PDCD1LG2 Human, Sf9

Programmed Cell Death 1 Ligand 2 Human Recombinant, Sf9
Cat. No.
BT7806
Source

Sf9, Baculovirus cells.

Synonyms

Programmed Cell Death 1 Ligand 2, B7 Dendritic Cell Molecule, Programmed Death Ligand 2, Butyrophilin B7-DC, PDCD1 Ligand 2, PDCD1L2, B7-DC, CD273, PD-L2,B7DC, PDL2, PD-1-Ligand 2, CD273 Antigen, PD-1 Ligand 2, BA574F11.2, Btdc.

Appearance
Sterile Filtered colorless solution.
Purity

Greater than 95.0% as determined by SDS-PAGE.

Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

PDCD1LG2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 423 amino acids (20-200a.a.) and having a molecular mass of 47.7kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).
PDCD1LG2 is expressed with a 239 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction

Programmed cell death 1 ligand 2 (PDCD1LG2), also known as B7-DC, plays a crucial role in regulating immune responses. It is involved in the co-stimulation of T cells, which is essential for their activation and proliferation. PDCD1LG2 binds to its receptor, PD-1, on T cells, and this interaction can either enhance or inhibit T cell responses depending on the context. PDCD1LG2 is also involved in the production of interferon gamma (IFN-γ), a key cytokine in immune responses, through a mechanism that is independent of PD-1.

Description

Recombinant human PDCD1LG2 protein was expressed in Sf9 insect cells using a baculovirus expression system. The protein is a single, glycosylated polypeptide chain that consists of 423 amino acids, spanning from amino acid positions 20 to 200a. It has a molecular weight of 47.7 kDa, but due to glycosylation, it appears as a band between 40-57 kDa on SDS-PAGE. The protein contains a 239 amino acid human IgG-His tag fused to its C-terminus, which facilitates purification using proprietary chromatographic techniques.

Physical Appearance
Sterile Filtered, clear and colorless solution.
Formulation

The provided PDCD1LG2 protein solution has a concentration of 1 mg/ml. It is formulated in a buffer containing Phosphate Buffered Saline (PBS) at pH 7.4 and 10% glycerol.

Stability
For short-term storage (up to 2-4 weeks), the protein solution can be stored at 4°C. For long-term storage, it is recommended to store the solution at -20°C. To further enhance stability during long-term storage, consider adding a carrier protein like HSA or BSA to a final concentration of 0.1%. Avoid repeated freezing and thawing of the protein solution.
Purity

The purity of the PDCD1LG2 protein is greater than 95% as determined by SDS-PAGE analysis.

Synonyms

Programmed Cell Death 1 Ligand 2, B7 Dendritic Cell Molecule, Programmed Death Ligand 2, Butyrophilin B7-DC, PDCD1 Ligand 2, PDCD1L2, B7-DC, CD273, PD-L2,B7DC, PDL2, PD-1-Ligand 2, CD273 Antigen, PD-1 Ligand 2, BA574F11.2, Btdc.

Source

Sf9, Baculovirus cells.

Amino Acid Sequence

ADPLFTVTVP KELYIIEHGS NVTLECNFDT GSHVNLGAIT ASLQKVENDT SPHRERATLL EEQLPLGKAS FHIPQVQVRD EGQYQCIIIY GVAWDYKYLT LKVKASYRKI NTHILKVPET DEVELTCQAT GYPLAEVSWP NVSVPANTSH SRTPEGLYQV TSVLRLKPPP GRNFSCVFWN THVRLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH.

Product Science Overview

Introduction

Programmed Cell Death 1 Ligand 2 (PD-L2) is a crucial immunosuppressive molecule that plays a significant role in the regulation of immune responses. It is one of the two known ligands for Programmed Cell Death Protein 1 (PD-1), the other being PD-L1 . PD-L2 is primarily expressed on dendritic cells and a few tumor lines . The recombinant form of PD-L2, produced in Sf9 insect cells, is used extensively in research to study its role in immune modulation and potential therapeutic applications.

Structure and Expression

PD-L2 belongs to the B7 family of proteins and shares structural similarities with PD-L1 . The expression of PD-L2 is more restricted compared to PD-L1 and is mainly found on dendritic cells and macrophages . The recombinant form of PD-L2 (Human Recombinant, Sf9) is produced using the baculovirus expression system in Sf9 insect cells, which allows for high-yield production of the protein with proper folding and post-translational modifications.

Function and Mechanism

PD-L2 interacts with PD-1 on T cells to inhibit their activity and proliferation . This interaction plays a dual role: it helps in maintaining immune homeostasis by preventing overactivation of the immune system, thus reducing the risk of autoimmune diseases, and it also contributes to immune evasion by tumors . By binding to PD-1, PD-L2 transmits inhibitory signals that reduce T-cell receptor signaling, leading to decreased cytokine production and T-cell proliferation .

Clinical Significance

The PD-1/PD-L1 axis has been extensively studied for its role in cancer immunotherapy. However, recent research has highlighted the importance of PD-L2 in cancer progression and patient prognosis . PD-L2 expression has been associated with poor prognosis in various cancers, and its role in immune escape mechanisms makes it a potential target for therapeutic intervention . Understanding the regulatory mechanisms of PD-L2 expression and its interaction with PD-1 can help in developing more effective immunotherapies .

Research and Therapeutic Applications

Recombinant PD-L2 (Human Recombinant, Sf9) is widely used in research to study its biological functions and therapeutic potential. It is used in various assays to investigate the interaction between PD-L2 and PD-1, as well as to screen for potential inhibitors that can block this interaction . Additionally, recombinant PD-L2 is used in preclinical studies to evaluate its efficacy as a therapeutic target in cancer treatment .

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