Recombinant Proteins

LBP
p53
CEA
HLA
TCL
TTC
NPM
MAF
Bax
BID

LBP Human, HEK

Lipopolysaccarid Binding Protein, Human Recombinant, HEK

Recombinant human LBP is a purified protein produced in the laboratory. This single-chain protein consists of 462 amino acids (specifically amino acids 26-481 of the native LBP sequence) and has a molecular weight of 51.7 kDa. To facilitate purification and research applications, a 6-amino acid histidine tag is added to the C-terminus of the protein.
Shipped with Ice Packs
Cat. No.
BT3318
Source

HEK293 Cells.

Appearance
White powder, freeze-dried.

LBP Mouse

Lipopolysaccaride Mouse Recombinant

Recombinant Mouse LBP is produced in a serum-free medium using mouse LBP transfected CHO-cells. For transfection purposes, the complete mouse LBP cDNA was first amplified via PCR and then cloned into the pPOL-DHFR expression vector. Rm LBP production was facilitated by a his-tag through metal affinity purification with Talon, and the process was monitored using SDS-PAGE. The analysis reveals a 58kDa band on the SDS-PAGE. Please note: The His-tag located at the LBP's c-terminal end does not have a protease site and cannot be cleaved.
Shipped with Ice Packs
Cat. No.
BT3378
Source
Chinese Hamster Ovarian Cells (CHO).
Appearance
Sterile Filtered White lyophilized powder.

LBP Human

Lipopolysaccaride Human Recombinant

Recombinant Human LBP is produced through a process involving Chinese hamster ovary (CHO) cells that have been specifically engineered to express human LBP in a serum-free environment. Prior to this, the complete human LBP cDNA sequence was amplified using PCR and then inserted into a specialized expression vector known as p-POL-DHFR. The purification process involves utilizing a histidine tag (his-tag) attached to the LBP molecule, allowing for affinity purification using a metal ion resin (Talon). The purity is then verified through SDS-PAGE, revealing a distinct band at the expected molecular weight of 58kDa. It's important to note that the his-tag used in this process lacks a protease cleavage site, meaning it remains permanently attached to the recombinant LBP.
Shipped with Ice Packs
Cat. No.
BT3146
Source
Chinese Hamster Ovarian Cells (CHO).
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Definition and Classification

Lipopolysaccharide Binding Protein (LBP) is a soluble acute-phase protein that plays a crucial role in the immune response to bacterial infections. It binds to bacterial lipopolysaccharides (LPS), which are components of the outer membrane of Gram-negative bacteria, and presents them to cell surface receptors such as CD14 and TLR4 . LBP is classified as an acute-phase protein due to its rapid increase in concentration in response to inflammation.

Biological Properties

Key Biological Properties: LBP is known for its ability to bind LPS and facilitate its recognition by the immune system. This binding is essential for the activation of immune responses against Gram-negative bacteria .

Expression Patterns: LBP is primarily expressed in the liver and is secreted into the bloodstream. It is also found in other tissues such as the lungs and intestines .

Tissue Distribution: LBP is predominantly found in the liver, but it is also present in other tissues including the lungs, intestines, and blood plasma .

Biological Functions

Primary Biological Functions: The primary function of LBP is to bind LPS and present it to CD14 and TLR4 receptors on immune cells, thereby initiating an immune response . This process is critical for the detection and elimination of Gram-negative bacteria.

Role in Immune Responses: LBP plays a significant role in the innate immune response by recognizing and binding to LPS, which triggers the activation of immune cells and the production of inflammatory cytokines .

Pathogen Recognition: By binding to LPS, LBP helps the immune system recognize and respond to Gram-negative bacterial infections .

Modes of Action

Mechanisms with Other Molecules and Cells: LBP interacts with CD14 and TLR4 receptors on the surface of immune cells. This interaction facilitates the transfer of LPS to these receptors, leading to the activation of downstream signaling pathways .

Binding Partners: The primary binding partners of LBP are LPS, CD14, and TLR4 .

Downstream Signaling Cascades: Upon binding to LPS, LBP facilitates the transfer of LPS to CD14 and TLR4, which activates downstream signaling pathways such as the NF-κB pathway. This results in the production of pro-inflammatory cytokines and the activation of immune responses .

Regulatory Mechanisms

Regulatory Mechanisms: The expression and activity of LBP are regulated at multiple levels, including transcriptional and post-translational modifications .

Transcriptional Regulation: The transcription of the LBP gene is upregulated in response to inflammatory signals such as cytokines (e.g., IL-6) and bacterial infections .

Post-Translational Modifications: LBP undergoes various post-translational modifications that can affect its stability, localization, and activity .

Applications

Biomedical Research: LBP is used as a biomarker for the detection of bacterial infections and sepsis .

Diagnostic Tools: LBP levels in the blood can be measured to diagnose and monitor bacterial infections and inflammatory conditions .

Therapeutic Strategies: Targeting LBP or its interactions with LPS and immune receptors is being explored as a potential therapeutic strategy for treating sepsis and other inflammatory diseases .

Role in the Life Cycle

Role Throughout the Life Cycle: LBP plays a critical role in the immune system throughout the life cycle. It is involved in the early detection and response to bacterial infections, which is essential for maintaining health and preventing disease .

From Development to Aging and Disease: The expression and activity of LBP can be influenced by various factors throughout life, including developmental stages, aging, and the presence of diseases such as infections and chronic inflammatory conditions .

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