Recombinant Human Tapasin Protein (His Tag)

Name: Recombinant Human Tapasin Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-4406
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	AAH80574.1
Synonym	NGS17, TAPA, TPN, TPSN
Description	A DNA sequence encoding the human TAPBP (AAH80574.1) (Met1-Val414) was expressed with a His tag at the C-terminus.
Source	HEK293
Predicted N Terminal	Gly 21
AA Sequence	Met1-Val414
Molecular Weight	The recombinant human TAPBP consists 405 a.a. and predicts a molecular mass of 43.5 kDa.
Purity	>90% as determined by SDS-PAGE.
Endotoxin	< 1.0 EU per μg protein as determined by the LAL method.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile PBS, pH 7.4..
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	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).
Subcellular Location	Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Database References	HGNC: 11566 OMIM: 601962 KEGG: hsa:6892 STRING: 9606.ENSP00000404833 UniGene: Hs.370937
Associated Diseases	Bare lymphocyte syndrome 1 (BLS1)
Tissue Specificity	Neutrophils, mostly in fully differentiated cells.

Gene Functions References

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 cancer PMID: 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 binding PMID: 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 biomarker PMID: 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 processing PMID: 11823531
tapasin is a modified Mhc class I molecule PMID: 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 molecules PMID: 11972874
results suggest that tapasin deficiency is another cause of type I bare lymphocyte syndrome PMID: 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 molecules PMID: 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 states PMID: 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 multiforme PMID: 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 complex PMID: 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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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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