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Merck
CN

SAB4200006

Anti-TDP-43 (N-terminal region) antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

别名:

Anti-ALS10, Anti-TARDBP, Anti-TARDP43, Anti-Tar DNA binding protein 43

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关于此项目

NACRES:
NA.41
UNSPSC Code:
12352203
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产品名称

Anti-TDP-43 (N-terminal region) antibody produced in rabbit, ~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~43 kDa

species reactivity

mouse, human

concentration

~1.0 mg/mL

technique(s)

immunohistochemistry: 5-10 μg/mL using human or mouse kidney
indirect immunofluorescence: 5-10 μg/mL using HepG2 cells
western blot: 1.5-3.0 μg/mL using HepG2 cell lysates

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... TARDBP(23435)
mouse ... Tardbp(230908)

Application

Anti-TDP-43 (N-terminal region) antibody produced in rabbit has been used in:
  • immunoblotting
  • immunofluorescence
  • immunohistochemistry
  • immunuprecipitation

Biochem/physiol Actions

TDP-43 is also involved in mediating the transcription regulation of human immune deficiency virus (HIV). TDP-43 has been identified as the major ubiquinated component of cytoplasmic inclusions in frontotemporal lobe degeneration subtype FTLD-U and amyotrophic lateral sclerosis (ALS). Pathological TDP-43 forms abnormal inclusions in neuronal perikarya and neurites, indicating that redistribution of TDP-43 to the cytoplasm is a pathogenic mechanism. Several pathogenic TDP43 mutations have been identified in familial ALS, causing aberrant cleavage of TDP-43 to C-terminal fragments, and predisposing nuclear TDP-43 to redistribute to the cytoplasm and form pathological aggregates. Abnormal phosphorylation of TDP-43 at Ser409/410 has also been observed in frontotemporal lobar degeneration and amyotrophic lateral sclerosis (FTLD-U and ALS) suggesting a toxic gain of function leading to apoptosis.

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.

General description

TDP-43 (TAR DNA binding protein, TARDP) belongs to the family of heterogeneous nuclear ribonucleoproteins (hnRNPs) that bind single stranded RNA. TDP-43 is predominantly localized to the nucleus.

Physical form

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

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存储类别

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

常规特殊物品
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历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Carlo Scialò et al.
Brain communications, 2(2), fcaa142-fcaa142 (2020-10-24)
The pathological deposition of the transactive response DNA-binding protein of 43 kDa occurs in the majority (∼97%) of amyotrophic lateral sclerosis and in around 45% of frontotemporal lobar degeneration cases. Amyotrophic lateral sclerosis and frontotemporal lobar degeneration clinically overlap, presenting a
Cross-regulation between TDP-43 and paraspeckles promotes pluripotency-differentiation transition
Modic M, et al.
Molecular Cell (2019)
TDP-43 loss of function inhibits endosomal trafficking and alters trophic signaling in neurons
Schwenk BM, et al.
The Embo Journal, 35(21), 2350-2370 (2016)
Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity
Zhang YJ, et al.
Proceedings of the National Academy of Sciences of the USA, 106(18), 7607-7612 (2009)
TDP-43 deposition in prospectively followed, cognitively normal elderly individuals: correlation with argyrophilic grains but not other concomitant pathologies
Arnold, Stacy J and Dugger, Brittany N and Beach, Thomas G
Acta Neuropathologica, 126(1), 51-57 (2013)

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