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Active Transport Collection

"Unlocking the Secrets of Active Transport

Background imageActive Transport Collection: Sodium-potassium ion pump protein F006 / 9656

Sodium-potassium ion pump protein F006 / 9656
Sodium-potassium ion pump protein, molecular model. Sodium-potassium ATPase (adenosine triphosphatase) is an ATP-powered ion pump found in all animal cells

Background imageActive Transport Collection: Sodium-potassium ion pump proteins C015 / 9993

Sodium-potassium ion pump proteins C015 / 9993
Sodium-potassium ion pump proteins, molecular model. Sodium-potassium ATPase (adenosine triphosphatase) is an ATP-powered ion pump found in all animal cells

Background imageActive Transport Collection: Sodium-potassium ion pump proteins C015 / 9997

Sodium-potassium ion pump proteins C015 / 9997
Sodium-potassium ion pump proteins, molecular model. Sodium-potassium ATPase (adenosine triphosphatase) is an ATP-powered ion pump found in all animal cells

Background imageActive Transport Collection: Vitamin B12 transport protein C015 / 5824

Vitamin B12 transport protein C015 / 5824
Vitamin B12 transport protein, molecular model. This transmembrane protein, known as BTUB, is from the Escherichia coli bacterium

Background imageActive Transport Collection: Vitamin B12 transport protein C015 / 5823

Vitamin B12 transport protein C015 / 5823
Vitamin B12 transport protein, molecular model. This transmembrane protein, known as BTUB, is from the Escherichia coli bacterium

Background imageActive Transport Collection: Sodium-potassium ion pump protein C016 / 2393

Sodium-potassium ion pump protein C016 / 2393
Sodium-potassium ion pump protein, molecular model. Sodium-potassium ATPase (adenosine triphosphatase) is an ATP-powered ion pump found in all animal cells

Background imageActive Transport Collection: Sodium-potassium ion pump protein C016 / 2392

Sodium-potassium ion pump protein C016 / 2392
Sodium-potassium ion pump protein, molecular model. Sodium-potassium ATPase (adenosine triphosphatase) is an ATP-powered ion pump found in all animal cells

Background imageActive Transport Collection: Sodium-potassium pump molecule

Sodium-potassium pump molecule. Computer model showing the structure of a molecule of Sodium-Potassium Adenosine Triphosphatase, or the sodium-potassium pump, embedded in a cell membrane

Background imageActive Transport Collection: Nuclear pore complexes, SEM

Nuclear pore complexes, SEM
Nuclear pore complexes. Coloured scanning electron micrograph (SEM) of the surface of a cell nucleus showing the numerous nuclear pore complexes (NPCs, rings) in its envelope


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"Unlocking the Secrets of Active Transport: Sodium-Potassium Ion Pump Proteins and Vitamin B12 Transport Protein" a fascinating process that plays a crucial role in maintaining the delicate balance within our cells. At the heart of this intricate mechanism are sodium-potassium ion pump proteins, such as F006/9656, C015/9993, and C015/9997. These remarkable proteins tirelessly work to regulate the concentration of sodium and potassium ions across cell membranes. The sodium-potassium ion pump proteins act like molecular pumps, expending energy to move three sodium ions out of the cell while simultaneously bringing two potassium ions inside. This constant exchange creates an electrochemical gradient essential for various cellular functions, including nerve impulse transmission and muscle contraction. Another key player is vitamin B12 transport protein (C015/5824). This specialized protein ensures that vitamin B12 molecules are efficiently transported into cells where they participate in vital metabolic processes. Its counterpart, C015/5823, also contributes to this transportation system by facilitating the movement of vitamin B12 across cell membranes. Intriguingly, these sodium-potassium ion pump proteins and vitamin B12 transport proteins belong to a larger family known as sodium-potassium pump molecules (C016/2393 & C016/2392). Together, they form an intricate network responsible for maintaining homeostasis within our bodies. To further unravel the mysteries surrounding active transport mechanisms, scientists have employed advanced imaging techniques like scanning electron microscopy (SEM) to study nuclear pore complexes. These complex structures serve as gateways between the nucleus and cytoplasm allowing selective passage of molecules necessary for cellular function. Understanding active transport at a molecular level opens doors to potential therapeutic interventions targeting diseases caused by malfunctioning or dysregulated transportation systems. The ongoing research on these remarkable proteins continues to shed light on their significance in human health and disease prevention.

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