Anti-ERP29 Antibody (3I584) is a Mouse antibody targeting ERP29. Anti-ERP29 Antibody (3I584) can be used in WB,IHC-P,IHC-Fr,ICC/IF,IF.

IgG2a, Kappa

3I584

Human (predicted:Mouse)

1. Cell line: HeLa
Fixative: 4% Paraformaldehyde
Permeabilization: 0.1% TritonX-100
Primary ab dilution: 1:50
Primary incubation condition: 4°C overnight
Secondary ab: Goat Anti-Mouse IgG
Nuclear counter stain: DAPI (Blue)
Comment: Color green is the positive signal for TMAB-05683
2. Blocking buffer: 5% NFDM/TBST
Primary ab dilution: 1：1000
Primary ab incubation condition: overnight, at 4 degree
Secondary ab: Goat Anti-Mouse IgG H&L (HRP)
Lysate: HeLa, 293, 4T1, Raw264.7
Protein loading quantity: 20 μg
Exposure time: 30 s
Predicted MW: 29 kDa
Observed MW: 29 kDa
3. Tissue: Human liver
Section type: Formalin fixed & Paraffin-embedded section
Retrieval method: High temperature and high pressure
Retrieval buffer: Tris/EDTA buffer, pH 9.0 Primary ab dilution: 1:100
Primary ab incubation condition: 1 hour at room temperature
Secondary ab: SP Kit (Mouse)
Counter stain: Hematoxylin (Blue)
Comment: Color brown is the positive signal for TMAB-05683

WB: 1:500-1000; IHC-P: 1:100-500; IHC-Fr: 1:100-500; ICC/IF: 1:100-500; IF: 1:100-500

Monoclonal

ERP29

Endoplasmic reticulum resident protein 29

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.