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Merck

ABC481

Anti-Cytosolic 5′-nucleotidase II Antibody

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O této položce

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Conjugate:
unconjugated
Clone:
polyclonal
Application:
IHC, WB
Citations:
-
Technický servis
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conjugate

unconjugated

Quality Level

antibody form

affinity purified immunoglobulin

clone

polyclonal

purified by

affinity chromatography

species reactivity

rabbit, human

concentration

(Please refer to lot specific datasheet.)

technique(s)

immunohistochemistry: suitable, western blot: suitable

UniProt accession no.

target post-translational modification

unmodified

General description

KLH-conjugated linear peptide corresponding to human Cytosolic 5′-nucleotidase II near the C-terminus.
~65 kDa observed. This antibody is expected to detect both isoforms.

Application

Immunohistochemistry Analysis: A 1:50-250 dilution from a representative lot detected Cytosolic 5′-nucleotidase II in human kidney tissue.

Physical form

Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Preparation Note

Stable for 1 year at 2-8°C from date of receipt.

Analysis Note

Evaluated by Western Blotting in A549 cell lysate.

Western Blotting Analysis: 0.5 µg/mL of this antibody detected Cytosolic 5′-nucleotidase II in 10 µg of A549 cell lysate.

Other Notes

Human. Predicted to react with Mouse, Rat, Feline, Canine, Bovine, and Horse based on 100% sequence homology.

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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Související obsah

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.





Globální číslo obchodní položky

Skladová položkaGTIN
ABC48104055977168921