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AB136366

Recombinant Human Scramblase 1 protein (His tag N-Terminus)

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Recombinant Human Scramblase 1 protein (His tag N-Terminus) is a Human Fragment protein, in the 1 to 288 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

Phospholipid scramblase 1, PL scramblase 1, Ca(2+)-dependent phospholipid scramblase 1, Erythrocyte phospholipid scramblase, Mg(2+)-dependent nuclease, MmTRA1b, PLSCR1

2 Images
SDS-PAGE - Recombinant Human Scramblase 1 protein (His tag N-Terminus) (AB136366)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human Scramblase 1 protein (His tag N-Terminus) (AB136366)

3ug by SDS-PAGE under reducing condition and visualized by coomassie blue stain.

SDS-PAGE - Recombinant Human Scramblase 1 protein (His tag N-Terminus) (AB136366)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human Scramblase 1 protein (His tag N-Terminus) (AB136366)

15% SDS-PAGE analysis of ab136366 (3 μg)

Key facts

Purity

>85% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

Mass Spec, SDS-PAGE

applications

Biologically active

No

Accession

O15162

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 30% Glycerol (glycerin, glycerine), 1.17% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMDKQNSQMNASHPETNLPVGYPPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAGFPVPNQPVYNQPVYNQPVGAAGVPWMPAPQPPLNCPPGLEYLSQIDQILIHQQIELLEVLTGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRIIDNMGQEVITLERPLRCSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCCGDVDFEIKSLDEQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVK","proteinLength":"Fragment","predictedMolecularWeight":"33.8 kDa","actualMolecularWeight":null,"aminoAcidEnd":288,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"O15162","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Scramblase 1 also known as PLSCR1 is a protein involved in the translocation of phospholipids between the inner and outer leaflets of the lipid bilayer. This protein has a molecular mass of approximately 37 kDa. PLSCR1 is found in various tissues and cells with notable expression in the hematopoietic system. As a type II membrane protein Scramblase 1 plays a role in maintaining lipid asymmetry especially during cellular activation or apoptosis.
Biological function summary

Scramblase 1 mediates phospholipid scrambling in response to increased intracellular calcium levels facilitating changes in cell membrane morphology. It performs this function independently and as part of specific protein complexes that regulate membrane curvature and vesicle fusion. The role of PLSCR1 extends beyond membrane activities; it has been linked to signal transduction and the immune response suggesting a broader impact on cellular dynamics.

Pathways

Scramblase 1 influences critical biological processes like blood coagulation and apoptosis. It interacts with proteins such as annexin V which stabilizes membrane phospholipids and regulates cell death pathways. In the coagulation cascade PLSCR1 has been shown to interact with factors involved in platelet activation demonstrating its regulatory role in maintaining hemostasis and tissue homeostasis.

Scramblase 1 has notable implications in cancer and autoimmune diseases. Altered expression or mutation of PLSCR1 links directly to the progression of certain cancers often associating with proteins like p53 which plays an important role in cell cycle regulation and tumor suppression. In autoimmune disorders Scramblase 1’s activity affects the balance of immune cell signaling potentially linking it with proteins involved in inflammatory responses such as cytokines. Understanding these connections provides insights into potential therapeutic targets and diagnostic markers for these diseases.

Specifications

Form

Liquid

Additional notes

ab136366 was purified using conventional chromatography techniques.

