GPAVIECWFVEDASGKGLAKRPGALLLRQGPGEPPPRPDLDPELYLSVHDPAGALQAAFRRYPRGAPAPHCEMSRFVPLPASAKWASGLTPAQNCPRALDGAWLMVSISSPVLSLSSLLRPQPEPQQEPVLITMATVVLTVLTHTPAPRVRLGQDALLDLSFAYMPPTSEAASSLAPGPPPFGLEWRRQHLGKGHLLLAATPGLNGQMPAAQEGAVAFAAWDDDEPWGPWTGNGTFWLPRVQPFQEGTYLATIHLPYLQGQVTLELAVYKPPKVSLMPATLARAAPGEAPPELLCLVSHFYPSGGLEVEWELRGGPGGRSQKAEGQRWLSALRHHSDGSVSLSGHLQPPPVTTEQHGARYACRIHHPSLPASGRSAEVTLEVAGLSGPSLEDSVGLFLSAFLLLGLFKALGWAAVYLSTCKDSKKKAE
Note: The complete
sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is
translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application,
please explicitly request the full and complete sequence of this protein before ordering.
Protein Length
full length protein
Tag Info
N-terminal 10xHis-tagged
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Involved in the association of MHC class I with transporter associated with antigen processing (TAP) and in the assembly of MHC class I with peptide (peptide loading).
Gene References into Functions
The results demonstrated that the mRNA expression levels of tapasin were significantly downregulated in patients with chronic hepatitis B (CHB) compared with in healthy controls and patients with acute hepatitis B Furthermore, the apoptotic rate of CD8+ T cells was increased in patients with CHB compared with in the other two groups.PMID:27510296
Fluctuation and entropy analyses show how tapasin chaperones major histocompatibility complex class I by stabilising it in a peptide-receptive conformation.PMID:26754481
reduction in tapasin expression is associated with tumor progression in colorectal cancerPMID:26310568
Data suggest that tapasin (Tsn) binds to MHC I with suboptimal cargo and thereby adjusts the energy landscape in favor of MHC I complexes with immunodominant epitopes.PMID:26416272
Analysis of expression of tapasin and/or HLA-I may be of value as prognostic tool for glioblastoma multiforme patients, especially when considering immunotherapy.PMID:25175688
Modified TAPBP gene function may contribute to the development of refractory chronic rhinosinusitis via reduction of circulating CD8 lymphocytes.PMID:23640800
Targeted re-sequencing identified rs3106189 at the 5' UTR of TAPBP and rs1052918 at the 3' UTR of TCF3 to be associated with the overall survival of colorectal cancer patients.PMID:23940558
the data indicate that TAPBPR and tapasin bind in a similar orientation to the same face of MHC class I.PMID:24163410
TAPBP polymorphisms may play a role in the development of aspirin-exacerbated respiratory disease.PMID:23736108
isoform lacking exon 3 affects MHC class I-peptide bindingPMID:23519916
Data indicate that the peptide-loading complex (PLC) consists maximally of 2x tapasin-ERp57/MHC I per TAP complex, but one tapasin-ERp57/MHC I in the PLC is essential and sufficient for antigen processing.PMID:22923333
Tapasin discriminates peptide-human leukocyte antigen-A*02:01 complexes formed with natural ligands.PMID:21518758
On infection with human cytomegalovirus tapasin mRNA levels were continuously downregulated during infection, while tapasin transcripts remained stable and long-lived.PMID:21248040
Downregulation of tapasin is associated with a poor clinical outcome for oral squamous cell carcinoma patients and may serve as a prognostic biomarkerPMID:20532727
The interactions of tapasin with both TAP and ERp57 are correlated with strong MHC class I recruitment and assembly enhancement.PMID:20070606
find that in a competitive situation between high- and low-affinity peptides, tapasin mediates the binding of the high-affinity peptide to class I by accelerating the dissociation of the peptide from an unstable intermediate of the binding reaction.PMID:20017190
recruits MHC class I molecules to TAP complex during antigen processingPMID:11823531
tapasin is a modified Mhc class I moleculePMID:11862402
MHC class I molecules can optimize their peptide repertoire over time and that this process is dependent on tapasin.PMID:11970875
tapasin is not required for calreticulin to bind to the alpha1 domain of MHC class I moleculesPMID:11972874
results suggest that tapasin deficiency is another cause of type I bare lymphocyte syndromePMID:12149238
