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Merck
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Documentos clave

HPA020587

Sigma-Aldrich

Anti-GULP1 antibody produced in rabbit

enhanced validation

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Sinónimos:

Anti-Cell death protein 6 homolog, Anti-GULP, Anti-PTB domain adapter protein CED-6, Anti-PTB domain-containing engulfment adapter protein 1

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About This Item

Código UNSPSC:
12352203
Atlas de proteínas humanas número:
NACRES:
NA.43

origen biológico

rabbit

Nivel de calidad

conjugado

unconjugated

forma del anticuerpo

affinity isolated antibody

tipo de anticuerpo

primary antibodies

clon

polyclonal

Línea del producto

Prestige Antibodies® Powered by Atlas Antibodies

Formulario

buffered aqueous glycerol solution

reactividad de especies

human, rat, mouse

validación mejorada

orthogonal RNAseq
Learn more about Antibody Enhanced Validation

técnicas

immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:50-1:200

secuencia del inmunógeno

KTDKRIFTFICKDSESNKHLCYVFDSEKCAEEITLTIGQAFDLAYRKFLESGGKDVETRKQIAGLQKRIQDLETENMELKNKVQDLENQLRITQVSA

Nº de acceso UniProt

Condiciones de envío

wet ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

unmodified

Información sobre el gen

human ... GULP1(51454)

Descripción general

PTB domain-containing engulfment adapter protein 1 (GULP1) is present in clathrin-coated vesicles. It possesses a phosphotyrosine binding domain (PTB) and the gene encoding it is localized on human chromosome 2.

Inmunógeno

PTB domain-containing engulfment adapter protein 1 recombinant protein epitope signature tag (PrEST)

Aplicación

All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project and as a result, are supported by the most extensive characterization in the industry.

The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. We also provide Prestige Antibodies® protocols and other useful information.

Acciones bioquímicas o fisiológicas

PTB domain-containing engulfment adapter protein 1 (GULP1) aids the endocytosis of low density lipoprotein receptor-related protein 1′s (LRP1′s) ligands and binds to clathrin machinery. GULP1 indirectly causes growth inhibition by regulating TGF (transforming growth factor)-β signaling. It also binds to amyloid precursor protein (APP) and stimulates the production of amyloid β (Aβ).

Características y beneficios

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

Ligadura / enlace

Corresponding Antigen APREST74202

Forma física

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Información legal

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

Cláusula de descargo de responsabilidad

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 clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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Certificados de análisis (COA)

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Visite la Librería de documentos

Apoptotic engulfment pathway and schizophrenia.
Chen X, et al.
PLoS ONE, 4(9), e6875-e6875 (2009)
Anupma Jha et al.
Molecular biology of the cell, 23(9), 1742-1764 (2012-03-09)
Clathrin-mediated endocytosis and phagocytosis are both selective surface internalization processes but have little known mechanistic similarity or interdependence. Here we show that the phosphotyrosine-binding (PTB) domain protein Ced-6, a well-established phagocytosis component that operates as a transducer of so-called "eat-me"
Cheng-I J Ma et al.
The Journal of biological chemistry, 287(24), 20636-20651 (2012-03-28)
Transforming growth factor β (TGF-β) is a key regulatory molecule with pleiotropic effects on cell growth, migration, and invasion. As a result, impairment of proper TGF-β signaling is central to tumorigenesis and metastasis. The TGF-β receptor V (TGFBRV or LRP1)
Yan Hao et al.
The Biochemical journal, 436(3), 631-639 (2011-04-14)
Altered production of Aβ (amyloid-β peptide), derived from the proteolytic cleavage of APP (amyloid precursor protein), is believed to be central to the pathogenesis of AD (Alzheimer's disease). Accumulating evidence reveals that APPc (APP C-terminal domain)-interacting proteins can influence APP
Jingyi Gong et al.
The Journal of cell biology, 218(10), 3455-3471 (2019-08-15)
Trogocytosis, in which cells nibble away parts of neighboring cells, is an intercellular cannibalism process conserved from protozoa to mammals. Its underlying molecular mechanisms are not well understood and are likely distinct from phagocytosis, a process that clears entire cells.

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