tPA Human, Sf9

Tissue Plasminogen Activator Human Recombinant, Sf9

Recombinant human tPA produced in Sf9 insect cells is a single, glycosylated polypeptide chain containing 545 amino acids (24-562 a.a) and having a molecular mass of 61.3 kDa. The molecular size on SDS-PAGE will appear at approximately 50-70 kDa. tPA is fused to a 6 amino acid His-tag at the C-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT79
Source
Sf9, Baculovirus cells.
Appearance
Sterile filtered colorless solution.

TPA (36-310) Human

Tissue Plasminogen Activator (36-310 a.a.) Human Recombinant

Recombinant Human TPA, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain containing 284 amino acids (36-310 a.a.) and having a molecular mass of 32.0 kDa (Molecular size on SDS-PAGE will appear at approximately 28-40 kDa). TPA is expressed with a 6 amino acids His tag at the C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28916
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

tPA Human

Tissue Plasminogen Activator Human Recombinant

This product is a recombinant human tissue plasminogen activator (tPA) produced in CHO cells. It is a single, glycosylated polypeptide chain with a molecular weight of 59,008.71 Daltons, consisting of 527 amino acids. This enzyme catalyzes the conversion of plasminogen to plasmin. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29010
Source
Chinese Hamster Ovary Cells (CHO)
Appearance
Sterile Filtered White lyophilized powder.

TPA (311-562) Human

Tissue Plasminogen Activator (311-562 a.a.) Human Recombinant

This product consists of the recombinant form of human tissue plasminogen activator (tPA), specifically amino acids 311 to 562. It is produced using Sf9 insect cells and undergoes glycosylation, a process crucial for its biological activity. The protein, with a molecular weight of 29.2 kDa, is engineered to carry a 6-amino acid His tag at its C-terminus to facilitate purification. The final product is highly pure, exceeding 95% purity, as confirmed by SDS-PAGE analysis.
Shipped with Ice Packs
Cat. No.
BT28841
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless solution, devoid of any particulate matter.
Definition and Classification

Tissue Plasminogen Activator (TPA), also known as tissue-type plasminogen activator (tPA), is a serine protease enzyme involved in the breakdown of blood clots. It converts plasminogen to plasmin, the major enzyme responsible for clot breakdown. TPA is classified as a thrombolytic agent and is encoded by the PLAT gene in humans .

Biological Properties

Key Biological Properties: TPA is a 527 amino acid protein with a molecular weight of approximately 70 kDa. It contains several domains, including a finger domain, an epidermal growth factor (EGF)-like domain, two kringle domains, and a serine protease domain .

Expression Patterns: TPA is primarily expressed in endothelial cells lining the blood vessels. It is also found in various tissues, including the brain, where it plays a role in neuronal plasticity and response to injury .

Tissue Distribution: TPA is widely distributed in the body, with high expression levels in the endothelium of blood vessels, the brain, and other tissues such as the liver and kidneys .

Biological Functions

Primary Biological Functions: The primary function of TPA is to catalyze the conversion of plasminogen to plasmin, leading to the degradation of fibrin clots. This process is crucial for maintaining vascular patency and preventing thrombosis .

Role in Immune Responses and Pathogen Recognition: TPA has been implicated in various immune responses, including the modulation of inflammation and the activation of immune cells. It also plays a role in pathogen recognition by facilitating the clearance of pathogens through the fibrinolytic system .

Modes of Action

Mechanisms with Other Molecules and Cells: TPA interacts with fibrin-bound plasminogen to convert it into plasmin. This interaction is facilitated by the binding of TPA to fibrin, which enhances its catalytic activity .

Binding Partners and Downstream Signaling Cascades: TPA binds to fibrin and plasminogen, forming a ternary complex that leads to the activation of plasmin. This activation triggers downstream signaling cascades involved in fibrinolysis and tissue remodeling .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: The expression of TPA is regulated at the transcriptional level by various factors, including hypoxia and inflammatory cytokines. Post-translational modifications, such as glycosylation, also play a role in regulating TPA activity and stability .

Transcriptional Regulation and Post-Translational Modifications: TPA gene expression is controlled by promoter elements responsive to hypoxia and other stimuli. Post-translational modifications, such as glycosylation and phosphorylation, influence TPA’s stability, activity, and interaction with other proteins .

Applications

Biomedical Research: TPA is widely used in research to study fibrinolysis, thrombosis, and related processes. It serves as a model enzyme for understanding serine protease function and regulation .

Diagnostic Tools: TPA levels are measured in clinical settings to assess the risk of thrombotic events and to monitor the efficacy of thrombolytic therapy .

Therapeutic Strategies: Recombinant TPA (rtPA) is used clinically to treat acute ischemic stroke, myocardial infarction, and pulmonary embolism. It is administered to dissolve blood clots and restore blood flow to affected tissues .

Role in the Life Cycle

Role Throughout the Life Cycle: TPA plays a critical role in various stages of life, from development to aging. During development, TPA is involved in tissue remodeling and angiogenesis. In adulthood, it maintains vascular health by preventing thrombosis. In aging and disease, TPA levels and activity may be altered, contributing to conditions such as stroke and cardiovascular disease .

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