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Merck

R4407

Sigma-Aldrich

Anti-RER1 antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

Sinónimos:

Anti-RER1 retention in endoplasmic reticulum 1

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About This Item

Código UNSPSC:
12352203
NACRES:
NA.41

origen biológico

rabbit

Nivel de calidad

conjugado

unconjugated

forma del anticuerpo

affinity isolated antibody

tipo de anticuerpo

primary antibodies

clon

polyclonal

Formulario

buffered aqueous solution

mol peso

antigen ~25 kDa

reactividad de especies

human, rat, mouse

concentración

~1.0 mg/mL

técnicas

indirect immunofluorescence: 1-2 μg/mL using mouse 3T3 and rat NRK cells
western blot: 3-6 μg/mL using whole extract of HEK-293T cells expressing human Rer1

Nº de acceso UniProt

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

unmodified

Información sobre el gen

human ... RER1(11079)
mouse ... Rer1(67830)
rat ... Rer1(98675)

Descripción general

Retention in endoplasmic reticulum 1 (Rer1p) is found in Golgi-compartment. The protein contains four transmembrane domains (TDMs), with the amino and carboxy termini facing the cytosol and recognizes polar amino acids in TMDs of several proteins including sec12p and sec71p.

Especificidad

Anti-Rer1 recognizes human, mouse, and rat Rer1.

Aplicación

Anti-RER1 antibody produced in rabbit has been used in:
  • immunoblotting
  • immunohistochemistry
  • immunofluorescence

Anti-RER1 antibody produced in rabbit may be used in immunoblotting, immunofluorescence and immunohistochemical (IHC) techniques. It is used to determine the roles of RER1 in the retention/retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment.

Acciones bioquímicas o fisiológicas

Retention in endoplasmic reticulum 1 (Rer1) is essential for retrieval of endoplasmic reticulum (ER) membrane proteins from the early Golgi compartment. In addition, mammalian Rer1 is also involved in the ER retention/retrieval of unassembled γsecretase complex subunits. Rer1 interacts with immature nicastrin and unassembled Pen2 through critical residues found in their TMDs. Downregulation of protein expression enhances surface localization of Pen2, whereas Upregulated expression of Rer1 stabilizes unassembled Pen2. Thus, Rer1 regulates the assembly of the γ-secretase complex and therefore contributes to total cellular γ-secretase activity.

Forma física

Solution in 0.01 M phosphate buffered saline pH 7.4, containing 15 mM sodium azide.

Almacenamiento y estabilidad

For continuous use, store at 2–8 °C for up to one month. For extended storage, freeze in working aliquots at –20 °C. Repeated freezing and thawing is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.

Cláusula de descargo de responsabilidad

Unless otherwise stated in our catalog, 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

12 - Non Combustible Liquids

Clase de riesgo para el agua (WGK)

WGK 1


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Visite la Librería de documentos

Endoplasmic reticulum quality control of unassembled iron transporter depends on Rer1p-mediated retrieval from the golgi
Sato M, et al.
Molecular Biology of the Cell, 15(3), 1417-1424 (2004)
The ER retention protein RER1 promotes alpha-synuclein degradation via the proteasome
Park HJ, et al.
Testing, 12(9), e0184262-e0184262 (2017)
RER1 enhances carcinogenesis and stemness of pancreatic cancer under hypoxic environment
Chen S, et al.
Journal of Experimental & Clinical Cancer Research, 38(1), 15-15 (2019)
Rer1p competes with APH-1 for binding to nicastrin and regulates gamma-secretase complex assembly in the early secretory pathway
Spasic D, et al.
The Journal of cell biology, 176(5), 629-640 (2007)
Endoplasmic reticulum retention of the $\gamma$-secretase complex component Pen2 by Rer1
Kaether C, et al.
EMBO Reports, 8(8), 743-748 (2007)

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