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TPSAB1 Antibody (Center)

Peptide Affinity Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - TPSAB1 Antibody (Center) AP5440c
    Anti-TPSAB1 Antibody (Center) at 1:1000 dilution + A431 whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 31 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
  • 4 - TPSAB1 Antibody (Center) AP5440c
    TPSAB1 Antibody (Center) (Cat. #AP5440c) flow cytometric analysis of 293 cells (right histogram) compared to a negative control cell (left histogram).FITC-conjugated goat-anti-rabbit secondary antibodies were used for the analysis.
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Product info
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, FC, E
Primary Accession Q15661
Other Accession NP_003285
Reactivity Human
Host Rabbit
Clonality Polyclonal
Isotype Rabbit Ig
Calculated MW 30515 Da
Additional info
Gene ID 7177
Other Names Tryptase alpha/beta-1, Tryptase-1, Tryptase I, Tryptase alpha-1, TPSAB1, TPS1, TPS2, TPSB1
Target/Specificity This TPSAB1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 61-87 amino acids from the Central region of human TPSAB1.
Dilution WB~~1:1000
FC~~1:10~50
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsTPSAB1 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name TPSAB1
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)
Research Areas

BACKGROUND

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. 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.

REFERENCES

Trivedi, N.N., et al. J. Allergy Clin. Immunol. 124(5):1099-1105(2009)
Radhakrishnan, Y., et al. Biol. Reprod. 81(4):647-656(2009)
Schiemann, F., et al. J. Immunol. 183(4):2223-2231(2009)

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