Recombinant Human Scramblase 1 Protein

Name: Recombinant Human Scramblase 1 Protein
Brand: Beta LifeScience
SKU: BLA-8040P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Human
Accession	O15162
Synonym	Ca(2+) dependent phospholipid scramblase 1 Ca(2+)-dependent phospholipid scramblase 1 Erythrocyte phospholipid scramblase MM1 cell-derived transplantability-associated gene 1b, mouse, homolog of MmTRA1a MmTRA1b Nor1 Phospholipid scramblase 1 PL scramblase 1 PLS1_HUMAN PLSCR 1 Plscr1 Scramblase1 Tra1 Tra1a Tra1b Transplantability-associated protein 1 Tras1 Tras2
Description	Recombinant Human Scramblase 1 Protein was expressed in E.coli. It is a Protein fragment
Source	E.coli
AA Sequence	MGSSHHHHHH SSGLVPRGSH MDKQNSQMNA SHPETNLPVG YPPQYPPTAF QGPPGYSGYP GPQVSYPPPP AGHSGPGPAG FPVPNQPVYN QPVYNQPVGA AGVPWMPAPQ PPLNCPPGLE YLSQIDQILI HQQIELLEVL TGFETNNKYE IKNSFGQRVY FAAEDTDCCT RNCCGPSRPF TLRIIDNMGQ EVITLERPLR CSSCCCPCCL QEIEIQAPPG VPIGYVIQTW HPCLPKFTIQ NEKREDVLKI SGPCVVCSCC GDVDFEIKSL DEQCVVGKIS KHWTGILREA FTDADNFGIQ FPLDLDVK
Molecular Weight	34 kDa including tags
Purity	Greater than 90% SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Liquid Solution
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target 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. Mediates calcium-dependent phosphatidylserine externalization and apoptosis in neurons via its association with TRPC5. 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. Negatively regulates FcR-mediated phagocytosis in differentiated macrophages. May contribute to cytokine-regulated cell proliferation and differentiation. 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. Acts as an attachment receptor for HCV.
Subcellular Location	Cell membrane; Single-pass type II membrane protein. Cell membrane; Lipid-anchor; Cytoplasmic side. Nucleus. Cytoplasm. Cytoplasm, perinuclear region.
Protein Families	Phospholipid scramblase family
Database References	HGNC: 9092 OMIM: 604170 KEGG: hsa:5359 STRING: 9606.ENSP00000345494 UniGene: Hs.130759
Tissue Specificity	Expressed in platelets, erythrocyte membranes, lymphocytes, spleen, thymus, prostate, testis, uterus, intestine, colon, heart, placenta, lung, liver, kidney and pancreas. Not detected in brain and skeletal muscle.

