Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | XP_005590891.2 |
express system | E.coli |
product tag | N-His |
purity | > 95% as determined by Tris-Bis PAGE |
background | TPSAB1, namely tryptase alpha/beta-1, is a serine protease with trypsinlike activity. TPSAB1 is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. It may play a role in innate immunity. Diseases associated with TPSAB1 include mastocytosis and systemic mastocytosis. |
molecular weight | The protein has a predicted MW of 28.57kDa. The protein migrates to 30-33kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Cynomolgus TPSAB1 protein 2980
$315.00 – $1,050.00
Summary
- Expression: E.coli
- Pure: Yes (SDS-PAGE)
- Amino Acid Range: Ile38-Pro282
Cynomolgus TPSAB1 protein 2980
protein |
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Size and concentration 100, 500µg and liquid |
Form Liquid |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped with dry ice. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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TPSAB1, namely tryptase alpha/beta-1, is a serine protease with trypsinlike activity. TPSAB1 is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. It may play a role in innate immunity. Diseases associated with TPSAB1 include mastocytosis and systemic mastocytosis. |
Protein names Tryptase alpha/beta-1 (Tryptase-1) (EC 3.4.21.59) (Tryptase I) (Tryptase alpha-1) |
Protein family Peptidase S1 family, Tryptase subfamily |
Mass 30515Da |
Function Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. May play a role in innate immunity. Isoform 2 cleaves large substrates, such as fibronectin, more efficiently than isoform 1, but seems less efficient toward small substrates (PubMed:18854315). {ECO:0000250, ECO:0000250|UniProtKB:P21845, ECO:0000269|PubMed:18854315}. |
Catalytic activity CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more restricted specificity than trypsin.; EC=3.4.21.59; |
Subellular location Secreted. Note=Released from the secretory granules upon mast cell activation. {ECO:0000250}. |
Tissues Isoform 1 and isoform 2 are expressed in lung, stomach, spleen, heart and skin; in these tissues, isoform 1 is predominant. Isoform 2 is expressed in aorta, spleen, and breast tumor, with highest levels in the endothelial cells of some blood vessels surrounding the aorta, as well as those surrounding the tumor and low levels, if any, in mast cells (at protein level). {ECO:0000269|PubMed:18854315}. |
Structure Homotetramer. The active tetramer is converted to inactive monomers at neutral and acidic pH in the absence of heparin. Low concentrations of inactive monomers become active monomers at pH 6.0 in the presence of heparin. When the concentration of active monomers is higher, they convert to active monomers and then to active tetramers. These monomers are active and functionally distinct from the tetrameric enzyme. In contrast to the hidden active sites in the tetrameric form, the active site of the monomeric form is accessible for macromolecular proteins and inhibitors eg: fibrinogen which is a substrate for the monomeric but not for the tetrameric form. The monomeric form forms a complex with SERPINB6. {ECO:0000269|PubMed:18039527}. |
Target Relevance information above includes information from UniProt accession: Q15661 |
The UniProt Consortium |
Publications
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