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R4407

Sigma-Aldrich

Anti-RER1 antibody produced in rabbit

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

Synonym(s):

Anti-RER1 retention in endoplasmic reticulum 1

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~25 kDa

species reactivity

human, rat, mouse

concentration

~1.0 mg/mL

technique(s)

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

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

General description

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.

Specificity

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

Application

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.

Biochem/physiol Actions

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.

Physical form

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

Storage and Stability

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.

Disclaimer

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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Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
Hyo-Jin Park et al.
The Journal of biological chemistry, 287(48), 40629-40640 (2012-10-09)
Aβ production is influenced by intracellular trafficking of secretases and amyloid precursor protein (APP). Retention in endoplasmic reticulum 1 (RER1) regulates the trafficking of γ-secretase and APP, thereby influences Aβ production. RER1, an ER retention/retrieval factor for γ-secretase and APP
Shi Chen et al.
Journal of experimental & clinical cancer research : CR, 38(1), 15-15 (2019-01-12)
Increasing incidence and mortality rates of pancreatic cancer (PC) highlight an urgent need for novel and efficient drugs. Retention in endoplasmic reticulum 1 (RER1) is an important retention factor in the endoplasmic reticulum (ER). However, it remains elusive whether RER1
Nathalie Jurisch-Yaksi et al.
The Journal of cell biology, 200(6), 709-720 (2013-03-13)
Cilia project from the surface of most vertebrate cells and are important for several physiological and developmental processes. Ciliary defects are linked to a variety of human diseases, named ciliopathies, underscoring the importance of understanding signaling pathways involved in cilia

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