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SAB3701431

Sigma-Aldrich

Monoclonal Anti-Esrp-1/2 antibody produced in mouse

clone 23A7.C9, purified immunoglobulin

Sinónimos:

Anti-Epithelial splicing regulatory protein 1, Anti-RNA-binding motif protein 35A, Anti-RNA-binding protein 35A, Anti-RNA-binding protein 35B, Anti-Rbm35a

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100 μG
MXP 8,313.00

MXP 8,313.00


Fecha estimada de envío14 de abril de 2025



Seleccione un Tamaño

Cambiar Vistas
100 μG
MXP 8,313.00

About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

MXP 8,313.00


Fecha estimada de envío14 de abril de 2025


biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

23A7.C9, monoclonal

form

buffered aqueous solution

species reactivity

mouse

technique(s)

ELISA: suitable
western blot: suitable

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

mouse ... Esrp2(77411)

General description

Epithelial splicing regulatory protein 1 (ESRP1) is a member of RBM family of RNA-binding proteins. It is also known as RBM35A. ESRP1 get highly expressed in both mouse and human epithelial stem cells and weakly expressed in normal pancreatic ductal cells.

Specificity

This antibody was purified from tissue culture supernatant by Protein-A chromatography followed by extensive dialysis against the buffer stated above. This antibody reacts with both mouse Esrp-1 and Esrp-2 proteins.  A BLAST analysis of the immunizing protein sequence shows 100% homology with Esrp-1 from mouse and a 91% sequence homology with Esrp-1 from human, pig, rat, opossum, horse, cattle, panda, dog, and chimpanzee .  The binding epitope of this monoclonal antibody has not been mapped

Immunogen

Full length recombinant mouse Esrp-1 fusion protein.

Biochem/physiol Actions

Epithelial splicing regulatory protein 1 (ESRP1) is essential for the expression of epithelial FGFR2-IIIb (fibroblast growth factor receptor 2). Suppression of ESRP1 can enhance induced pluripotent stem (iPS) cell colony generation. It can also repress cancer cell motility by different mechanisms. ESRP1 modulates splicing of Ras-related C3 botulinum toxin substrate 1 (Rac1) isoforms and participates in the maintenance of epithelial cell-specific isoforms. The protein controls epithelial splicing regulatory network and pluripotency.

Features and Benefits

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Physical form

Supplied in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2 with 0.01% (w/v) 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


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The RNA binding protein ESRP1 fine-tunes the expression of pluripotency-related factors in mouse embryonic stem cells.
Fagoonee S, et al.
PLoS ONE, 8(8), e72300-e72300 (2013)
The epithelial splicing factors ESRP1 and ESRP2 positively and negatively regulate diverse types of alternative splicing events.
Warzecha C C, et al.
RNA Biology, 6(5), 546-562 (2009)
Epithelial splicing regulatory proteins 1 (ESRP1) and 2 (ESRP2) suppress cancer cell motility via different mechanisms.
Ishii H, et al.
The Journal of Biological Chemistry, 289(40), 27386-27399 (2014)
Claude C Warzecha et al.
Molecular cell, 33(5), 591-601 (2009-03-17)
Cell-type-specific expression of epithelial and mesenchymal isoforms of Fibroblast Growth Factor Receptor 2 (FGFR2) is achieved through tight regulation of mutually exclusive exons IIIb and IIIc, respectively. Using an application of cell-based cDNA expression screening, we identified two paralogous epithelial

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