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The antibody against PDIA5 was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 22-140 of human PDIA5 (NP_006801.1) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, ELISA.
The antibody against PDIA5 was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 22-140 of human PDIA5 (NP_006801.1) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, ELISA.
| Cat.No | ADA-05675A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | PDIA5 |
| Target Synonyms | PDIR; PDIA5 | Form | Liquid |
| Species Reactivity | Mouse, Rat | Isotype | IgG |
| Storage Buffer | 50% Glycerol, PBS with 0.01% thimerosal, pH7.3. | Purification Method | Affinity purification |
| Positive Samples | Mouse kidney, Mouse liver, Mouse pancreas, Rat liver | Application | ELISA, WB |
| Immunogen Description | Recombinant fusion protein containing a sequence corresponding to amino acids 22-140 of human PDIA5 (NP_006801.1). | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | SSAKVSSLIERISDPKDLKKLLRTRNNVLVLYSKSEVAAENHLRLLSTVAQAVKGQGTICWVDCGDAESRKLCKKMKVDLSPKDKKVELFHYQDGAFHTEYNRAVTFKSIVAFLKDPKG | 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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