Overview

Description

  • Nature
    Recombinant
  • Source
    Wheat germ
  • Amino Acid Sequence
    • Species
      Human
    • Sequence
      LPLDTVTFYKVIPKSKFVLVKFDTQYPYGEKQDEFKRLAENSASSDDLLV AEVGISDYGDKLNMELSEKYKLDKESYPVFYLFRDGDFENPVPYTGAVKV
    • Amino acids
      39 to 138
    • Tags
      proprietary tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab161218 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    Western blot

    ELISA

  • Form
    Liquid
  • Additional notes
    Protein concentration is above or equal to 0.05 mg/ml.
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    pH: 8.00
    Constituents: 0.31% Glutathione, 0.79% Tris HCl

General Info

  • Alternative names
    • C12orf8
    • Chromosome 12 open reading frame 8
    • Endoplasmic reticulum lumenal protein ERp28
    • Endoplasmic reticulum protein 29
    • Endoplasmic reticulum protein 29 isoform 1
    • Endoplasmic reticulum protein ERp29
    • Endoplasmic reticulum resident protein 28
    • Endoplasmic reticulum resident protein 29
    • Endoplasmic reticulum resident protein 31
    • Epididymis secretory protein Li 107
    • ERp28
    • ERP29_HUMAN
    • ERp31
    • HEL S 107
    • PDI-DB
    • PDIA9
    • Protein disulfide isomerase family A member 9
    see all
  • Relevance
    Proper protein folding and post-translational modifications are essential for secretory protein export out of the endoplasmic reticulum. This task is accomplished by chaperone proteins such as protein disulfide isomerase (PDI), GRP94, and BiP. A recently characterized protein, designated ERp29, is closely related to these chaperone proteins and appears to be upregulated during ER stress conditions. ERp29 is a soluble 259-residue protein that is localized to the lumen of the endoplasmic reticulum in all mammalian cells. Research has shown that there are two primary domains within ERp29. The first is the C-terminal region that is a novel, all helical, fold that is most likely involved with ERp29 retention to the ER. The second is the N-terminal region that resembles that of PDI’s thioredoxin module. The protein shows sequence similarity to the protein disulfide isomerase family. However, it lacks the thioredoxin motif characteristic of this family, suggesting that this protein does not function as a disulfide isomerase. The protein dimerizes and is thought to play a role in the processing of secretory proteins within the ER.
  • Cellular localization
    Endoplasmic reticulum, Cell surface.

Images

  • ab161218 on a 12.5% SDS-PAGE stained with Coomassie Blue.

References

ab161218 has not yet been referenced specifically in any publications.

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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

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