Recombinant Proteins

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ULBP1 Human

UL16 Binding Protein 1 Human Recombinant

Recombinant Human ULBP1, produced in E.coli, is a single, non-glycosylated polypeptide chain comprising 216 amino acids (26-216) with a molecular weight of 25.0 kDa. This ULBP1 protein is fused to a 25 amino acid His-tag at its N-terminus and is purified through standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT23732
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

ULBP1 Human, Sf9

UL16 Binding Protein 1 Human Recombinant, Sf9

Recombinant human ULBP1, produced in Sf9 insect cells using a baculovirus expression system, is a single, glycosylated polypeptide chain. It consists of 200 amino acids (residues 26-216) and has a molecular mass of 23.4 kDa. On SDS-PAGE, the apparent molecular size will be approximately 20-40 kDa due to glycosylation. ULBP1 is fused to a 6-amino acid IgG His-tag at its C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23811
Source
Sf9, Baculovirus cells.
Appearance
Clear, sterile-filtered solution.

ULBP4 Human

UL16 Binding Protein 4 Human Recombinant

Recombinant Human ULBP4, produced in E. coli, is a single, non-glycosylated polypeptide chain representing Isoform 3 of Q8TD07. It comprises 192 amino acids, including a 10 amino acid His tag located at the N-terminus. The calculated molecular mass of the protein is 22 kDa.
Shipped with Ice Packs
Cat. No.
BT24257
Source
Escherichia Coli.
Appearance
Sterile filtered white lyophilized (freeze-dried) powder.

ULBP2 Human

UL16 Binding Protein 2 Human Recombinant

Recombinant Human ULBP2, produced in E. coli, is a single polypeptide chain comprising 216 amino acids (26-216) with a molecular weight of 24.3 kDa. It includes a 25 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT23914
Source
E.coli.
Appearance
A sterile, colorless solution.

ULBP2 Human, Sf9

UL16 Binding Protein 2 Human Recombinant, Sf9

Recombinant Human ULBP2, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain consisting of 200 amino acids (26-216a.a). It has a molecular mass of 22.7kDa, but on SDS-PAGE, it appears at approximately 28-40kDa. The protein is fused to a 9 amino acid His-tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24001
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless, and sterile-filtered solution.

ULBP3 Human

UL16 Binding Protein 3 Human Recombinant

ULBP3 Human Recombinant is a laboratory-produced protein designed to mimic the structure and function of naturally occurring human ULBP3. It is expressed in E. coli bacteria and undergoes a purification process to ensure its quality and purity. This recombinant protein is a single polypeptide chain consisting of 198 amino acids, representing the primary structure of ULBP3. Importantly, it lacks any post-translational modifications like glycosylation, making it a simplified version of the naturally occurring protein. For ease of handling and storage, it is provided in a lyophilized (freeze-dried) powder form.
Shipped with Ice Packs
Cat. No.
BT24081
Source
Escherichia Coli.
Appearance
White, solid substance in a powdered form.

ULBP3 Human, Sf9

UL16 Binding Protein 3 Human Recombinant, Sf9

Recombinant human ULBP3 protein has been produced using Sf9 insect cells infected with a baculovirus expression system. This method results in a glycosylated polypeptide chain containing 430 amino acids, encompassing residues 30 to 217a.a of the ULBP3 protein. The recombinant ULBP3 has a molecular weight of approximately 49.3 kDa. To facilitate purification and detection, a 239 amino acid hIgG-His-Tag is fused to the C-terminus of the protein. The protein is purified to a high degree using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT24183
Source

Sf9, Baculovirus cells.

Appearance

The ULBP3 protein solution appears as a clear and colorless liquid after sterilization by filtration.

Definition and Classification

UL16 binding proteins (ULBPs) are a family of MHC class I-related molecules that were initially identified as targets of the human cytomegalovirus (HCMV) glycoprotein, UL16 . These proteins are also known as retinoic acid early transcripts (RAET1) and are ligands for the NKG2D receptor, an activating receptor expressed on natural killer (NK) cells and certain T cells . The ULBP family includes several members, such as ULBP1, ULBP2, and ULBP3, each with distinct but related functions .

Biological Properties

Key Biological Properties: ULBPs are glycoproteins that are structurally related to MHC class I molecules but lack the α3 domain and the transmembrane segment . They are anchored to the cell membrane via a glycosylphosphatidylinositol (GPI) anchor .

Expression Patterns and Tissue Distribution: ULBPs are expressed on the surface of various cell types, including tumor cells and cells under stress conditions such as infection . They are frequently upregulated in response to cellular stress, infection, and transformation . For example, ULBP1 is upregulated during HCMV infection .

Biological Functions

Primary Biological Functions: ULBPs function as stress-induced ligands for the NKG2D receptor, mediating the activation of NK cells and certain T cells . This interaction plays a crucial role in immune surveillance by enabling the immune system to recognize and eliminate stressed, infected, or transformed cells .

Role in Immune Responses and Pathogen Recognition: By binding to the NKG2D receptor, ULBPs activate NK cells and cytotoxic T cells, leading to the destruction of target cells . This mechanism is vital for the immune response against tumors and viral infections .

Modes of Action

Mechanisms with Other Molecules and Cells: ULBPs interact with the NKG2D receptor on NK cells and certain T cells . This binding triggers a series of downstream signaling cascades that result in the activation of these immune cells .

Binding Partners and Downstream Signaling Cascades: Upon binding to NKG2D, ULBPs induce marked protein tyrosine phosphorylation and activate several signaling pathways, including the Janus kinase 2 (JAK2), STAT5, extracellular signal-regulated kinase (ERK), mitogen-activated protein kinase (MAPK), and phosphatidylinositol 3-kinase (PI3K)/Akt pathways . These pathways are crucial for the activation and function of NK cells and cytotoxic T cells .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: The expression of ULBPs is regulated at both the transcriptional and post-transcriptional levels . For instance, the unfolded protein response pathways during endoplasmic reticulum (ER) stress can upregulate ULBP expression via the protein kinase RNA-like ER kinase-activating factor 4-C/EBP homologous protein (PERK-ATF4-CHOP) pathway .

Transcriptional Regulation and Post-Translational Modifications: ULBPs undergo various post-translational modifications, including glycosylation, which are essential for their stability and function . Additionally, the proteolytic release of soluble ULBPs from tumor cells can modulate their activity and availability .

Applications

Biomedical Research: ULBPs are valuable tools in studying immune responses and the mechanisms of immune surveillance . They are frequently used in research to understand how the immune system recognizes and eliminates stressed or transformed cells .

Diagnostic Tools and Therapeutic Strategies: ULBPs have potential applications in cancer immunotherapy and the development of diagnostic tools for detecting tumors and infections . Their ability to activate NK cells and cytotoxic T cells makes them promising candidates for therapeutic interventions .

Role in the Life Cycle

Role Throughout the Life Cycle: ULBPs play a critical role in immune surveillance throughout the life cycle, from development to aging and disease . Their expression and activity are tightly regulated to ensure the effective elimination of stressed, infected, or transformed cells while avoiding damage to normal tissues .

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