Human SR-BI Recombinant Protein

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Product nameHuman SR-BI Recombinant Protein
Uniprot IDQ8WTV0
Uniprot linkhttp://www.uniprot.org/uniprot/Q8WTV0
Origin speciesHomo sapiens (Human)
Expression systemProkaryotic expression
SequenceMAHNHRHKHKLTFNNNDTVSFLEYRTFQFQPSKSHGSESDYIVMPNILVLGAAVMMENKPMTLKLIMTLAFTTLGERAFM NRTVGEIMWGYKDPLVNLINKYFPGMFPFKDKFGLFAELNNSDSGLFTVFTGVQNISRIHLVDKWNGLSKVDFWHSDQCN MINGTSGQMWPPFMTPESSLEFYSPEACRSMKLMYKESGVFE
Molecular weight23,24 kDa
Protein delivered with Tag?Yes
Purity estimated80%
BufferPBS, Urea 8M, imidazole 400mM
Formliquid
Delivery conditionDry Ice
Delivery lead time in business days10-25
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)
BrandProteoGenix
Host speciesEscherichia coli (E.coli)
Fragment TypePartial
Protein AccessionNP_005496.4
Spec:Entrez GeneID949
Spec:NCBI Gene AliasesCD36L1, HDLQTL6, CLA-1, SRB1, SR-BI, CLA1
Spec:SwissProtIDQ8WTV0
NCBI ReferenceNP_005496.4
Aliases /SynonymsSR-BI [310-882], scavenger receptor class B, member 1
ReferencePX-P1156
NoteFor research use only

Description of Human SR-BI Recombinant Protein

Introduction

Human SR-BI (scavenger receptor class B type I) is a membrane-bound protein that plays a crucial role in cholesterol metabolism and transport. It is encoded by the SCARB1 gene and is expressed in various tissues including the liver, adrenal glands, and macrophages. SR-BI is a drug target for the treatment of dyslipidemia and atherosclerosis, making it an important protein in the field of cardiovascular research.

Structure of Human SR-BI

Human SR-BI is a 509 amino acid protein with a molecular weight of approximately 82 kDa. It is composed of two transmembrane domains, an extracellular N-terminal domain, and a cytoplasmic C-terminal domain. The N-terminal domain contains a cysteine-rich region and a highly conserved sequence known as the CLA-1 motif, which is responsible for binding to high-density lipoproteins (HDL) and other ligands.

The cytoplasmic C-terminal domain of SR-BI contains a conserved sequence known as the PDZ-binding motif, which is responsible for protein-protein interactions. This domain also contains a phosphorylation site that regulates the activity of SR-BI.

The structure of SR-BI allows it to function as a receptor for various lipoproteins, including HDL, low-density lipoprotein (LDL), and very low-density lipoprotein (VLDL).

Activity of Human SR-BI

Human SR-BI is primarily involved in the selective uptake of cholesterol from HDL particles. This process, known as reverse cholesterol transport, is essential for maintaining cholesterol homeostasis in the body. SR-BI binds to HDL particles through its N-terminal domain and facilitates the transfer of cholesterol from HDL to cells, primarily in the liver and steroidogenic tissues.

In addition to cholesterol transport, SR-BI also plays a role in the regulation of lipoprotein metabolism. It is involved in the clearance of LDL and VLDL particles from the bloodstream, preventing the accumulation of these harmful lipoproteins in the arteries. SR-BI also regulates the uptake of free fatty acids and fat-soluble vitamins, further contributing to lipid metabolism.

Application of Human SR-BI Recombinant Protein

Due to its crucial role in cholesterol metabolism and transport, Human SR-BI has been identified as a potential drug target for the treatment of dyslipidemia and atherosclerosis. Recombinant SR-BI protein can be used for various applications in the field of drug discovery and development.

One potential application of recombinant SR-BI protein is in the screening of potential drugs that target SR-BI. By using recombinant SR-BI in high-throughput assays, researchers can identify compounds that modulate the activity of SR-BI and potentially develop new therapies for dyslipidemia and atherosclerosis.

Recombinant SR-BI protein can also be used to study the structure and function of SR-BI in more detail. By producing mutated versions of SR-BI and studying their effects on cholesterol transport and metabolism, researchers can gain a better understanding of the role of SR-BI in these processes.

Furthermore, recombinant SR-BI protein can be used to generate antibodies for the detection and quantification of SR-BI in various tissues and biological samples. This can aid in the diagnosis and monitoring of cardiovascular diseases and other conditions related to cholesterol metabolism.

Conclusion

In summary, Human SR-BI is a critical protein involved in cholesterol metabolism and transport. Its structure and activity make it an attractive drug target for the treatment of dyslipidemia and atherosclerosis. Recombinant SR-BI protein has various applications in drug discovery, research, and diagnostics, making it a valuable tool in the study of cardiovascular diseases and lipid metabolism.

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