ABE1948

Anti-CLIM-1/2 Antibody

Name: Anti-CLIM-1/2 Antibody
Brand: MM

serum, from rabbit

Synonym(s):

LIM domain-binding protein 2, LDB-2, Carboxyl-terminal LIM domain-binding protein 1, CLIM-1, LIM domain-binding factor CLIM1, CLIM-1/2

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About This Item

UNSPSC Code:

12352203

eCl@ss:

32160702

NACRES:

NA.41

biological source

rabbit

Quality Level

100

conjugate

unconjugated

antibody form

serum

antibody product type

primary antibodies

clone

polyclonal

species reactivity

chicken, hamster, human, mouse

technique(s)

ChIP: suitable
immunocytochemistry: suitable
immunofluorescence: suitable
immunohistochemistry: suitable
western blot: suitable

NCBI accession no.

NP_034828

UniProt accession no.

O55203

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... LDB2(9079)

General description

LIM domain-binding protein 1 (UniProt P70662; CLIM-2, LDB-1) encoded by the murine Ldb2 gene (Clim2, Nli; Gene ID 16825) and LIM domain-binding protein 2 (UniProt O55203; CLIM-1, LDB-2, CLP-36) encoded by the murine Ldb2 gene (Clim1; Gene ID 16826) are LIM domain-interacting cofactors whose interaction with LIM homeodomain (LIM-HD) transcription factors are crucial for the development of specific types of interneurons and motor neurons during neural tube development. The ubiquitin ligase RLIM targets CLIM for proteasomal degradation, thereby inhibiting developmental LIM-HD activity.

~50/43 kDa observed. Uncharacterized band(s) may appear in some lysates.

Immunogen

Recombinant protein corresponding to mouse CLIM-1.

Application

This Anti-CLIM-1/2 Antibody is validated for use in Western Blotting, Immunocytochemistry, Chromatin Immunoprecipitation (ChIP), Immunohistochemistry, Immunofluorescence for the detection of CLIM-1/2.

Western Blotting Analysis: A representative lots detected endogenous CLIM1/2 in CHO and murine pituitary gonadotroph Alpha T3 cells, as well as bacterially expressed and in vitro tranlsated recombinant CLIM1/2 (Ostendorff, H.P., et al. (2006). Dev Dyn. 235(3):786-791; Ostendorff, H.P., et al. (2002). Nature. 416(6876):99-103).
Immunocytochemistry Analysis: A representative lot revealed an inverse correlation between the expression level of endogenous CLIM1/2 and that of its negative regulator RLIM in HEK293, CHO, murine pituitary gonadotroph Alpha T3, and chicken ectodermal cells by dual fluorescent immunocytochemistry (Ostendorff, H.P., et al. (2002). Nature. 416(6876):99-103).
Chromatin Immunoprecipitation (ChIP) Analysis: A representative lot detected CLIM1/2 occupancy at the alphaGSU promoter in murine pituitary gonadotroph Alpha T3 cells (Ostendorff, H.P., et al. (2002). Nature. 416(6876):99-103).
Immunohistochemistry Analysis: A representative lot detected similar stage-dependent expression patterns between CLIM1/2 and the ubiquitin ligase RLIM in the developing neural tube during early mouse embryogenesis (Ostendorff, H.P., et al. (2006). Dev Dyn. 235(3):786-791).
Immunofluorescence Analysis: A representative lot revealed highly co-localized expressions of CLIM1/2 and RLIM on thoracic sections from E12.5 mouse embryos by dual fluorescent immunohistochemistry (Ostendorff, H.P., et al. (2006). Dev Dyn. 235(3):786-791).

Biochem/physiol Actions

Reacts with both CLIM1 and CLIM2. Expected to react with all spliced isoforms of CLIM1 (CLIM-1a, CLIM-1b, and isoform 3) & CLIM2 (Visvader-a, Tran-a, Tran-b).

Analysis Note

Evaluated by Western Blotting in E16 embryonic mouse brain tissue lysate.

Western Blotting Analysis: A 1:5,000 dilution of this antibody detected CLIM-1/2 in 10 µg of E16 embryonic mouse brain tissue lysate.

Other Notes

Concentration: Please refer to lot specific datasheet.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Certificates of Analysis (COA)

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Characterization of Estrogen Receptor α Phosphorylation Sites in Breast Cancer Tissue Using the SNAP i.d® 2.0 System

A major focus of breast cancer research is to understand the mechanisms responsible for disease progression and drug resistance. Toward that end, it has been found that approximately two thirds of all human breast carcinomas overexpress the Estrogen Receptor α (ERα) protein and it remains the primary pharmacological target for endocrine therapy1,2. The normal cellular function of ERα is as a transcription factor that mediates a wide variety of physiological processes, many of which are dependent upon phosphorylation of the receptor at specific amino acid residues3,4. Indeed, ERα is known to be phosphorylated at a multitude of different sites, yet how these all correlate to disease remains unclear5. Here, we interrogated multiple sites of ERα for phosphorylation status by screening an extensive panel of different breast cancer patient samples and other non-breast cancer tissue microarray (TMA) slide samples to determine their relevance to disease.

Global Trade Item Number

SKU	GTIN
ABE1948	04055977274820

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