Recombinant Human Tapasin (TAPBP) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-00628P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Tapasin (TAPBP) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-00628P
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Product Overview

Description Recombinant Human Tapasin (TAPBP) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb O15533
Target Symbol TAPBP
Synonyms (TPN)(TPSN)(NGS-17)(TAP-associated protein)(TAP-binding protein)
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His&C-Myc
Target Protein Sequence GPAVIECWFVEDASGKGLAKRPGALLLRQGPGEPPPRPDLDPELYLSVHDPAGALQAAFRRYPRGAPAPHCEMSRFVPLPASAKWASGLTPAQNCPRALDGAWLMVSISSPVLSLSSLLRPQPEPQQEPVLITMATVVLTVLTHTPAPRVRLGQDALLDLSFAYMPPTSEAASSLAPGPPPFGLEWRRQHLGKGHLLLAATPGLNGQMPAAQEGAVAFAAWDDDEPWGPWTGNGTFWLPTVQPFQEGTYLATIHLPYLQGQVTLELAVYKPPKVSLMPATLARAAPGEAPPELLCLVSHFYPSGGLEVEWELRGGPGGRSQKAEGQRWLSALRHHSDGSVSLSGHLQPPPVTTEQHGARYACRIHHPSLPASGRSAEVTLEVAGLSGPSLEDSV
Expression Range 21-414aa
Protein Length Partial
Mol. Weight 49.4 kDa
Research Area Immunology
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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: 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.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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