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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 Code

12 - Non Combustible Liquids

WGK

WGK 1


Certificates of Analysis (COA)

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Endoplasmic reticulum retention of the $\gamma$-secretase complex component Pen2 by Rer1
Kaether C, et al.
EMBO Reports, 8(8), 743-748 (2007)
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)

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