Anti-Mast Cell Tryptase Picoband Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P, E |
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Primary Accession | Q15661 |
Host | Rabbit |
Reactivity | Human |
Clonality | Polyclonal |
Format | Lyophilized |
Description | Rabbit IgG polyclonal antibody for Tryptase alpha/beta-1(TPSAB1) detection. Tested with WB, IHC-P, ELISA in Human. |
Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
Gene ID | 7177 |
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Other Names | Tryptase alpha/beta-1, Tryptase-1, 3.4.21.59, Tryptase I, Tryptase alpha-1, TPSAB1, TPS1, TPS2, TPSB1 |
Calculated MW | 30515 MW KDa |
Application Details | Immunohistochemistry(Paraffin-embedded Section), 0.5-1 µg/ml, Human, By Heat ELISA , 0.1-0.5 µg/ml, Human, - Western blot, 0.1-0.5 µg/ml, Human |
Subcellular Localization | Secreted. Released from the secretory granules upon mast cell activation. . |
Tissue Specificity | 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). . |
Protein Name | Tryptase alpha/beta-1 |
Contents | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3. |
Immunogen | E. coli-derived human Mast Cell Tryptase recombinant protein (Position: H65-P275). Human Mast Cell Tryptase shares 77% and 76.1% amino acid (aa) sequence identity with mouse and rat Mast Cell Tryptase, respectively. |
Purification | Immunogen affinity purified. |
Cross Reactivity | No cross reactivity with other proteins |
Storage | At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing. |
Name | TPSAB1 |
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Synonyms | TPS1, TPS2, TPSB1 |
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). |
Cellular Location | Secreted. Note=Released from the secretory granules upon mast cell activation. |
Tissue Location | 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) |
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Provided below are standard protocols that you may find useful for product applications.
Background
Tryptase alpha-1 and tryptase beta-1 are enzymes that in humans are encoded by the same TPSAB1 gene. Tryptases comprise a family of trypsin-like serine proteases, the peptidase family S1. Tryptases are enzymatically active only as heparin-stabilized tetramers, and they are resistant to all known endogenous proteinase inhibitors. Several tryptase genes are clustered on chromosome 16p13.3. These genes are characterized by several distinct features. They have a highly conserved 3' UTR and contain tandem repeat sequences at the 5' flank and 3' UTR which are thought to play a role in regulation of the mRNA stability. In addition, these genes have an intron immediately upstream of the initiator Met codon, which separates the site of transcription initiation from protein coding sequence. This feature is characteristic of tryptases but is unusual in other genes. The alleles of this gene exhibit an unusual amount of sequence variation, such that the alleles were once thought to represent two separate genes, alpha and beta 1. Beta tryptases appear to be the main isoenzymes expressed in mast cells; whereas in basophils, alpha tryptases predominate. Tryptases have been implicated as mediators in the pathogenesis of asthma and other allergic and inflammatory disorders.
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