1μg (R: reducing condition, N: non-reducing condition).
Endothelin B Receptor mFc Chimera Protein, Human
Endothelin B Receptor mFc Chimera Protein, Human
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Product Details
Product Details
Product Specification
| Species | Human |
| Synonyms | Endothelin receptor type B; EDNRB; ET-B; ET-BR; Endothelin receptor non-selective type; ETRB |
| Accession | NP_000106.1 |
| Amino Acid Sequence | Glu27-Lys101 with Mouse IgG2a Fc at C-Terminus |
| Expression System | HEK293 |
| Molecular Weight | 40-55kDa (Reducing) |
| Purity | ＞95% by SDS-PAGE &＞90% by SEC-HPLC |
| Endotoxin | <0.1EU/μg |
| Conjugation | Unconjugated |
| Tag | Mouse IgG2a Fc |
| Physical Appearance | Lyophilized Powder |
| Storage Buffer | PBS, PH7.4, 5% trehalose |
| Reconstitution | Reconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation. |
| Stability & Storage | · 12 months from date of receipt, lyophilized powder stored at -20 to -80℃. |
| Reference | 1.Marazziti, D. et al. (1997) Genomics, 45:68. |
Background
GPR37 (G-protein coupled receptor 37), also known as ETBR-LP-1 (endothelin B receptor-like protein 1) or PAELR (Parkin-associated endothelin receptor-like receptor), is a 587 amino acid (aa), 7-transmembrane receptor for the neuroprotective and glioprotective factor prosaposin. It is predominantly expressed in neuronal cells, particularly in cerebellar Purkinje cells and the hippocampus. GPR37 is a substrate of the E3 ubiquitin ligase, parkin, which is upregulated during endoplasmic reticulum stress. In a juvenile form of Parkinson's disease, the accumulation of GPR37 contributes to stress-induced neuronal cell death. The extracellular domains (aa 27-265) of human and mouse GPR37 share 68% amino acid identity.
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SDS-PAGE
SEC-HPLC
The purity of Endothelin B Receptor mFc Chimera Protein, Human is greater than 90% as determined by SEC-HPLC.
ELISA
Immobilized EDNRB Rabbit pAb (A2908) at 2.0μg/mL (100μL/well) can bind Endothelin B Receptor mFc Chimera Protein, Human (Cat. No. UA011122) with EC50 of 1.13-1.38 ng/mL.
