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Merck

HPA029856

Sigma-Aldrich

Anti-LALBA antibody produced in rabbit

enhanced validation

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

别名:

Anti-LYZL7, Anti-Lactalbumin, α-

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About This Item

分類程式碼代碼:
12352203
人類蛋白質圖譜編號:
NACRES:
NA.41

生物源

rabbit

共軛

unconjugated

抗體表格

affinity isolated antibody

抗體產品種類

primary antibodies

無性繁殖

polyclonal

產品線

Prestige Antibodies® Powered by Atlas Antibodies

形狀

buffered aqueous glycerol solution

物種活性

human

加強驗證

recombinant expression
Learn more about Antibody Enhanced Validation

技術

immunoblotting: 0.04-0.4 μg/mL
immunohistochemistry: 1:1000-1:2500

免疫原序列

QVPQSRNICDISCDKFLDDDITDDIMCAKKILDIKGIDYWLAHKALCTEKLEQWLCEK

UniProt登錄號

運輸包裝

wet ice

儲存溫度

−20°C

目標翻譯後修改

unmodified

基因資訊

human ... LALBA(3906)

一般說明

The gene LALBA (α-lactalbumin) is mapped to human chromosome 12q13. It is a small acidic calcium-binding milk protein. LALBA constitutes about 20-25% of total protein in human milk. The protein has a helical α-domain and a β-sheeted β-domain.

免疫原

lactalbumin, alpha- recombinant protein epitope signature tag (PrEST)

應用

All Prestige Antibodies®Powered by Atlas Antibodies is developed and validated by the Human Protein Atlas (HPA) project . Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. We also provide Prestige Antibodies® protocols and other useful information.
Anti-LALBA antibody produced in rabbit has been used in western blotting and immunohistochemistry.

生化/生理作用

LALBA (α-lactalbumin) is part of the lactose synthase complex and is responsible for the biosynthesis of lactose. Peptides generated after partial digestion of this protein have antimicrobial and immunostimulatory properties. A multimeric α-lactalbumin enhances cell death in tumors.

特點和優勢

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

聯結

Corresponding Antigen APREST77903

外觀

Solution in phosphate buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide.

法律資訊

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

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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儲存類別代碼

10 - Combustible liquids

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable


分析证书(COA)

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The oleic acid complexes of proteolytic fragments of alpha-lactalbumin display apoptotic activity.
Tolin S, et al.
FEBS Journal, 277, 163-173 (2010)
The protective role of pregnancy in breast cancer.
Russo J, et al.
Breast Cancer Research, 7, 131-142 (2005)
The human alpha-lactalbumin molten globule: comparison of structural preferences at pH 2 and pH 7.
Rosner HI and Redfield C
Journal of Molecular Biology, 394, 351-362 (2009)
Vincent K Tuohy et al.
Cancers, 8(6) (2016-06-21)
We have proposed that safe and effective protection against the development of adult onset cancers may be achieved by vaccination against tissue-specific self-proteins that are "retired" from expression at immunogenic levels in normal tissues as we age, but are overexpressed
The small heat-shock protein aB-crystallin uses different mechanisms of chaperone action to prevent the amorphous versus fibrillar aggregation of a-lactalbumin.
Kulig M and Ecroyd H
The Biochemical Journal, 448, 343-352 (2012)

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