Prolyl 4-Hydroxylase, beta Polypeptide (P4HB) (AA 109-214) antibody

Antigen: Prolyl 4-Hydroxylase, beta Polypeptide (P4HB)

Synonyms: DSI, GIT, PDI, PHDB, PDIA1, PO4DB, PO4HB, PROHB, ERBA2L, P4Hbeta, Thbp, ERp59, Pdia1, PDIR, LOC100328595, p55, P4HB, DKFZp469E2031

Binding Site: AA 109-214

Clonality: Monoclonal (34)

Host: Mouse

Reactivity: Cow (Bovine)

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunofluorescence (IF)

Catalog no.: ABIN968267

Additional Information

Alternative name: PDI

Immunogen: Bovine PDI

Cross-Reactivity: Human, Dog (Canine), Rat (Rattus), Mouse (Murine)

Format: Liquid

Isotype: IgG1

Clone: 34

Description: The ER is the site of translation of membrane and secretory proteins. Following synthesis, it shuttles these proteins through a contiguous membrane system to their appropriate destinations. Protein disulfide isomerase (PDI) is an abundant, multifunctional, eukaryotic protein. Although it exhibits ubiquitous expression, it is primarily located in the ER lumen. Here, it functions to catalyze the isomerization of intramolecular disulfide bridges, thereby allowing them to generate their most thermodynamically stable configurations. This role in rearrangement has lead to the classification of PDI as a chaperone. Although protein folding occurs in its absence, PDI may be essential for it to proceed at a physiological relevant rate. In addition, PDI is the beta-subunit of prolyl 4- hydroxylase and is a component of the triglyceride transfer complex. PDI is retained in the ER lumen via its C-terminal -KDEL sequence. Via this sequence, it is continuously recycled back to the ER from other membranous compartments. Thus, PDI is a diverse protein whose primary function may be to correct disulfide bonding and, thus, ensure the most stable conformation of newly synthesized proteins.

Characteristics: 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
4. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.

Molecular Weight: 55 kDa

Comments:

Related Products: ABIN968551, ABIN967389

Application Details

Concentration: 250 µg/ml

Purity: Purified

Purification: Purified from tissue culture supernatant or ascites by affinity chromatography.

Buffer: Aqueous buffered solution containing BSA, glycerol.

Preservative: 0.09% Sodium azide.

Storage: Store undiluted at -20° C.

Research Area: Cancer, Organelles

Restrictions: For Research Use only

Images

Western blot analysis of PDI on HCT-8 cell lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of anti-PDI antibdy.

Publications

Product: Wetterau, Combs, Spinner et al.: "Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex." in: The Journal of biological chemistry, Vol. 265, Issue 17, pp. 9800-7, 1990 (PubMed).

Yamauchi, Yamamoto, Hayashi et al.: "Sequence of membrane-associated thyroid hormone binding protein from bovine liver: its identity with protein disulphide isomerase." in: Biochemical and biophysical research communications, Vol. 146, Issue 3, pp. 1485-92, 1987 (PubMed).

Weissman, Kim: "Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase." in: Nature, Vol. 365, Issue 6442, pp. 185-8, 1993 (PubMed).

Schlegel, Arvan, Lisanti: "Caveolin-1 binding to endoplasmic reticulum membranes and entry into the regulated secretory pathway are regulated by serine phosphorylation. Protein sorting at the level of the endoplasmic reticulum." in: The Journal of biological chemistry, Vol. 276, Issue 6, pp. 4398-408, 2001 (PubMed).

Jenne, Frey, Brugger et al.: "Oligomeric state and stoichiometry of p24 proteins in the early secretory pathway." in: The Journal of biological chemistry, Vol. 277, Issue 48, pp. 46504-11, 2002 (PubMed).