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Merck
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Key Documents

SAB3701084

Sigma-Aldrich

Anti-Mouse IgG (H+L), highly cross adsorbed-Peroxidase antibody produced in rabbit

affinity isolated antibody, lyophilized powder

别名:

HRP

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About This Item

分類程式碼代碼:
12352203
NACRES:
NA.46

生物源

rabbit

共軛

peroxidase conjugate

抗體表格

affinity isolated antibody

抗體產品種類

secondary antibodies

無性繁殖

polyclonal

形狀

lyophilized powder

物種活性

mouse

技術

immunohistochemistry: suitable
indirect ELISA: suitable
western blot: suitable

運輸包裝

wet ice

儲存溫度

2-8°C

目標翻譯後修改

unmodified

特異性

This product was prepared from monospecific antiserum by immunoaffinity chromatography using Mouse IgG coupled to agarose beads followed by solid phase adsorption(s) to remove any unwanted reactivities. Assay by immunoelectrophoresis resulted in a single precipitin arc against Anti-Peroxidase, Anti-Rabbit Serum, Mouse IgG, and Mouse Serum. No reaction was observed against Human Serum Proteins. Specificity was confirmed by ELISA at less than 1% cross reactivity against other Mouse or Human heavy or light chain isotypes.

免疫原

Mouse IgG whole molecule

物理性質

Antibody format: IgG

外觀

Supplied in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2 with 10 mg/mL Bovine Serum Albumin (BSA) - Immunoglobulin and Protease free

重構

Reconstitute with 1.0 mL deionized water (or equivalent).

免責聲明

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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象形圖

Exclamation mark

訊號詞

Warning

危險聲明

防範說明

危險分類

Skin Sens. 1

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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Rebecca San Gil et al.
Scientific reports, 7(1), 2387-2387 (2017-05-26)
Heat shock proteins (Hsps) are molecular chaperones that prevent the aggregation of client proteins by facilitating their refolding, or trafficking them for degradation. The chaperone activities of Hsps are dependent on dynamic protein-protein interactions, including their oligomerisation into large multi-subunit

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