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Key Documents

HPA021937

Sigma-Aldrich

Anti-CLEC10A antibody produced in rabbit

enhanced validation

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution, Ab1

Synonim(y):

Anti-C-type lectin domain family 10 member A, Anti-C-type lectin superfamily member 14, Anti-CD301 antigen, Anti-Macrophage lectin 2

Zaloguj sięWyświetlanie cen organizacyjnych i kontraktowych


About This Item

Kod UNSPSC:
12352203
Numer w atlasie ludzkich białek:
NACRES:
NA.43

pochodzenie biologiczne

rabbit

Poziom jakości

białko sprzężone

unconjugated

forma przeciwciała

affinity isolated antibody

rodzaj przeciwciała

primary antibodies

klon

polyclonal

linia produktu

Prestige Antibodies® Powered by Atlas Antibodies

Postać

buffered aqueous glycerol solution

reaktywność gatunkowa

human

rozszerzona walidacja

recombinant expression
Learn more about Antibody Enhanced Validation

metody

immunoblotting: 0.04-0.4 μg/mL
immunohistochemistry: 1:50-1:200

sekwencja immunogenna

CPVNWVEHQDSCYWFSHSGMSWAEAEKYCQLKNAHLVVINSREEQNFVQKYLGSAYTWMGLSDPEGAWKWVDGTDYATGFQNWKPGQPDDWQGHGLGGGEDCAHFHPDGRWND

numer dostępu UniProt

Warunki transportu

wet ice

temp. przechowywania

−20°C

docelowa modyfikacja potranslacyjna

unmodified

informacje o genach

human ... CLEC10A(10462)

Powiązane kategorie

Opis ogólny

CLEC10A (C-type lectin domain family 10, member A) is a macrophage calcium-dependent (C-type) glycoreceptor belonging to the C-type lectin family. It is also referred to as CD301. It is expressed in the intermediate monocytes and macrophages.

Immunogen

C-type lectin domain family 10 member A recombinant protein epitope signature tag (PrEST)

Zastosowanie

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.

Działania biochem./fizjol.

CLEC10A (C-type lectin domain family 10, member A) functions as a tumor associated macrophages in the tumor progression. It has been predicted that after being expressed by macrophages, glycoreceptor CLEC10A may directly interact with the glycan-binding receptors to identify the presence of certain glycan in human tumors. It has also been reported that macrophage cell surface lectin recognizes a common human carcinoma-associated epitope, Tn antigen.

Cechy i korzyści

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.

Powiązanie

Corresponding Antigen APREST70017

Postać fizyczna

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

Informacje prawne

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

Oświadczenie o zrzeczeniu się odpowiedzialności

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.
This page may contain text that has been machine translated.

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Kod klasy składowania

10 - Combustible liquids

Klasa zagrożenia wodnego (WGK)

WGK 1

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable


Certyfikaty analizy (CoA)

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Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Peter Nollau et al.
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 61(3), 199-205 (2013-01-01)
Specialized protein domains bind to posttranslational modifications (PTMs) of proteins, such as phosphorylation or glycosylation. When such PTM-binding protein domains are used as analytical tools, the functional states of cells and tissues can be determined with high precision. Here, we
N Suzuki et al.
Journal of immunology (Baltimore, Md. : 1950), 156(1), 128-135 (1996-01-01)
A human macrophage calcium-dependent (C-type) lectin cDNA clone was obtained from a library derived from IL-2-treated peripheral blood monocytes. The cDNA cloning was based on the structural homology to hepatic asialoglycoprotein receptors. The nucleotide sequence of this cDNA clone was
Toshiya Okumura et al.
PloS one, 9(6), e100559-e100559 (2014-06-20)
Phosphorylation of hormone-sensitive lipase (HSL) and perilipin by protein kinase A (PKA) promotes the hydrolysis of lipids in adipocytes. Although activation of lipolysis by PKA has been well studied, inactivation via protein phosphatases is poorly understood. Here, we investigated whether

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