Recombinant Human CD233/SLC4A1, N-His

Reference: YHB99801
Product nameRecombinant Human CD233/SLC4A1, N-His
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight30.72 kDa
Protein delivered with Tag?N-Terminal His Tag
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeAla35-Ser290
Aliases /SynonymsAnion exchange protein 1, Anion exchanger 1, EPB3, CD233, Band 3 anion transport protein, AE 1, DI, AE1, SLC4A1, Solute carrier family 4 member 1
ReferenceYHB99801
NoteFor research use only.

Description of Recombinant Human CD233/SLC4A1, N-His

Introduction

Recombinant proteins play a crucial role in various fields of biotechnology and medicine. One such protein is Recombinant Human CD233/SLC4A1, which has gained significant attention due to its diverse functions and potential applications. In this article, we will explore the structure, activity, and application of this protein in detail.

Structure of Recombinant Human CD233/SLC4A1

Recombinant Human CD233/SLC4A1, also known as Band 3 protein, is a transmembrane glycoprotein that belongs to the anion exchanger (AE) family. It is encoded by the SLC4A1 gene and is primarily expressed in red blood cells (RBCs) and kidney cells. The protein consists of 911 amino acids and has a molecular weight of approximately 100 kDa.

The structure of Recombinant Human CD233/SLC4A1 is composed of two major domains: the cytoplasmic domain and the transmembrane domain. The cytoplasmic domain contains binding sites for various cytoskeletal proteins, while the transmembrane domain is responsible for the transport of anions such as chloride, bicarbonate, and sulfate across the cell membrane.

Activity of Recombinant Human CD233/SLC4A1

The primary function of Recombinant Human CD233/SLC4A1 is to maintain the acid-base balance in the body by regulating the transport of anions across the cell membrane. It acts as an anion exchanger, exchanging bicarbonate ions for chloride ions in RBCs, thereby maintaining the pH of the blood. This process is essential for the proper functioning of various organs, including the kidneys, lungs, and brain.

In addition to its role in acid-base balance, Recombinant Human CD233/SLC4A1 also plays a crucial role in cell adhesion, cell signaling, and cell volume regulation. It interacts with various proteins and molecules, such as hemoglobin, carbonic anhydrase, and glycolytic enzymes, to carry out these functions.

Application of Recombinant Human CD233/SLC4A1

The unique structure and activity of Recombinant Human CD233/SLC4A1 make it a potential candidate for various applications in biotechnology and medicine.

Diagnostic Tool

Abnormalities in the SLC4A1 gene have been linked to various diseases, including hereditary spherocytosis, distal renal tubular acidosis, and hereditary elliptocytosis. Therefore, Recombinant Human CD233/SLC4A1 can be used as a diagnostic tool to detect these genetic disorders.

Therapeutic Agent

Recombinant Human CD233/SLC4A1 has also shown potential as a therapeutic agent for the treatment of diseases such as cystic fibrosis, sickle cell anemia, and hypertension. It can be used to correct the abnormal ion transport in these conditions, thereby improving the overall health of the patient.

Vaccine Development

Recombinant Human CD233/SLC4A1 has been identified as a potential antigen for vaccine development against malaria. Studies have shown that antibodies against this protein can inhibit the invasion of malaria parasites into RBCs, making it a promising target for vaccine development.

Conclusion

In conclusion, Recombinant Human CD233/SLC4A1 is a crucial protein with diverse functions and potential applications. Its unique structure and activity make it a valuable tool for diagnostic, therapeutic, and vaccine development purposes. Further research and studies on this protein

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