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AB1327

Anti-SEC61A antibody

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(2 Publications)

Goat Polyclonal SEC61A antibody. Suitable for WB, IHC-P and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Synthetic Peptide within Human SEC61A1 aa 450-500.

View Alternative Names

SEC61A, SEC61A1, Protein transport protein Sec61 subunit alpha isoform 1, Sec61 alpha-1

1 Images
Western blot - Anti-SEC61A antibody (AB1327)
  • WB

Unknown

Western blot - Anti-SEC61A antibody (AB1327)

All lanes:

Western blot - Anti-SEC61A antibody (ab1327) at 1 µg/mL

All lanes:

Human cerebellum lysate in RIPA buffer at 35 µg

Predicted band size: 52 kDa

false

Key facts

Host species

Goat

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB, IHC-P

applications

Immunogen

Synthetic Peptide within Human SEC61A1 aa 450-500. The exact immunogen used to generate this antibody is proprietary information.

P61619

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
Purified from goat serum by ammonium sulphate precipitation followed by antigen affinity chromatography using the immunizing peptide.
Storage buffer
pH: 7.3 Preservative: 0.02% Sodium azide Constituents: 0.5% BSA, 0.05% Tris
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

SEC61A also known as Sec61p or protein transport protein Sec61 subunit alpha isoform 1 serves as an important component of the protein translocation process. This protein weighs approximately 54 kDa and is expressed in the endoplasmic reticulum (ER) membrane of eukaryotic cells. SEC61A forms part of the SEC61 complex which operates as a channel for polypeptide chains to enter the ER from the cytosol. It plays a central role in the translocation of nascent polypeptide chains into the ER or their integration into the ER membrane.
Biological function summary

The SEC61 complex holds significance in the translocon channel with SEC61A contributing to the determination of ER insertion or membrane integration of proteins. Its function is often associated with the ribosome as the complex forms a conduit for nascent proteins during translation. The SEC61A ensures proper protein localization with the translocon complex acting as a bridge between the ribosome and the ER. It is integral to cellular processes that require precise protein folding modification and targeting within cells.

Pathways

The role of SEC61A in protein targeting is vital for maintaining various cellular functions. The unfolded protein response (UPR) and the ER-associated degradation (ERAD) pathways depend on SEC61A for the recognition and resolution of misfolded proteins. In these pathways SEC61A interacts with the proteins like BIP and other chaperones involved in monitoring protein folding status and activating the necessary stress responses if unfolded proteins accumulate. Its involvement in these pathways highlights its importance in maintaining cellular homeostasis.

Mutations or dysfunctions of SEC61A contribute to various conditions such as cystic fibrosis and diabetes. Improper function of SEC61A links to defective protein translocation leading to accumulation of misfolded proteins a characteristic observed in cystic fibrosis alongside the CFTR protein. Similarly in diabetes inefficient SEC61A function might disturb insulin production or secretion since SEC61A's role in protein translocation and processing is fundamental. Moreover SEC61A dysfunction can affect proteins like IAPP involved in β-cell amyloid formation further linking it to diabetes pathogenesis.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Component of SEC61 channel-forming translocon complex that mediates transport of signal peptide-containing precursor polypeptides across the endoplasmic reticulum (ER) (PubMed : 12475939, PubMed : 22375059, PubMed : 28782633, PubMed : 29719251, PubMed : 32814900). Forms a ribosome receptor and a gated pore in the ER membrane, both functions required for cotranslational translocation of nascent polypeptides (PubMed : 22375059, PubMed : 28782633, PubMed : 29719251). May cooperate with auxiliary protein SEC62, SEC63 and HSPA5/BiP to enable post-translational transport of small presecretory proteins (PubMed : 22375059, PubMed : 29719251). The SEC61 channel is also involved in ER membrane insertion of transmembrane proteins : it mediates membrane insertion of the first few transmembrane segments of proteins, while insertion of subsequent transmembrane regions of multi-pass membrane proteins is mediated by the multi-pass translocon (MPT) complex (PubMed : 32820719, PubMed : 36261522). The SEC61 channel cooperates with the translocating protein TRAM1 to import nascent proteins into the ER (PubMed : 8616892). Controls the passive efflux of calcium ions from the ER lumen to the cytosol through SEC61 channel, contributing to the maintenance of cellular calcium homeostasis (PubMed : 28782633). Plays a critical role in nephrogenesis, specifically at pronephros stage (By similarity).
See full target information SEC61A1

Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Cellular and molecular life sciences : CMLS 80:177 PubMed37285022

2023

siRNA screening reveals that SNAP29 contributes to exosome release.

Applications

Unspecified application

Species

Unspecified reactive species

Nina Pettersen Hessvik,Krizia Sagini,Silvana Romero,Manuel Ramirez-Garrastacho,Marta Rodriguez,Astrid Elisabeth V Tutturen,Audun Kvalvaag,Espen Stang,Andreas Brech,Kirsten Sandvig,Alicia Llorente

Diabetes 59:460-70 PubMed19934005

2009

A point mutation in Sec61alpha1 leads to diabetes and hepatosteatosis in mice.

Applications

ICC/IF

Species

Mouse

David J Lloyd,Matthew C Wheeler,Nicholas Gekakis
View all publications

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