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The antibody against PDIA5 was raised in rabbit using the Human PDIA5 as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, WB, IHC.
The antibody against PDIA5 was raised in rabbit using the Human PDIA5 as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, WB, IHC.
$600.00
| Cat.No | ADC-52415A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | PDIA5 |
| Target Synonyms | Pdia5 antibody; PDIA5_HUMAN antibody; PDIR antibody; Protein disulfide isomerase related antibody; Protein disulfide isomerase-related protein antibody; Protein disulfide-isomerase A5 antibody | Form | Liquid |
| Species Reactivity | Human, Mouse, Rat | Isotype | IgG |
| Storage Buffer | 50% Glycerol, Avoid freeze / thaw cycles., PBS with 0.02% sodium azide | Purification Method | Antigen affinity purified |
| Conjugate | Non-conjugated | Application | ELISA, IHC, WB |
| Storage | Upon receipt |
| Immunogen Description | Human PDIA5 | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | Complete sequences for the immunogen, target protein, and peptides are available upon request. | Uniprot ID | Q14554 |
Uniprot Id
Q14554
Target Species
Human
Target Name
PDIA5
Target Full Name
Protein disulfide-isomerase A5
Target Subcellular Location
Endoplasmic reticulum lumen.
Target Protein Families
Protein disulfide isomerase family
Target Synonyms
Pdia5; PDIA5_HUMAN; PDIR; Protein disulfide isomerase related; Protein disulfide isomerase-related protein; Protein disulfide-isomerase A5
Target Background
This gene encodes a member of the disulfide isomerase (PDI) family of endoplasmic reticulum (ER) proteins that catalyze protein folding and thiol-disulfide interchange reactions. The encoded protein has an N-terminal ER-signal sequence, three catalytically active thioredoxin (TRX) domains, a TRX-like domain, and a C-terminal ER-retention sequence. The N-terminal TRX-like domain is the primary binding site for the major ER chaperone calreticulin and possibly other proteins and substrates as well. Alternative splicing results in multiple protein- and non-protein-coding transcript variants.
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