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Merck

P6246

Sigma-Aldrich

Anti-PABP antibody, Mouse monoclonal

clone 10E10, purified from hybridoma cell culture

Sinónimos:

Anti-Poly(A)-Binding Protein

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

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

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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Storage Class

10 - Combustible liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

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
Poly(A) Binding Protein 1 Enhances Cap-Independent Translation Initiation of Neurovirulence Factor from Avian Herpesvirus
Abdessamad T
PLoS ONE (2014)
BTG2 bridges PABPC1 RNA-binding domains and CAF1 deadenylase to control cell proliferation
Stupfler B, et al.
Nature Communications, 7, 10811-10811 (2016)
Poly (A)-binding proteins: multifunctional scaffolds for the post-transcriptional control of gene expression
Brook M and Gray NK
Genome Biology, 4(7), 223-223 (2003)
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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