Tapasin enhances the structural stability of TAP1.TAP2 complexes.PMID:12213826
The domain organization of tapasin is an assembly of two core regions of different sizes loosely connected by a linker or loop comprising residues ~85-93.PMID:12463753
tapasin has a essential function of tapasin in quality control of HLA-G moleculesPMID:12582157
A major role for tapasin as a stabilizer of the TAP peptide transporter and consequences for MHC class I expression.PMID:12594855
Downregulation of tapasin in advanced stages of human melanoma may reflect accumulation of alterations in antigen-presenting/processing machinery associated with neoplastic progression. May contribute to immune escape phenotype of human melanoma cells.PMID:12682852
The ERp57-tapasin conjugate can also be modified with the oxidizing agent diamide, indicating that within the pool of ERp57-tapasin complexes the free, non-tapasin-linked CXXC motif exists in both oxidized and reduced statesPMID:13678524
Defects in tapasin and HLA class I antigen expression in primary maxillary sinus SCC lesions may play a role in the clinical course of the maxillary sinus cancer, because these defects were associated with poor prognosis.PMID:14519625
In its role as peptide facilitator, tapasin stabilizes the peptide-free conformation of class I major histocompatibility (MHC) complex molecules in the endoplasmic reticulum and thus increases the number and variety of peptides bound to class I MHC.PMID:14607930
Mutational analysis of tapasin provides insight into aspects of tapasin structure that are crucial to its ability to assist major histocompatibility complex class I assembly.PMID:14978101
Transfection of tapasin into the Panc02 cells did not quantitatively increase MHC class I surface expression or detectably affect MHC class I association with tumor-specific peptides and beta(2)-microglubulin (beta(2)m).PMID:15163903
Defective tapasin transcription and thus absence of HLA-B44 expression is associateed with colorectal tumors.PMID:15455354
Substitutions at position lysine-408 in tapasin are shown to affect the expression of major histocompatibility complex class I molecules at the cell surface, by down-regulating tapasin stabilization of TAP.PMID:15634919
Tapasin association specifically inhibits the escape pathway required for disulfide-bond isomerization within conventional protein substrates, suggesting a specific structural role for ERp57 within the MHC class I peptide-loading complex.PMID:16193070
Down-regulation of tapasin expression was associated with glioblastoma multiformePMID:16322289
Besides beta(2)m and tapasin, an extra unidentified component is also critical for the expression of certain human class I alleles.PMID:17498802
A ternary complex between heavy chain, ERp57, and tapasin was observed and shown to be stabilized by a disulfide between both tapasinheavy chain and tapasin-ERp57.PMID:18039656
Transgenic tapasin establishes hierarchical responses in vivo according to peptide-major histocompatibility complex class I stability.PMID:18196518
In this review, interaction of accessory protein tapasin with HLA-DM crucially influences the selection of peptides that bind to major histocompatibility complex (MHC) molecules during antigen presentation.PMID:18261958
the 2.6 A resolution structure of the tapasin-ERp57 core of the peptide-loading complexPMID:19119025
HLA-B27 polymorphism drives the tapasin dependency, rates of intracellular maturation and expressions of homodimers.PMID:19167761
tapasin conjugation with ERp57 is as critical as its integration into the membrane for efficient MHC class I assembly, surface expression, and Ag presentation to CD8+ T cells.PMID:19701894
The N-terminal region of Tapasin (Tpn) can be recombinantly expressed and adopt a structure, which at least partially resembles that of wild-type Tpn. This region of Tpn features chaperone activity facilitating peptide binding of MHC-I.PMID:19728311
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Subcellular Location
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Tissue Specificity
Neutrophils, mostly in fully differentiated cells.