TPP2 antibody

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Description
This gene encodes a mammalian peptidase that, at neutral pH, removes tripeptides from the N terminus of longer peptides. The protein has a specialized function that is essential for some MHC class I antigen presentation. The protein is a high molecular mass serine exopeptidase; the amino acid sequence surrounding the serine residue at the active site is similar to the peptidases of the subtilisin class rather than the trypsin class.
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Product specifications
Category | Primary Antibodies |
Immunogen Target | tripeptidyl peptidase II (TPP2) |
Host | Rabbit |
Reactivity | Human, Mouse |
Recommended Dilution | WB: 1:500-1:2000; IP: 1:500-1:1000; IHC: 1:50-1:500; IF: 1:20-1:200 |
Clonality | polyclonal |
Conjugation | Unconjugated |
Isotype | IgG |
Observed MW | 138 kDa |
Purity | ≥95% as determined by SDS-PAGE |
Purification | Immunogen affinity purified |
Size 1 | 100µg |
Form | liquid |
Tested Applications | ELISA, WB, IHC, IF, FC |
Storage | PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20℃ for 12 months(Avoid repeated freeze / thaw cycles.) |
UniProt ID | P29144 |
Gene ID | 7174 |
Alias | Tripeptidyl-peptidase 2 (TPP-2),Tripeptidyl aminopeptidase,Tripeptidyl-peptidase II (TPP-II),TPP2 |
Background | Antibody anti-TPP2 |
Status | RUO |
Note | Mol. Weight 138 kDa |
Descripción
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TPP2 antibody
This gene encodes a mammalian peptidase that, at neutral pH, removes tripeptides from the N terminus of longer peptides. The protein has a specialized function that is essential for some MHC class I antigen presentation. The protein is a high molecular mass serine exopeptidase; the amino acid sequence surrounding the serine residue at the active site is similar to the peptidases of the subtilisin class rather than the trypsin class.
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TPP2 Antibody is a Rabbit Polyclonal antibody against TPP2. This gene encodes a mammalian peptidase that, at neutral pH, removes tripeptides from the N terminus of longer peptides. The protein has a specialized function that is essential for some MHC class I antigen presentation. The protein is a high molecular mass serine exopeptidase; the amino acid sequence surrounding the serine residue at the active site is similar to the peptidases of the subtilisin class rather than the trypsin class.
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