Gene Functions References

Inhibition of PLSCR1 decreased the antiviral activity of IFN against HBV. PMID: 30004207
Data suggest that PLSCR1 is involved in viral entry; here, herpes simplex viruses activate PLSCR1 and up-regulate flipping of phosphatidylserines and AKT to outside of plasma membrane shortly following HSV-1 or HSV-2 exposure. (PLSCR1 = phospholipid scramblase 1; AKT = proto-oncogene c-Akt) PMID: 29293671
wogonoside promotes the expression of PLSCR1 and enhances its nuclear translocation and binding to the 1, 4, 5-trisphosphate receptor 1 (IP3R1) promoter in AML patient-derived primary cells. Wogonoside activates IP3R1, in turn, promotes release of Ca(2+) from endoplasmic reticulum, and eventually leads to cell differentiation. PMID: 28492556
Data indicate heterogeneous expression of phospholipid scramblase 1 (PLSCR1) and suggest its possible implication in the response to anticancer therapies, especially to drugs promoting protective autophagy. PMID: 27248824
investigate how the polar aspartate residue is accommodated in lipid bilayers containing POPC with and without cholesterol, using all-atom molecular dynamics simulations PMID: 28372945
Human phospholipid scramblase 1 has five histidine residues and point mutations of histidine residues to alanine in hPLSCR1 resulted in 60 % loss in nuclease activity. PMID: 27206388
The mechanisms of pH-induced functional activation of hPLSCR1 are described. PMID: 26204401
PLSCR1 positively regulates hepatic carcinoma cell proliferation and migration through interacting with midkine PMID: 26642712
Suggest role for PLSCR1 in negatively regulating trophoblast fusion rather than directly promoting fusion. PMID: 25362260
PLSCR1 mediates the antiviral activity and anticarcinogenesis against hepatitis B virus by regulating HBx stability. PMID: 25365352
affinity of SCR for cholesterol-rich domains in membranes PMID: 25229146
This is the first biochemical evidence to prove the above hypothesis that hPLSCR1 is activated in heavy metal poisoning, which leads to bidirectional transbilayer movement of phospholipids. PMID: 23659204
The C-terminal transmembrane domain of human phospholipid scramblase 1 is essential for the protein flip-flop activity and Ca(2)-binding. PMID: 24343571
This is the first report showing the transcriptional regulation of hPLSCR1 expression by Snail TF and its possible implications in cancer progression. PMID: 24878522
PLSCR1 interacted with ANG in the cell nucleus and regulated rRNA transcription. PMID: 24356419
hPLSCR1 and PRD-hPLSCR2 showed Ca(2+)-dependent aggregation and scrambling activity PMID: 24648509
The data are in agreement with the possibility that PLSCR1 is an integral membrane protein. PMID: 24099740
Phospholipid Scramblase 1, an interferon-regulated gene located at 3q23, is regulated by SnoN/SkiL in ovarian cancer cells. PMID: 23621864
The C-terminal helix of human PLSCR1 is required for membrane insertion and calcium binding. PMID: 23590222
Phospholipid scramblase 1 expression is enhanced in patients with antiphospholipid syndrome. PMID: 22526829
Overexpression of PLSCR1 efficiently represses the Tat-dependent transactivation of the HIV-1 long terminal repeat (LTR) and reduces the nuclear translocation of Tat. PMID: 23501106
Calcium-dependent PLSCR-1 activity is required for compensatory endocytosis (but not for exocytosis) in neuroendocrine cells. PMID: 23426682
PLSCR1 is overexpressed in colorectal cancer and metastatic liver cancer. Silencing of PLSCR1 by siRNA inhibits the proliferation, adhesion, migration and invasion of tumor cells. PMID: 22893466
PLSCR1 may play an important role in the IFN-mediated repression of Tax-dependent transactivation during HTLV-1 infection. PMID: 22789739
this report identifies PLSCR1 as a protein that physically interacts with Receptor expressed in lymphoid tissues family members and is a potential substrate for phosphorylation by the OSR1 kinase in a RELT-dependent fashion. PMID: 22052202
PLSCR1 inhibited HBV replication through a reduction in the synthesis of viral proteins and DNA replication. PMID: 22342889
IFNalpha-induced PLSCR1 associates with the cytoskeleton after exposure to alpha-toxin, and cellular depletion of PLSCR1 negates IFN-induced protection from alpha-toxin. PMID: 22264514
summarizes the mechanisms and roles of PS exposure following platelet activation and discusses the recent identification of TMEM16F and its significance in the scrambling process PMID: 21958383
PLSCR1 might be used as a noninvasive serological diagnostic and prognostic biomarker for CRC. PMID: 20927484
PLSCR1 was required for the initial attachment of HCV onto hepatoma cells, where it specifically interacted with entry factor OCLN. We show that PLSCR1 is a novel attachment factor for HCV entry. PMID: 21806988
Interferon tau induces expression of DDX58 and PLSCR1 via the classical STAT1-mediated cell signaling pathway. PMID: 20926691
PLSCR1 interacts with the tandem repeat region of ECM1a in the dermal epidermal junction zone of human skin. PMID: 20870722
Monocytes in systemic lupus erythematosus patients had enhanced PLSCR1 mRNA expression, as well as increased fibrin turnover and cell-surface PS exposure. PMID: 20516018
Suppression of ovarian carcinoma cell growth in vivo by the interferon-inducible plasma membrane protein, phospholipid scramblase 1. PMID: 11809687
PLSCR1 co-localizes with the epidermal growth factor (EGF) receptor in lipid rafts and plays a role in the EGF-induced metabolic or mitogenic response. PMID: 12009895
expression has a role in the induction of differentiation of human myeloid leukemia cells into granulocytes. PMID: 12031648
Trafficking of PLSCR1 to the plasma membrane is dependent upon palmitoylation of the polypeptide; in the absence of palmitoylation, PLSCR1 traffics into the nucleus. PMID: 12564925
Identification of domains for PLSCR1 and BACE binding and their colocalization in the Golgi area and endosomal compartments suggest involvement of PLSCR1 in the intracellular distribution and/or recruitment of BACE into the lipid raft. PMID: 12586838
phospholipid scramblase 1 plays a role in ischemic injury in the human hippocampus PMID: 12605885
PLSCR1, through its interaction with Shc, promotes Src kinase activation through the EGF receptor. PMID: 12871937
Higher MmTRA1b mRNA levels were associated with significantly longer overall survival in AML, especially in AML-M4 patients, independent of chromosomal aberrations PMID: 14654079
both PLSCR1 and phospholipid flip-flop characterize uropod raft domains of polarized neutrophils PMID: 14766753
Data support a mechanism of receptor-mediated nuclear import of PLSCR1 and suggest a potential nuclear function for this plasma membrane protein, mediated through potential interaction with genomic DNA. PMID: 15035622
as a protein induced upon PKCdelta activation, PLSCR1 is required for ATRA- and PMA-triggered leukemic cell differentiation PMID: 15308560
PLSCR1, which is itself an IFN-stimulated gene-encoded protein, provides a mechanism for amplifying and enhancing the IFN response through increased expression of a select subset of potent antiviral genes PMID: 15308695
x-ray crystallography shows that there is a nonclassical nuclear localization signal in PLSCR1 with a unique binding site in importin alpha PMID: 15611084
PLSCR1 binds to the promoter region of the IP3R1 gene to enhance its expression PMID: 16091359
protein kinase Cdelta and JNK have roles in Ifn-alpha induced expression of phospholipid scramblase 1 through STAT1 PMID: 16260419
PR3 externalization depended on PLSCR1 PMID: 17712045
the same region of the cytoplasmic domain of PLSCR1 is involved in the binding to CD4 and SLPI PMID: 19333378

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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