| Product Name | Human Aspartyl/asparaginyl beta-hydroxylase (ASPH) ELISA Kit |
|---|---|
| Description | ASPH is is thought to play an important role in calcium homeostasis. The gene is expressed from two promoters and undergoes extensive alternative splicing. The encoded set of proteins share varying amounts of overlap near their N-termini but have substantial variations in their C-terminal domains resulting in distinct functional properties. The longest isoforms (a and f) include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the epidermal growth factor (EGF)-like domains of some proteins, including protein C, coagulation factors VII, IX, and X, and the complement factors C1R and C1S. Other isoforms differ primarily in the C-terminal sequence and lack the hydroxylase domain, and some have been localized to the endoplasmic and sarcoplasmic reticulum. This assay has high sensitivity and excellent specificity for detection of Human ASPH. No significant cross-reactivity or interference between Human ASPH and analogues was observed. |
| Synonyms | AAH, BAH, CASQ2BP1, HAAH, JCTN, junctin, A beta H-J-J|aspartyl/asparaginyl-beta-hydroxylase|cardiac junctin|humbug|junctate|peptide-aspartate beta-dioxygenase |
| Method | Sandwich ELISA |
| Detection Range | 0.156-10 ng/mL |
| Sensitivity | 0.057 ng/mL |
| Reactivity | Human |
| Sample Types | Serum, Plasma, Other biological fluids. |
| Background | ASPH is is thought to play an important role in calcium homeostasis. The gene is expressed from two promoters and undergoes extensive alternative splicing. The encoded set of proteins share varying amounts of overlap near their N-termini but have substantial variations in their C-terminal domains resulting in distinct functional properties. The longest isoforms (a and f) include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the epidermal growth factor (EGF)-like domains of some proteins, including protein C, coagulation factors VII, IX, and X, and the complement factors C1R and C1S. Other isoforms differ primarily in the C-terminal sequence and lack the hydroxylase domain, and some have been localized to the endoplasmic and sarcoplasmic reticulum. |
| Supplier | Abebio |
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