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07-1401

Sigma-Aldrich

Anti-GLUT-1 Antibody, CT

from rabbit, purified by affinity chromatography

Sinônimo(s):

Glucose Transporter type 1, Solute carrier family 2, facilitated glucose transporter, member 1

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About This Item

Código UNSPSC:
12352203
eCl@ss:
32160702
NACRES:
NA.41

fonte biológica

rabbit

Nível de qualidade

forma do anticorpo

purified immunoglobulin

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

purificado por

affinity chromatography

reatividade de espécies

human

reatividade da espécie (prevista por homologia)

mouse (Human. Predicted to react with Mouse based on 100% sequence homology.)

técnica(s)

immunocytochemistry: suitable
immunohistochemistry: suitable (paraffin)
western blot: suitable

Isotipo

IgG

nº de adesão NCBI

nº de adesão UniProt

Condições de expedição

wet ice

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... SLC2A1(6513)

Descrição geral

Solute carrier family 2, facilitated glucose transporter member 1 (UniProt: P11166; also known as Glucose transporter type 1, erythrocyte/brain, GLUT-1, HepG2 glucose transporter) is encoded by the SLC2A1 (also known as GLUT1) gene (Gene ID: 6513) in human. Glucose transporters are a family of integral membrane proteins that facilitative glucose uptake by cells. Seven different glucose transport proteins have been described that are designated as GLUT-1 to 7. GLUT-1 is a highly conserved; ubiquitously distributed, multi-pass membrane protein that is responsible for constitutive glucose uptake. It displays very broad substrate specificity and can transport a wide range of aldoses including both pentoses and hexoses. It is the predominant glucose transporter in embryonic and fetal tissues. In many organs, GLUT-1 is concentrated in endothelial cells of blood-tissue barriers. Hence, it has a specialized role to shuttle glucose between blood and organs that have limited access to small solutes via passive diffusion. It is also abundant in the mammalian erythrocyte membrane where it can rapidly equilibrate glucose between the cytoplasm of the erythrocyte and the blood plasma. GLUT-1 levels are reported to be frequently upregulated during tumorigenesis. Mutations in SLC2A1 gene are linked to GLUT-1 deficiency syndrome 1 and 2 that are characterized by infantile-onset epileptic encephalopathy, delayed development, microcephaly, and motor incoordination, and paroxysmal exercise-induced dyskinesia.

Especificidade

This rabbit polyclonal antibody specifically detects Glucose transporter type 1 (GLUT-1). It targets an epitope within 12 amino acids from the C-terminal region.

Imunogênio

Epitope: C-Terminus
KLH-conjugated linear peptide corresponding to the C-terminal of Human Glucose transporter-1 (GLUT-1).

Aplicação

Anti-GLUT-1, CT, Cat. No. 07-1401, is a rabbit polyclonal antibody that detects glucose transporter member 1 and is tested for use in Western Blotting, Immunohistochemistry (Paraffin), and Immunocytochemistry
Research Category
Signaling
Research Sub Category
Insulin/Energy Signaling
Tested Applications
  • Immunocytochemistry Analysis: A 1:500 dilution from a representative lot detected GLUT-1 in A431 cells.
  • Immunohistochemistry (Paraffin) Analysis: A 1:1,000 dilution from a representative lot detected GLUT-1 in Human pancreas, Human lung, and Human placenta tissue sections.
  • Note: Actual optimal working dilutions must be determined by end user as specimens, and experimental conditions may vary with the end user.

Qualidade

Evaluated by Western Blotting in Human umbilical vein endothelial cell (HUVEC) lysate.
  • Western Blotting Analysis: A 1:1,000 dilution of this antibody detected GLUT-1 in Human umbilical vein endothelial cell (HUVEC) lysate.

Descrição-alvo

~54 kDa observed; 54.08 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

Ligação

Replaces: AB1340

forma física

Affinity purified
Purified rabbit polyclonal antibody in buffer containing 0.02 M phosphate buffer, pH 7.6, 0.25 M NaCl, and 0.1% sodium azide.

Armazenamento e estabilidade

Recommended storage: +2°C to +8°C.

Nota de análise

Control
Jurkat Cell Lysate

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 2

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (COA)

Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.

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GLUT1 protein expression correlates with unfavourable histologic category and high risk in patients with neuroblastic tumours.
Ramani, Pramila, et al.
Virchows Archiv (2013)
I W Smoak et al.
Anatomy and embryology, 201(5), 327-333 (2000-06-06)
The embryonic heart depends on glucose during early organogenesis. Glut-1 functions in constitutive glucose uptake in adult tissues and is the predominant glucose transporter in embryonic and fetal tissues. This study focuses on Glut-1 expression in the heart during normal
Critical role for lactate dehydrogenase A in aerobic glycolysis that sustains pulmonary microvascular endothelial cell proliferation.
Parra-Bonilla, G; Alvarez, DF; Al-Mehdi, AB; Alexeyev, M; Stevens, T
American Journal of Physiology. Lung Cellular and Molecular Physiology null
GLUT4 and UBC9 protein expression is reduced in muscle from type 2 diabetic patients with severe insulin resistance.
Kampmann, U; Christensen, B; Nielsen, TS; Pedersen, SB; ?rskov, L; Lund, S; M?ller, N; Jessen, N
Testing null
Sugar transporter regulation by ATP and quaternary structure.
Cloherty, E K, et al.
Blood Cells, Molecules and Diseases, 27, 102-107 (2001)

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