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Key Documents

SAB1403068

Sigma-Aldrich

Monoclonal Anti-CLEC10A antibody produced in mouse

clone 2D6, purified immunoglobulin, buffered aqueous solution

Sinonimo/i:

CD301, CLECSF13, CLECSF14, HML, HML2

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About This Item

Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

mouse

Coniugato

unconjugated

Forma dell’anticorpo

purified immunoglobulin

Tipo di anticorpo

primary antibodies

Clone

2D6, monoclonal

Forma fisica

buffered aqueous solution

PM

antigen ~37.11 kDa

Reattività contro le specie

human

tecniche

capture ELISA: suitable
indirect ELISA: suitable
western blot: 1-5 μg/mL

Isotipo

IgG2aκ

N° accesso NCBI

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... CLEC10A(10462)

Categorie correlate

Descrizione generale

This gene encodes a member of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. Members of this family share a common protein fold and have diverse functions, such as cell adhesion, cell-cell signalling, glycoprotein turnover, and roles in inflammation and immune response. The encoded type 2 transmembrane protein may function as a cell surface antigen. Two transcript variants encoding distinct isoforms have been identified for this gene. (provided by RefSeq)

Immunogeno

CLEC10A (NP_006335.2, 70 a.a. ~ 169 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
VTLRTDFSNFTSNTVAEIQALTSQGSSLEETIASLKAEVEGFKQERQAVHSEMLLRVQQLVQDLKKLTCQVATLNNNGEEASTEGTCCPVNWVEHQDSCY

Applicazioni

Monoclonal Anti-CLEC10A antibody produced in mouse is suitable for capture ELISA, indirect ELISA and western blot applications.

Azioni biochim/fisiol

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 Ag.

Stato fisico

Solution in phosphate buffered saline, pH 7.4

Esclusione di responsabilità

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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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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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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