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Brand: ProteoGenix

Recombinant Human TAP1, N-His

Host species:
Escherichia coli (E.coli)
Origin species:
Human
Molecular weight:
33.24 kDa

$392.00

100ug + 392 loyalty points
Tyr525–Glu808
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Recombinant Human TAP1, N-His

Recombinant Human TAP1, N-His

Product name Recombinant Human TAP1, N-His
Origin species Human
Expression system Prokaryotic expression
Molecular weight 33.24 kDa
Buffer Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Delivery condition Dry Ice
Delivery lead time in business days 3-5 days if in stock; 3-5 weeks if production needed
Storage condition 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
Brand ProteoGenix
Host species Escherichia coli (E.coli)
Fragment Type Tyr525-Glu808
Aliases /Synonyms TAP1, APT1, Peptide transporter involved in antigen processing 1, Really interesting new gene 4 protein, Peptide transporter TAP1, Peptide transporter PSF1, RING4, Antigen peptide transporter 1, PSF-1, ABCB2, Y3, Peptide supply factor 1, PSF1, ATP-binding cassette sub-family B member 2
Reference ARO-P12869
Note For research use only.
Molecular Constructor
Tyr525–Glu808

Recombinant Human TAP1: Structure, Activity, and Application

Introduction

Recombinant Human TAP1 (Transporter associated with Antigen Processing 1) is a protein that plays a crucial role in the immune response. It is a member of the ATP-binding cassette (ABC) transporter family and is involved in the transport of peptides from the cytosol into the endoplasmic reticulum (ER) for loading onto major histocompatibility complex (MHC) class I molecules. In this article, we will discuss the structure, activity, and application of Recombinant Human TAP1.

Structure of Recombinant Human TAP1

Recombinant Human TAP1 is a transmembrane protein that consists of 808 amino acids. It has a molecular weight of approximately 90 kDa and is composed of two subunits, TAP1 and TAP2. The TAP1 subunit contains six transmembrane domains (TMDs) and a nucleotide-binding domain (NBD), while the TAP2 subunit contains one TMD and one NBD. These two subunits form a heterodimer that is responsible for the transport of peptides.

Transmembrane Domains

The TMDs of TAP1 are responsible for the translocation of peptides from the cytosol into the ER. These domains are highly conserved and contain hydrophobic amino acids that allow them to span the membrane. The TMDs also contain a signature sequence, known as the Walker A motif, which is involved in ATP binding and hydrolysis.

Nucleotide-Binding Domains

The NBDs of TAP1 are responsible for the binding and hydrolysis of ATP, which provides the energy for peptide transport. These domains also contain the Walker B motif, which is involved in ATP hydrolysis. The NBDs are connected to the TMDs by a linker region, which is crucial for the proper functioning of TAP1.

Activity of Recombinant Human TAP1

The main function of Recombinant Human TAP1 is to transport peptides from the cytosol into the ER for loading onto MHC class I molecules. This process is essential for the presentation of antigens to T cells and the initiation of an immune response. TAP1 achieves this by utilizing the energy from ATP hydrolysis to pump peptides against a concentration gradient from the cytosol into the ER lumen.

In addition to its role in antigen processing, TAP1 also plays a crucial role in the maintenance of cellular homeostasis. It has been shown to transport a wide range of endogenous peptides, including viral peptides, self-peptides, and peptides derived from damaged proteins. This function helps to prevent the accumulation of toxic peptides in the cell and ensures proper immune surveillance.

Application of Recombinant Human TAP1

Recombinant Human TAP1 has a wide range of applications in research, diagnostics, and therapeutics. Its role in antigen processing makes it a valuable tool for studying the immune response and developing vaccines. Recombinant TAP1 can also be used in diagnostic assays to detect the presence of specific peptides, such as viral peptides, in patient samples. In addition, TAP1 has been investigated as a potential therapeutic target for diseases such as cancer and autoimmune disorders.

Furthermore, the production of recombinant TAP1 has allowed for the development of TAP1-deficient cell lines, which can be used to study the effects of TAP1 deficiency on antigen presentation and immune response. These cell lines

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