AV41195
Anti-HNRPA3 (AB1) antibody produced in rabbit
IgG fraction of antiserum, lyophilized powder
Synonym(s):
Anti-Heterogeneous Nuclear Ribonucleoprotein A3
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About This Item
UNSPSC Code:
12352203
biological source
rabbit
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
lyophilized powder
mol wt
42 kDa
species reactivity
human, rat, bovine, rabbit, canine, mouse
technique(s)
immunohistochemistry: suitable
western blot: suitable
immunogen sequence
EVKPPPGRPQPDSGRRRRRRGEEGHDPKEPEQLRKLFIGGLSFETTDDSL
NCBI accession no.
storage temp.
−20°C
Gene Information
human ... HNRPA3(220988)
General description
Heterogeneous Nuclear Ribonucleoproteins (hnRNP) are RNA binding proteins that form complexes with heterogeneous nuclear RNA (hnRNA). HnRNPs regulate pre-mRNA processing, metabolism and nuclear cytoplasmic shuttling. Specific HnRNPs have unique nucleic acid binding properties. Heterogeneous Nuclear Ribonucleoprotein A3 interacts with the regulatory region of Hoxc8 gene, which is involved in the regulation of the anterior-posterior axis in developing embryos.
Specificity
Anti-HNRPA3 (AB1) polyclonal antibody reacts with canine, human, mouse, rat, and bovine Heterogeneous Nuclear Ribonucleoprotein A3 proteins.
Immunogen
synthetic peptide corresponding to a region of human HNRPA3 with an internal ID of P22570
Application
Anti-HNRPA3 (AB1) polyclonal antibody is used to tag the heterogeneous nuclear ribonucleoprotein A3 for detection and quantitation by Western blotting and in plasma by immunohistochemical (IHC) techniques. It is used as a probe to determine the roles of heterogeneous nuclear ribonucleoprotein A3 in processes such as embryogenesis.
Physical form
Lyophilized from PBS buffer with 2% sucrose
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
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Yvonne S Davidson et al.
Acta neuropathologica communications, 5(1), 31-31 (2017-04-23)
Frontotemporal Lobar Degeneration (FTLD) encompasses certain related neurodegenerative disorders which alter behaviour, personality and language. Heterogeneous ribonuclear proteins (hnRNPs) maintain RNA metabolism and changes in their function may underpin the pathogenesis of FTLD. Immunostaining for hnRNP A1, A2/B1 and A3
Kohji Mori et al.
EMBO reports, 17(9), 1314-1325 (2016-07-28)
Intronic hexanucleotide (G4C2) repeat expansions in C9orf72 are genetically associated with frontotemporal lobar degeneration (FTLD) and amyotrophic lateral sclerosis (ALS). The repeat RNA accumulates within RNA foci but is also translated into disease characterizing dipeptide repeat proteins (DPR). Repeat-dependent toxicity
Yang Li et al.
Brain research, 1647, 79-93 (2016-03-17)
The pathological accumulation of RNA-binding proteins (RBPs) within inclusion bodies is a hallmark of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). RBP aggregation results in both toxic gain and loss of normal function. Determining the protein binding partners
Steven Boeynaems et al.
Scientific reports, 6, 20877-20877 (2016-02-13)
Hexanucleotide repeat expansions in C9orf72 are the most common cause of amyotrophic lateral sclerosis (ALS) and frontotemporal degeneration (FTD) (c9ALS/FTD). Unconventional translation of these repeats produces dipeptide repeat proteins (DPRs) that may cause neurodegeneration. We performed a modifier screen in
Yoshihiro Nihei et al.
Acta neuropathologica, 139(1), 99-118 (2019-10-24)
Repeat expansion in C9orf72 causes amyotrophic lateral sclerosis and frontotemporal lobar degeneration. Expanded sense and antisense repeat RNA transcripts in C9orf72 are translated into five dipeptide-repeat proteins (DPRs) in an AUG-independent manner. We previously identified the heterogeneous ribonucleoprotein (hnRNP) A3
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