARR, ICC, IP, WB
Citations:
19
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Laissez-nous vous aiderantibody product type
primary antibodies
biological source
mouse
conjugate
unconjugated
antibody form
purified from hybridoma cell culture
clone
10E10, monoclonal
form
buffered aqueous solution
mol wt
antigen ~69 kDa
species reactivity
hamster, canine, bovine, Xenopus, human, monkey
technique(s)
immunocytochemistry: suitable, immunoprecipitation (IP): suitable, microarray: suitable, western blot: 0.5-1 μg/mL using whole cell extracts of HEK 293T cells
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... PABPC1(26986)
General description
Monoclonal Anti-PABP (mouse IgG1 isotype) is derived from the 10E10 hybridoma produced by the fusion of mouse myeloma cells (SP2/0) and splenocytes from BALB/c mice immunized with recombinant human PABP. Poly(A) binding protein (PABP) is highly conserved between different organisms especially at the amino-terminal region of the protein that contains four RNA-binding domains (RBDs).
Poly(A) binding protein (PABP) possesses RNA recognition motifs (RRMs), a proline-rich region and a PABP C-terminal domain. The gene encoding this protein is localized on human chromosome 8q22.3.
Immunogen
recombinant human PABP.
Application
Monoclonal Anti-PABP antibody produced in mouse has been used for immunofluorescence.
Monoclonal Anti-PABP antibody produced in mouse has been used in:
- Immunoblotting
- Immunostaining
- Immunoprecipitation
- Enzyme linked immunosorbent assay(ELISA)
- Immunocytochemistry
Biochem/physiol Actions
Poly(A) binding protein (PABP) has a role in mRNA translation and stability. It modulates gene expression. The protein binds to the poly(A) tail, bridges the ends of mRNA and forms a closed loop. This might help in translation initiation by promoting ribosome recruitment.
Poly(A) binding protein (PABP) is found in excess, relative to the amount of cytoplasmic poly(A) (three fold) and binds to its poly(A) target at high affinity (Kd of 7nM). The eukaryotic initiation factor, EIF4F complex, interacts with PABP indirectly via the PAIP-1 protein (PABP-interacting protein-1). As a consequence, an interaction between the 5′ and 3′ ends of mRNA occurs. This proximity between the mRNA ends contributes to its stability and enhances translation, since terminating ribosomes may start translation again.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, and 15 mM sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Classe de stockage
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
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An integrative approach to identify YB-1-interacting proteins required for cisplatin resistance in MCF7 and MDA-MB-231 breast cancer cells
Chantal Garand
Cancer Science (2011)
RNA UK 2012: The role of mammalian poly(A)-binding proteins in co-ordinating mRNA turnover
Brook M and Gray NK
Biochemical Society Transactions, 40(Pt 4), 856-856 (2012)
Hun-Way Hwang et al.
Cell reports, 15(2), 423-435 (2016-04-07)
Accurate and precise annotation of 3' UTRs is critical for understanding how mRNAs are regulated by microRNAs (miRNAs) and RNA-binding proteins (RBPs). Here, we describe a method, poly(A) binding protein-mediated mRNA 3' end retrieval by crosslinking immunoprecipitation (PAPERCLIP), that shows
BTG2 bridges PABPC1 RNA-binding domains and CAF1 deadenylase to control cell proliferation
Stupfler B, et al.
Nature Communications, 7, 10811-10811 (2016)
Molecular dynamics of FMRP and other RNA-binding proteins in MEG-01 differentiation: the role of mRNP complexes in non-neuronal development
Marie McCoy
Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire (2016)
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