Skip to Content
Merck
All Photos(1)

Documents

R5653

Sigma-Aldrich

Monoclonal Anti-hnRNP-Q antibody produced in mouse

clone 18E4, purified immunoglobulin, buffered aqueous solution

Synonym(s):

Anti-Heterogeneous Nuclear Ribonucleoprotein-Q

Sign Into View Organizational & Contract Pricing
All Photos(1)

About This Item

MDL number:
MFCD03845440
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

18E4, monoclonal

form

buffered aqueous solution

mol wt

antigen 55-70 kDa

species reactivity

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

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SYNCRIP(10492)

General description

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.

Specificity

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

Immunogen

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.

Biochem/physiol Actions

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.

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.

Not finding the right product?  

Try our Product Selector Tool.

Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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)
View All Related Papers

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service