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Key Documents

SAB1406995

Anti-CLEC10A antibody produced in mouse

Name: Anti-CLEC10A antibody produced in mouse
Brand: SIGMA

purified immunoglobulin, buffered aqueous solution

Synonyme(s) :

CD301, CLECSF13, CLECSF14, HML, HML2

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About This Item

Code UNSPSC :

12352203

Nomenclature NACRES :

NA.41

Source biologique

mouse

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~35.4 kDa

Espèces réactives

human

Technique(s)

western blot: 1 μg/mL

Numéro d'accès NCBI

NM_182906

Numéro d'accès UniProt

Q8IUN9

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... CLEC10A(10462)

Catégories apparentées

Primary Antibodies

Description générale

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)

Immunogène

CLEC10A (NP_878910.1, 1 a.a. ~ 316 a.a) full-length human protein.

Sequence
MTRTYENFQYLENKVKVQGFKNGPLPLQSLLQRLCSGPCHLLLSLGLGLLLLVIICVVGFQNSKFQRDLVTLRTDFSNFTSNTVAEIQALTSQGSSLEETIASLKAEVEGFKQERQAGVSELQEHTTQKAHLGHCPHCPSVCVPVHSEMLLRVQQLVQDLKKLTCQVATLNNNASTEGTCCPVNWVEHQDSCYWFSHSGMSWAEAEKYCQLKNAHLVVINSREEQNFVQKYLGSAYTWMGLSDPEGAWKWVDGTDYATGFQNWKPGQPDDWQGHGLGGGEDCAHFHPDGRWNDDVCQRPYHWVCEAGLGQTSQESH

Application

Anti-CLEC10A antibody produced in mouse is suitable for western blot assay.

Actions biochimiques/physiologiques

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.

Forme physique

Solution in phosphate buffered saline, pH 7.4

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

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Protein domain histochemistry (PDH): binding of the carbohydrate recognition domain (CRD) of recombinant human glycoreceptor CLEC10A (CD301) to formalin-fixed, paraffin-embedded breast cancer tissues.

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

Molecular cloning and expression of cDNA encoding human macrophage C-type lectin. Its unique carbohydrate binding specificity for Tn antigen.

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

Phospholipase C-related catalytically inactive protein (PRIP) regulates lipolysis in adipose tissue by modulating the phosphorylation of hormone-sensitive lipase.

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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