Recombinant Human Plastin-2 (LCP1) Protein (His-SUMO)

Name: Recombinant Human Plastin-2 (LCP1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-03371P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Plastin-2 (LCP1) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P13796
Target Symbol	LCP1
Synonyms	CP64; L plastin; L-plastin; Larval cuticle protein 1; LC64P; LCP-1; LCP1; LPL; Lplastin; Lymphocyte cytosolic protein 1; Plastin 2; Plastin-2; PLS2; PLSL_HUMAN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	ARGSVSDEEMMELREAFAKVDTDGNGYISFNELNDLFKAACLPLPGYRVREITENLMATGDLDQDGRISFDEFIKIFHGLKSTDVAKTFRKAINKKEGICAIGGTSEQSSVGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTNDLFNAVGDGIVLCKMINLSVPDTIDERTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIELSRNEALIALLREGESLEDLMKLSPEELLLRWANYHLENAGCNKIGNFSTDIKDSKAYYHLLEQVAPKGDEEGVPAVVIDMSGLREKDDIQRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNRYPALHKPENQDIDWGALEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGGNMKKLENCNYAVELGKNQAKFSLVGIGGQDLNEGNRTLTLALIWQLMRRYTLNILEEIGGGQKVNDDIIVNWVNETLREAKKSSSISSFKDPKISTSLPVLDLIDAIQPGSINYDLLKTENLNDDEKLNNAKYAISMARKIGARVYALPEDLVEVNPKMVMTVFACLMGKGMKRV
Expression Range	2-627aa
Protein Length	Full Length of Mature Protein
Mol. Weight	86.2kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 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.

Target Details

Target Function	Actin-binding protein. Plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. Modulates the cell surface expression of IL2RA/CD25 and CD69.
Subcellular Location	Cytoplasm, cytoskeleton. Cell junction. Cell projection. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side.
Database References	HGNC: 6528 OMIM: 153430 KEGG: hsa:3936 STRING: 9606.ENSP00000315757 UniGene: PMID: 28230172 MOLP8/R cells display a very high overexpression of LCP1 gene (l-Plastin) controlled by HIF1&alpha. PMID: 29882856 these findings support a plausible mechanism by which the AP4/L-plastin axis is regulated by the PI3K/AKT pathway in human prostate cancer (PCa)and may represent a novel therapeutic target in PCa treatment. PMID: 28981098 Mutated LCP1 is a driver of chronic lymphocytic leukemia. PMID: 28679620 AngII-dependent phosphorylation of LCP1 in cultured podocytes was mediated by the kinases ERK, p90 ribosomal S6 kinase, PKA, or PKC. LCP1 phosphorylation increased filopodia formation. PMID: 28768720 L-plastin regulates the stability of the immune synapse of naive and effector T-cells. (Review) PMID: 27720134 The findings support a mechanism in which miR-375 suppresses RUNX1 levels, resulting in reduced vimentin and L-plastin expression. Knockdown of RUNX1, L-plastin, and vimentin resulted in significant reductions in cell invasion in vitro, indicating the functional significance of miR-375 regulation of specific proteins involved in head and neck squamous cell carcinoma (HNSCC) invasion. PMID: 28499703 In this study, the authors found that the actin filament bundling abilities of PLS1 and PLS2 were similarly sensitive to Ca(2+) (pCa50 ~6.4), whereas PLS3 was less sensitive (pCa50 ~5.9). PMID: 28694070 elevated L-plastin expression promotes elongation and reduces protrusion density in cells with relatively lower L-plastin than fascin levels. PMID: 26945069 Enhanced nitroxidative stress may results in LPL S-glutathionylation leading to impaired chemotaxis, polarization, and bactericidal activity of human neutrophils. PMID: 25881549 association of SNPs in LCP1 and CTIF with hearing PMID: 26264041 An NKX3.1 binding site polymorphism in the l-plastin promoter leads to differential gene expression in human prostate cancer PMID: 26148677 The proteins (HSP90b, TSM1 and L-plastin) in the current study may hold potential in differentiating between melanoma and benign nevi in diagnostically challenging cases. PMID: 25191796 Data suggest that several single-nucleotide polymorphisms (SNPs) of the plastin genes PLS3 and LCP1 could serve as gender- and/or stage-specific molecular predictors of tumor recurrence in stage II/III colorectal cancer as well as therapeutic targets. PMID: 24170770 L-plastin plays an important role in the clustering of NKG2D into lipid rafts, and it participates in NKG2D-mediated inhibition of NK cell chemotaxis. PMID: 24803550 expression of L-plastin promotes tumor metastasis and, importantly, that this effect depends on an additionally required phosphorylation of L-plastin PMID: 24438191 L-plastin is indispensable for podosome formation and function in macrophages. PMID: 24236012 LCP1 is functionally relevant to CXCL12 induced B-cell migration. PMID: 24009233 High serum LCP1 is associated with kidney cancer. PMID: 23479363 Hepatic LCP1 mRNA was increased (by 300%) in liver biopsy samples from patients with nonalcoholic fatty liver disease compared to controls PMID: 23213074 This study adds L-plastin to a growing list of proteins implicated in T lymphocyte polarity and migration PMID: 22581862 our data introduce costimulation-induced L-plastin phosphorylation as an important event for immune synapse formation and its inhibition by dexamethasone as a novel mode of function of this immunosuppressive glucocorticoid. PMID: 21805466 Results establish a causative role for PKCbetaII and L-plastin in linking GM-CSF-induced eosinophil priming for chemotaxis. PMID: 21525390 Plasmic L-plastin level in patients with colorectal cancer was higher than that in healthy adults, and was associated with tumor size, penetration, and lymphatic metastasis. PMID: 20878578 required for immune synapse formation PMID: 20683899 This study discloses a novel unexpected role of the actin bundling protein L-plastin as a cell protective protein against TNF-cytotoxicity. PMID: 19799649 Data demonstrate for the first time that L-plastin contributes to the fine-tuning of actin turn-over, an activity which is regulated by Ser5 phosphorylation promoting its high affinity binding to the cytoskeleton. PMID: 20169155 Data show that the serine protease plasmin cleaved both propeptides from human vascular endothelial growth factor (VEGF)-D, generating mature forms, and also activated VEGF-C. PMID: 12963694 association of L-plastin overexpression with increased rate of proliferation and invasion, and loss of E-cadherin expression in the SW480 colon cancer cell line indicates that L-plastin plays an important mechanistic role in colorectal cancer metastasis PMID: 16287074 Data suggest that phosphorylated L-plastin might act as an integrator of signals controlling the assembly of the actin cytoskeleton and cell motility in a 3D-space. PMID: 16636079 Data show that an increase in melanoma cell invasiveness requires not only expression but also phosphorylation of L-plastin. PMID: 17290393 Phosphorylation of the actin bundling protein L-plastin represents a mechanism by which costimulation controls the transport of activation receptors to the T cell surface. PMID: 17294403 L-plastin and S100A9 were differentially expressed in nasopharyngeal carcinoma and normal nasopharyngeal epithelial tissue PMID: 19142861

FAQs

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.