General info

Function

Catalyzes calcium-induced ATP-independent rapid bidirectional and non-specific movement of phospholipids (lipid scrambling or lipid flip-flop) between the inner and outer leaflet of the plasma membrane resulting in collapse of the phospholipid asymmetry which leads to phosphatidylserine externalization on the cell surface (PubMed : 10770950, PubMed : 18629440, PubMed : 23590222, PubMed : 23659204, PubMed : 24343571, PubMed : 24648509, PubMed : 29748552, PubMed : 32110987, PubMed : 8663431, PubMed : 9218461, PubMed : 9485382, PubMed : 9572851). Mediates calcium-dependent phosphatidylserine externalization and apoptosis in neurons via its association with TRPC5 (By similarity). Also exhibits magnesium-dependent nuclease activity against double-stranded DNA and RNA but not single-stranded DNA and can enhance DNA decatenation mediated by TOP2A (PubMed : 17567603, PubMed : 27206388). Negatively regulates FcR-mediated phagocytosis in differentiated macrophages (PubMed : 26745724). May contribute to cytokine-regulated cell proliferation and differentiation (By similarity). May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes (PubMed : 15308695). Inhibits the functions of viral transactivators, including human T-cell leukemia virus (HTLV)-1 protein Tax, human immunodeficiency virus (HIV)-1 Tat, human hepatitis B virus (HBV) HBx, Epstein-Barr virus (EBV) BZLF1 and human cytomegalovirus IE1 and IE2 proteins through direct interactions (PubMed : 22789739, PubMed : 23501106, PubMed : 25365352, PubMed : 31434743, PubMed : 35138119). Mediates also the inhibition of influenza virus infection by preventing nuclear import of the viral nucleoprotein/NP (PubMed : 29352288, PubMed : 35595813). Plays a crucial role as a defense factor against SARS-CoV-2 independently of its scramblase activity by directly targeting nascent viral vesicles to prevent virus-membrane fusion and the release of viral RNA into the host-cell cytosol (PubMed : 37438530).. (Microbial infection) Acts as an attachment receptor for HCV.

Sequence similarities

Belongs to the phospholipid scramblase family.

Post-translational modifications

Phosphorylation at Thr-161 by PKC/PKCD increases its phospholipid scramblase activity during both cell stimulation and apoptosis (PubMed:10770950). Phosphorylated by OXSR1 in the presence of RELT.. Palmitoylation is required for its phospholipid scramblase activity (PubMed:9572851). Palmitoylation regulates its localization to the cell membrane or the nucleus; trafficking to the cell membrane is dependent upon palmitoylation whereas in the absence of palmitoylation, localizes to the nucleus (PubMed:12564925).

Subcellular localisation

Nucleus

Product protocols

Target data

Catalyzes calcium-induced ATP-independent rapid bidirectional and non-specific movement of phospholipids (lipid scrambling or lipid flip-flop) between the inner and outer leaflet of the plasma membrane resulting in collapse of the phospholipid asymmetry which leads to phosphatidylserine externalization on the cell surface (PubMed : 10770950, PubMed : 18629440, PubMed : 23590222, PubMed : 23659204, PubMed : 24343571, PubMed : 24648509, PubMed : 29748552, PubMed : 32110987, PubMed : 8663431, PubMed : 9218461, PubMed : 9485382, PubMed : 9572851). Mediates calcium-dependent phosphatidylserine externalization and apoptosis in neurons via its association with TRPC5 (By similarity). Also exhibits magnesium-dependent nuclease activity against double-stranded DNA and RNA but not single-stranded DNA and can enhance DNA decatenation mediated by TOP2A (PubMed : 17567603, PubMed : 27206388). Negatively regulates FcR-mediated phagocytosis in differentiated macrophages (PubMed : 26745724). May contribute to cytokine-regulated cell proliferation and differentiation (By similarity). May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes (PubMed : 15308695). Inhibits the functions of viral transactivators, including human T-cell leukemia virus (HTLV)-1 protein Tax, human immunodeficiency virus (HIV)-1 Tat, human hepatitis B virus (HBV) HBx, Epstein-Barr virus (EBV) BZLF1 and human cytomegalovirus IE1 and IE2 proteins through direct interactions (PubMed : 22789739, PubMed : 23501106, PubMed : 25365352, PubMed : 31434743, PubMed : 35138119). Mediates also the inhibition of influenza virus infection by preventing nuclear import of the viral nucleoprotein/NP (PubMed : 29352288, PubMed : 35595813). Plays a crucial role as a defense factor against SARS-CoV-2 independently of its scramblase activity by directly targeting nascent viral vesicles to prevent virus-membrane fusion and the release of viral RNA into the host-cell cytosol (PubMed : 37438530).. (Microbial infection) Acts as an attachment receptor for HCV.
See full target information PLSCR1

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