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Recombinant Human Cell cycle control protein 50A (TMEM30A), partial

Recombinant Human Cell cycle control protein 50A (TMEM30A), partial

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MSDS	MSDS Datasheet
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Source
Conjugate
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Target Background

Product Details

Abbreviation

TMEM30A

Purity

>85% (SDS-PAGE)

Target Names

TMEM30A

Uniprot NO.

Q9NV96

Alternative Names

TMEM30A; C6orf67; CDC50A; Cell cycle control protein 50A; P4-ATPase flippase complex beta subunit TMEM30A; Transmembrane protein 30A

Species

Homo sapiens (Human)

Source

Yeast

Protein Length

Partial

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage Condition

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. The beta subunit may assist in binding of the phospholipid substrate. Required for the proper folding, assembly and ER to Golgi exit of the ATP8A2:TMEM30A flippase complex. ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth, and, reconstituted to liposomes, predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). The ATP8A1:TMEM30A flippase complex seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane. Required for the formation of the ATP8A2, ATP8B1 and ATP8B2 P-type ATPAse intermediate phosphoenzymes. Involved in uptake of platelet-activating factor (PAF), synthetic drug alkylphospholipid edelfosine, and, probably in association with ATP8B1, of perifosine. Also mediates the export of alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B and ATP11C from the ER to other membrane localizations.

Gene References into Functions

results indicated that the extracellular domain of CDC50A has important roles both in CDC50A's ability to chaperone ATP11C to the plasma membrane and in inducing ATP11C's ATP hydrolysis-coupled flippase activity. PMID:29276178
Data indicate that the lipid flippase (ATP8B1)-transmembrane protein 30A (CDC50A) heterodimer is essential for the apical localization of sodium-dependent bile acid transporter (SLC10A2/ASBT) in Caco-2 cells. PMID:25239307
ATP11C and CDC50A are required for aminophospholipid translocation from the outer to the inner plasma membrane leaflet; that is, they display flippase activity. PMID:24904167
the phospholipid flippase complex of ATP8A1 and CDC50A proteins has a role in cell migration PMID:23269685
Import of choline phospholipids into Saccharomyces cerevisiae DeltaLem3 vector is partially reconstituted by human TMEM30a and by Lem3p-TMEM30a chimeras, showing that the proteins are orthologous. PMID:21289302
CDC50A plays a key role in perifosine uptake in human cells, presumably by forming a functional plasma membrane translocator. PMID:20510206
CDC50A may be the potential beta-subunit or chaperone for ATP8B1 in hepatocytes. PMID:17948906