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Merck
CN

MABC534

Sigma-Aldrich

Anti-TPM3 Antibody, isoform TC22, clone TC22-4

clone TC22-4, from mouse

别名:

Tropomyosin alpha-3 chain, Gamma-tropomyosin, Tropomyosin-3, Tropomyosin-5, hTM5

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UNSPSC代码:
12352203
eCl@ss:
32160702

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生物来源

mouse

抗体形式

purified antibody

抗体产品类型

primary antibodies

克隆

TC22-4, monoclonal

种属反应性

human

技术

ELISA: suitable
flow cytometry: suitable
immunohistochemistry: suitable
western blot: suitable

同位素/亚型

IgG1κ

NCBI登记号

NP_000357

UniProt登记号

P06753-4

运输

wet ice

靶向翻译后修饰

unmodified

基因信息

human ... TPM3(7170)

一般描述

Tropomyosins are dimmers of coiled-coil proteins that provide stability to actin filaments and regulate access of other actin-binding proteins. The human TPM3 gene (Gene ID 7170; also known as TM3, TM5, TRK, CFTD, NEM1, TM-5, TM30, CAPM1, TM30nm, TPMsk3, hscp30, HEL-189, HEL-S-82p, OK/SW-cl.5) encodes seven tropomyosin alpha-3 chain isoforms (UniProt P06753; also known as Tropomyosin-3) as a result of alternative splicing. Spliced variants 1, 2, 4, and 5 are also known as the skeletal muscle, TM30nm, TC22, and hTM5 isoform, respectively. The TC22 and the hTM5 variants are identical in sequence other than the 25 amino acids at their C-terminal end. TC22 is expressed in 100% of colorectal carcinomas, but is not expressed in normal colon epithelial cells. The anticarcinogenic potency of sulfasalazine (SASP) and its active metabolite 5-aminosalicylate (5-ASA, mesalamine) in protecting ulcerative colitis (UC) patients from developing colorectal cancer is directly linked to their efficacy in reducing cellular expression of TC22. Likewise, siRNA-mediated TC22 downregulation is shown to significantly alter several critical carcinogenic pathways in the human colon adenocarcinoma LS180 cells.
~32 kDa observed. Uncharacterized band(s) may appear in some lysates.

免疫原

Recombinant human TC22 and boosts with TC22-specific C-terminal peptide.

应用

This Anti-TPM3 Antibody, isoform TC22, clone TC22-4 is validated for use in Western blotting, Immunohistochemistry, ELISA and FLow Cytometry for the detection of TPM3.
Western Blotting Analysis: A representative lot detected endogenous TC22 in human colorectal carcinoma T84 cell lysate, as well as recombinant human TC22, but not five other human TPM3 isoforms (Lin, J.L., et al. (2002). Gastroenterology. 123(1):152-162; Das, K.K., et al. (2009). Mol Pharmacol. 76(1):183-191).
ELISA Analysis: A representative lot specifically detected recombinant human TC22, but not five other human TPM3 isoforms (Das, K.K., et al. (2009). Mol Pharmacol. 76(1):183-191.).
Flow Cytometry Analysis: A representative lot detected time-dependent TC22 downregulation in LS180 cells upon 2 mM 5-Aminosalicylate (5-ASA) treatment (Das, K.K., et al. (2009). Mol Pharmacol. 76(1):183-191.)
Immunohistochemistry: Representative lots detected TC22 expression in human colon carcinoma and adenomatous polyp tissues, but not in normal colon tissue samples (Lin, J.L., et al. (2002). Gastroenterology. 123(1):152-162; Watari, J., et al. (2008). Clin Gastroenterol Hepatol. 6(4):409-17).

生化/生理作用

Clone TC22-4 selectively detects human tropomyosin alpha-3 chain (TMP3) spliced variant TC22 (isoform 4), but not spliced Isoform 1 (Skeletal muscle), 2 (TM30nm), 3, 5 (hTM5), 6, or 7.

外形

Format: Purified

分析说明

Evaluated by Western Blotting in recombinant human TC22 protein.

Western Blotting Analysis: 0.5 µg/mL of this antibody detected TPM3 in 10 µg of recombinant human TC22 protein.

其他说明

Concentration: Please refer to lot specific datasheet.

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储存分类代码

12 - Non Combustible Liquids

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable

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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.

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