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Key Documents

R5653

Sigma-Aldrich

Monoclonal Anti-hnRNP-Q antibody produced in mouse

clone 18E4, purified immunoglobulin, buffered aqueous solution

Synonyme(s) :

Anti-Heterogeneous Nuclear Ribonucleoprotein-Q

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

18E4, monoclonal

Forme

buffered aqueous solution

Poids mol.

antigen 55-70 kDa

Espèces réactives

mouse, bovine, human, rat, canine, Xenopus, chicken

Technique(s)

immunohistochemistry: suitable
immunoprecipitation (IP): suitable
indirect ELISA: suitable
microarray: suitable
western blot: 1-2 μg/mL using HeLa total cell extract

Isotype

IgG1

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... SYNCRIP(10492)

Description générale

Monoclonal Anti-hnRNP-Q (mouse IgG1) is derived from the 18E4 hybridoma produced by the fusion of murine myeloma cells (SP2/0 cells) and splenocytes from BALB/c mice immunized with recombinant human hnRNP-Q. Heterogeneous nuclear ribonucleoproteins-Q (hnRNP-Q) family of proteins consist of three proteins (Q1, 2, and 3) that are derived by alternative splicing from the same gene.

Spécificité

The hnRNP-Q and hnRNP-R antibodies share 83% homology.

Immunogène

recombinant human hnRNP-Q.

Application

Monoclonal Anti-hnRNP-Q antibody produced in mouse has been used in immunoblotting and immunofluorescence. It may be used in enzyme linked immunosorbent assay (ELISA), immunoprecipitation and immunohistochemistry.

Actions biochimiques/physiologiques

Heterogeneous nuclear ribonucleoproteins (hnRNPs) act in several biological activities such as transcription, pre- mRNA processing, cytoplasmic mRNA translation and turnover. These proteins interact with the survival of motor neurons protein (SMN) that is mutated in patients with spinal muscular atrophy (SMA). Immunodepletion of hnRNP-Q proteins and their localization in spliceosomes, indicate their important role in splicing.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Structural determinants of APOBEC3B non-catalytic domain for molecular assembly and catalytic regulation
Xiao X, et al.
Nucleic Acids Research, 45(12), 7494-7506 (2017)
Gain of Additional BIRC3 Protein Functions through xn-3-t6a-UTR-Mediated Protein Complex Formation
Lee SH and Mayr C
Molecular Cell, 74(4), 701-712 (2019)
Z Mourelatos et al.
The EMBO journal, 20(19), 5443-5452 (2001-09-28)
Spinal muscular atrophy (SMA) is a common neurodegenerative disease caused by deletion or loss-of-function mutations of the survival of motor neurons (SMN) protein. SMN is in a complex with several proteins, including Gemin2, Gemin3 and Gemin4, and it plays important
SMN interacts with a novel family of hnRNP and spliceosomal proteins
Mourelatos Z, et al.
The Embo Journal, 20(19), 5443-5452 (2001)
A Membraneless Organelle Associated with the Endoplasmic Reticulum Enables 3'UTR-Mediated Protein-Protein Interactions
Ma W and Mayr C
Cell, 175(6), 1492-1506 (2018)

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