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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

Sinônimo(s):

CD301, CLECSF13, CLECSF14, HML, HML2

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About This Item

Código UNSPSC:

12352203

NACRES:

NA.41

fonte biológica

mouse

conjugado

unconjugated

forma do anticorpo

purified immunoglobulin

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

forma

buffered aqueous solution

peso molecular

antigen ~35.4 kDa

reatividade de espécies

human

técnica(s)

western blot: 1 μg/mL

nº de adesão NCBI

NM_182906

nº de adesão UniProt

Q8IUN9

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... CLEC10A(10462)

Categorias relacionadas

Primary Antibodies

Descrição geral

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)

Imunogênio

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

Sequence
MTRTYENFQYLENKVKVQGFKNGPLPLQSLLQRLCSGPCHLLLSLGLGLLLLVIICVVGFQNSKFQRDLVTLRTDFSNFTSNTVAEIQALTSQGSSLEETIASLKAEVEGFKQERQAGVSELQEHTTQKAHLGHCPHCPSVCVPVHSEMLLRVQQLVQDLKKLTCQVATLNNNASTEGTCCPVNWVEHQDSCYWFSHSGMSWAEAEKYCQLKNAHLVVINSREEQNFVQKYLGSAYTWMGLSDPEGAWKWVDGTDYATGFQNWKPGQPDDWQGHGLGGGEDCAHFHPDGRWNDDVCQRPYHWVCEAGLGQTSQESH

Aplicação

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

Ações bioquímicas/fisiológicas

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.

forma física

Solution in phosphate buffered saline, pH 7.4

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Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Certificados de análise (COA)

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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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