Recombinant Human Plastin L Protein (Tagged)

Name: Recombinant Human Plastin L Protein (Tagged)
Brand: Beta LifeScience
SKU: BLA-7101P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Host Species	Human
Accession	P13796
Synonym	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
Description	Recombinant Human Plastin L Protein (Tagged) was expressed in E.coli. It is a Full length protein
Source	E.coli
AA Sequence	ARGSVSDEEMMELREAFAKVDTDGNGYISFNELNDLFKAACLPLPGYRVR EITENLMATGDLDQDGRISFDEFIKIFHGLKSTDVAKTFRKAINKKEGIC AIGGTSEQSSVGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTN DLFNAVGDGIVLCKMINLSVPDTIDERTINKKKLTPFTIQENLNLALNSA SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIELSRNEALIAL LREGESLEDLMKLSPEELLLRWANYHLENAGCNKIGNFSTDIKDSKAYYH LLEQVAPKGDEEGVPAVVIDMSGLREKDDIQRAECMLQQAERLGCRQFVT ATDVVRGNPKLNLAFIANLFNRYPALHKPENQDIDWGALEGETREERTFR NWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLG GNMKKLENCNYAVELGKNQAKFSLVGIGGQDLNEGNRTLTLALIWQLMRR YTLNILEEIGGGQKVNDDIIVNWVNETLREAKKSSSISSFKDPKISTSLP VLDLIDAIQPGSINYDLLKTENLNDDEKLNNAKYAISMARKIGARVYALP EDLVEVNPKMVMTVFACLMGKGMKRV
Molecular Weight	86 kDa including tags
Purity	>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 -20°C or -80°C. Avoid freeze / thaw cycle.

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: Hs.381099
Associated Diseases	Chromosomal aberrations involving LCP1 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;13)(q27;q14), with BCL6.
Tissue Specificity	Detected in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia, in spleen and other lymph node-containing organs. Expressed in peripheral blood T-lymphocytes, neutrophils, monocytes, B-lymphocytes, and myeloid cells.

Gene Functions References

LCP1-positive oral squamous cell carcnome samples were correlated closely with the primary tumor size and regional lymph node metastasis. 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

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.