GRP78 antibody (AA 525-628)

Catalog No. ABIN968290

Product Details anti-GRP78 Antibody

Target: GRP78 (HSPA5) (Heat Shock 70kDa Protein 5 (Glucose-Regulated Protein, 78kDa) (HSPA5))

Binding Specificity: AA 525-628

Reactivity: Human, Rat, Mouse, Dog

Host: Mouse

Clonality: Monoclonal

Conjugate: This GRP78 antibody is un-conjugated

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

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

Characteristics: 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. 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.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.

Purification: The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.

Immunogen: Human BiP/GRP78 aa. 525-628

Clone: 40-BiP

Isotype: IgG2a

Application Details

Comment:

Related Products: ABIN968587, ABIN967389

Restrictions: For Research Use only

Handling

Format: Liquid

Concentration: 250 μg/mL

Buffer: Aqueous buffered solution containing BSA, glycerol, and ≤0.09 % sodium azide.

Preservative: Sodium azide

Precaution of Use: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Storage: -20 °C

Storage Comment: Store undiluted at -20°C.

References for anti-GRP78 antibody (ABIN968290)

Han, Kim, Lee, Lee, Lee, Ohba, Kuroki, Suh, Ryu: "Localization of phospholipase D1 to caveolin-enriched membrane via palmitoylation: implications for epidermal growth factor signaling." in: Molecular biology of the cell, Vol. 13, Issue 11, pp. 3976-88, (2002) (PubMed).

Waelter, Boeddrich, Lurz, Scherzinger, Lueder, Lehrach, Wanker: "Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation." in: Molecular biology of the cell, Vol. 12, Issue 5, pp. 1393-407, (2001) (PubMed).

Yamazaki, Chang, Haass, Ihara: "Accumulation and aggregation of amyloid beta-protein in late endosomes of Niemann-pick type C cells." in: The Journal of biological chemistry, Vol. 276, Issue 6, pp. 4454-60, (2001) (PubMed).

Ting, Lee: "Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation." in: DNA (Mary Ann Liebert, Inc.), Vol. 7, Issue 4, pp. 275-86, (1988) (PubMed).

Target Details for GRP78

Target: GRP78 (HSPA5) (Heat Shock 70kDa Protein 5 (Glucose-Regulated Protein, 78kDa) (HSPA5))

Alternative Name: BiP (HSPA5 Products)

Background: Synthesis of nascent proteins occurs at sites on the endoplasmic reticulum (ER) called translocons. Translocon proteins form a pore in the membrane that allow passage of the newly synthesized protein from the ribosome into the ER lumen. As the nascent protein enters the lumen, it is bound by BiP (binding protein), the major chaperone of the ER. This protein is identical to the 78kDa glucose regulated protein, GRP78. BiP binds short hydrophobic sequences of the emerging peptide and prevents denaturation or nonspecific aggregation. Hydrolysis of ATP by BiP results in the release of the nascent protein which quickly assumes its proper conformation. However, if folding is incorrect, BiP again binds the protein and prevents its exit from the ER. In addition, BiP binding is thought to enhance the movement of secretory polypeptides across the ER membrane, but it is not required for protein translocation. It is 60% identical to Hsp70 and is similarly increased by conditions that produce incorrectly folded proteins. Thus, BiP is a chaperone of the ER lumen that binds misfolded or unassembled secretory proteins and ensures proper movement of proteins from the ER to the Golgi apparatus.

Molecular Weight: 78 kDa

Pathways: Thyroid Hormone Synthesis, ER-Nucleus Signaling