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Recombinant Human SNX9, N-His

Reference: ARO-P12962
Size

100ug

Brand

Arovia

Product type

Recombinant Proteins

Product nameRecombinant Human SNX9, N-His
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight42.43 kDa
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)
BrandArovia
Host speciesEscherichia coli (E.coli)
Fragment TypePhe250-Met595
Aliases /SynonymsSH3 and PX domain-containing protein 3A, SNX9, SH3PXD3A, Sorting nexin-9, SH3PX1, SH3 and PX domain-containing protein 1, Protein SDP1
ReferenceARO-P12962
NoteFor research use only.

Description of Recombinant Human SNX9, N-His

Introduction

Recombinant Human SNX9 is a protein that plays a critical role in regulating endocytosis, actin cytoskeleton organization, and cell migration. It is a member of the sorting nexin (SNX) family of proteins, which are involved in the sorting and trafficking of proteins within cells. Recombinant Human SNX9 is a valuable tool for studying the function and mechanism of action of this protein in various cellular processes.

Structure of Recombinant Human SNX9

Recombinant Human SNX9 is a 609 amino acid protein with a molecular weight of approximately 69 kDa. It contains several functional domains, including a PX (phox homology) domain, a BAR (Bin/amphiphysin/Rvs) domain, and a SH3 (Src homology 3) domain. The PX domain is responsible for binding to phosphatidylinositol 3-phosphate (PI3P), a lipid found on the surface of cellular membranes. The BAR domain is involved in protein-protein interactions and membrane curvature sensing, while the SH3 domain is responsible for binding to proline-rich motifs on other proteins.

Activity of Recombinant Human SNX9

Recombinant Human SNX9 plays a crucial role in regulating endocytosis, the process by which cells internalize molecules from the external environment. It does so by interacting with other proteins involved in endocytosis, such as dynamin, clathrin, and actin. The PX domain of Recombinant Human SNX9 binds to PI3P on the plasma membrane, leading to the recruitment of other proteins involved in endocytosis. The BAR domain of Recombinant Human SNX9 also plays a role in endocytosis by sensing membrane curvature and promoting the formation of endocytic vesicles. Additionally, Recombinant Human SNX9 is involved in the regulation of actin dynamics, which is essential for cell migration and other cellular processes.

Application of Recombinant Human SNX9

Recombinant Human SNX9 has a wide range of applications in scientific research. One of its primary uses is in studying the role of SNX9 in endocytosis and actin dynamics. By overexpressing or silencing Recombinant Human SNX9 in cells, researchers can investigate its effects on these processes and gain a better understanding of its function. Additionally, Recombinant Human SNX9 can be used to study the interaction between SNX9 and other proteins involved in endocytosis, such as dynamin and clathrin.

Furthermore, Recombinant Human SNX9 has potential therapeutic applications. It has been shown to play a role in cancer cell migration and invasion, making it a potential target for cancer treatment. Additionally, SNX9 has been linked to neurodegenerative diseases, such as Alzheimer’s and Parkinson’s, and studying its function using Recombinant Human SNX9 could provide insights into these conditions.

Conclusion

Recombinant Human SNX9 is a crucial protein involved in regulating endocytosis, actin dynamics, and cell migration. Its structure, activity, and applications make it a valuable tool for studying various cellular processes and potential therapeutic targets. With the use of Recombinant Human SNX9, researchers can continue to unravel the complex mechanisms of this protein and its role in health and disease.

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