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Documentos Principais

07-2268

Sigma-Aldrich

Anti-phospho-TBC1D1 Antibody (Ser237)

from rabbit, purified by affinity chromatography

Sinônimo(s):

TBC1 domain family member 1, TBC1 (tre-2/USP6, BUB2, cdc16) domain family, member 1

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About This Item

Código UNSPSC:
12352203
eCl@ss:
32160702

fonte biológica

rabbit

Nível de qualidade

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

purificado por

affinity chromatography

reatividade de espécies

human

reatividade da espécie (prevista por homologia)

ox (based on 100% sequence homology), chimpanzee (based on 100% sequence homology), mouse (based on 100% sequence homology), rat (based on 100% sequence homology), rhesus macaque (based on 100% sequence homology)

técnica(s)

western blot: suitable

nº de adesão NCBI

nº de adesão UniProt

Condições de expedição

wet ice

modificação pós-traducional do alvo

phosphorylation (pSer237)

Informações sobre genes

human ... TBC1D1(23216)

Descrição geral

TBC1D1 is the first member of a family of proteins that contain the tbc box motif of 180-220 amino acids and may be related to cell growth and differentiation. The composition of TBC1D1 has the same function as a known regulator of insulin-mediated Glut4 translocation and may play a role in severe human obesity. An insulin-independent increase in glucose transport several hours after exercise has been attributed to TBC1D1 phosphorylation. The R125W mutation of TBC1D1 is thought to decrease skeletal muscle glucose transport and could be the main reason for the obesity that seems to be linked to this type of mutation.

Especificidade

This antibody recognizes TBC1D1 phosphorylated at Ser237.

Imunogênio

Epitope: Phosphorylated Ser237
KLH-conjugated linear peptide corresponding to human TBC1D1 phosphorylated at Ser237.

Aplicação

Research Category
Signaling
Research Sub Category
Insulin/Energy Signaling

Glucose/Glycogen Metabolism
This phospho-TBC1D1 antibody is validated for use in WB for the detection of the phospho-TBC1D1 protein.

Qualidade

Evaluated by Western Blot in lambda phosphatase treated and untreated HEK293 cell lysates.

Western Blot Analysis: 1 µg/mL of this antibody detected TBC1D1 on 10 µg of lambda phosphatase treated and untreated HEK293 cell lysates.

Descrição-alvo

~145 kDa observed

forma física

Affinity purified
Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Armazenamento e estabilidade

Stable for 1 year at 2-8°C from date of receipt.

Nota de análise

Control
Lambda phosphatase treated and untreated HEK293 cell lysates

Outras notas

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Exoneração de responsabilidade

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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Código de classe de armazenamento

12 - Non 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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Marie Locard-Paulet et al.
Molecular systems biology, 16(7), e9524-e9524 (2020-07-04)
T-cell receptor (TCR) ligation-mediated protein phosphorylation regulates the activation, cellular responses, and fates of T cells. Here, we used time-resolved high-resolution phosphoproteomics to identify, quantify, and characterize the phosphorylation dynamics of thousands of phosphorylation sites in primary T cells during
Jonas Roland Knudsen et al.
Experimental physiology, 104(5), 704-714 (2019-02-03)
What is the central question of this study? Resolving the mechanism(s) leading to glucose transporter 4 (GLUT4) translocation to the muscle surface membrane has great therapeutic potential. However, the measurement of GLUT4 translocation is technically challenging. Here, we asked whether

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