ASPH (75-270, His-Tag) Human Protein
Specifications
| Product Data | |
| Species | Human |
|---|---|
| Expression Host | E. coli |
| Expression cDNA Clone or AA Sequence | |
| Tag | His-Tag |
| Predicted MW | 24.5 kDa (217aa) confirmed by MALDI-TOF (Molecular weight on SDS-PAGE will appear higher) |
| Concentration | 1mg/ml (determined by Bradford assay) |
| Purity | > 90% by SDS-PAGE |
| Presentation State | Purified |
| Buffer | Liquid in. 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 10% glycerol |
| Preparation | Liquid purified protein |
| Recommended Dilution | SDS-PAGE |
| Protein Description | Recombinant human ASPH protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Storage | Can be stored at +2°C to +8°C for 1 week. For long term storage, aliquot and store at -20°C to -80C. Avoid repeated freezing and thawing cycles. |
| Stability | Shelf life: one year from despatch. |
| Shipping | Blue Ice |
| Reference Data | |
| RefSeq | NP_001158227.1 |
| Locus ID | 444 |
| UniProt ID | Q12797 |
| Cytogenetics | 8q12.3 |
| Synonyms | Aspartyl/asparaginyl beta-hydroxylase, AAH, BAH, CASQ2BP1, HAAH, JCTN, junctin, Aspartyl/asparaginyl beta-hydroxylase ASP beta hydroxylase, Aspartyl/asparaginyl beta hydroxylase, Peptide aspartate beta dioxygenase |
| Summary | This gene 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. Some of these isoforms are found in complexes with calsequestrin, triadin, and the ryanodine receptor, and have been shown to regulate calcium release from the sarcoplasmic reticulum. Some isoforms have been implicated in metastasis. provided by RefSeq, Sep 2009 |
| Protein Categories | Growth Factors, Intracellular Proteins, Membrane Proteins |
| Protein Families | Druggable Genome, Transmembrane |
Reviews
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Resources
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