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Merck
CN

HPA021175

Sigma-Aldrich

Anti-CDC37L1 antibody produced in rabbit

enhanced validation

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

别名:

Anti-CDC37B, Anti-Cell division cycle 37 homolog (S. cerevisiae)-like 1, Anti-FLJ20639, Anti-HARC

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关于此项目

UNSPSC代码:
12352203
人类蛋白质图谱编号:
NACRES:
NA.41
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生物来源

rabbit

偶联物

unconjugated

抗体形式

affinity isolated antibody

抗体产品类型

primary antibodies

克隆

polyclonal

产品线

Prestige Antibodies® Powered by Atlas Antibodies

表单

buffered aqueous glycerol solution

种属反应性

human

增强验证

recombinant expression
Learn more about Antibody Enhanced Validation

技术

immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:200-1:500

免疫原序列

LHNSESLDQEHAKAQTAVSELRQREEEWRQKEEALVQREKMCLWSTDAISKDVFNKSFINQDKRKDTEDEDKSE

UniProt登记号

运输

wet ice

储存温度

−20°C

靶向翻译后修饰

unmodified

基因信息

human ... CDC37L1(55664)

一般描述

The gene CDC37L1 (Hsp90 co-chaperone Cdc37-like 1) is mapped to human chromosome 9p24.1. It is expressed in various human tissues and localizes in the cytoplasm. CDC37L1 is commonly referred to as HARC (Hsp90-associating relative of Cdc37).

免疫原

cell division cycle 37 homolog (S. cerevisiae)-like 1 recombinant protein epitope signature tag (PrEST)

应用

All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project and as a result, are supported by the most extensive characterization in the industry.

The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set 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.

生化/生理作用

CDC37L1 (Hsp90 co-chaperone Cdc37-like 1) has been shown to form a complex with HSP90 (heat shock protein 90), HOP (Hsp70/Hsp90 organizing protein) and HSP70. It is suggested to be involved in HSP90-mediated protein folding.

特点和优势

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.

外形

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

其他说明

Corresponding Antigen APREST75193

法律信息

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

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储存分类代码

10 - Combustible liquids

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

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分析证书(COA)

Lot/Batch Number

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Françoise Bonnet et al.
BMC medical genomics, 5, 54-54 (2012-11-29)
Despite entering complete remission after primary treatment, a substantial proportion of patients with early stage breast cancer will develop metastases. Prediction of such an outcome remains challenging despite the clinical use of several prognostic parameters. Several reports indicate that genomic
G M Scholz et al.
The Journal of biological chemistry, 276(33), 30971-30979 (2001-06-20)
Although little is known about the precise mechanisms by which the molecular chaperone Hsp90 recognizes its client proteins, Cdc37 has been shown to play a critical role in the targeting of Hsp90 to client protein kinases. Described here is the
Kellie Cartledge et al.
Biochemistry, 46(51), 15144-15152 (2007-12-07)
Hsp90 is a molecular chaperone that acts in concert with Hsp70 to mediate the folding of many important regulatory proteins (e.g., protein kinases) into functional conformations. The chaperone activity of Hsp90 is primarily regulated by its cochaperones. For example, the

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