Recombinant Human Lim And Sh3 Domain Protein 1 (LASP1) Protein (GST)

Name: Recombinant Human Lim And Sh3 Domain Protein 1 (LASP1) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08444P
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 Lim And Sh3 Domain Protein 1 (LASP1) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q14847
Target Symbol	LASP1
Synonyms	LASP 1; LASP-1; LASP1; LASP1_HUMAN; LIM and SH3 domain protein 1; LIM and SH3 protein 1; Metastatic lymph node gene 50 protein; MLN 50; MLN50; OTTHUMP00000164238; OTTHUMP00000164239
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MNPNCARCGKIVYPTEKVNCLDKFWHKACFHCETCKMTLNMKNYKGYEKKPYCNAHYPKQSFTMVADTPENLRLKQQSELQSQVRYKEEFEKNKGKGFSVVADTPELQRIKKTQDQISNIKYHEEFEKSRMGPSGGEGMEPERRDSQDGSSYRRPLEQQQPHHIPTSAPVYQQPQQQPVAQSYGGYKEPAAPVSIQRSAPGGGGKRYRAVYDYSAADEDEVSFQDGDTIVNVQQIDDGWMYGT
Expression Range	1-243aa
Protein Length	Partial
Mol. Weight	54.8kDa
Research Area	Transport
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	Plays an important role in the regulation of dynamic actin-based, cytoskeletal activities. Agonist-dependent changes in LASP1 phosphorylation may also serve to regulate actin-associated ion transport activities, not only in the parietal cell but also in certain other F-actin-rich secretory epithelial cell types.
Subcellular Location	Cytoplasm, cell cortex. Cytoplasm, cytoskeleton.
Database References	HGNC: 6513 OMIM: 602920 KEGG: hsa:3927 STRING: 9606.ENSP00000325240 UniGene: PMID: 29207145 An in vitro study showed that overexpression of miR-133b inhibited the proliferation, migration, and invasion of HepG2 and Hep3B cells. Similarly, knockdown of LASP1 reduced HepG2 and Hep3B cell proliferation, migration, and invasion. PMID: 28117027 Findings indicated that LASP-1, as a downstream target of SOX9, may act as a novel biomarker for lung cancer and plays an important role in cell proliferation, migration, and invasion. PMID: 29138807 miR-203a-3p suppresses tumor growth and metastasis through targeting LASP1 in NPC. PMID: 28982387 LASP1 silencing elicited effects similar to miR-326 overexpression on HCC cells. PMID: 28713953 A combination of low 14-3-3sigma and high LASP1 expression shows a worse trend with overall survival of colorectal cancer patients. PMID: 27156963 Furthermore, we identify flotillin-1 (FLOT1) and histone H1 as downstream factors for cytoplasmic and nuclear pathway of S100A11, which are required for LASP1-S100A11 axis-mediated epithelial-mesenchymal transition and colorectal cancer progression. PMID: 27181092 Overexpression of LASP-1 in thyroid cancer tissues.LASP-1 role in thyroid cancer cell proliferation and invasion.LASP-1 is an oncogene. PMID: 27938497 Study found LASP1 to be downregulated after knockdown of PVT1 and overexpression of LASP1 attenuated the tumor-suppressive roles of PVT1 knockdown in esophageal squamous cell carcinoma. PMID: 28404954 Data indicate that LIM and SH3 protein 1 (LASP1) is a direct target of miR-145. PMID: 27626692 LASP1 enhances the expression and secretion of MMPs, favoring breast cancer cell migration and invasiveness. PMID: 27588391 miR-218 contributes to PE by targeting LASP1 to inhibit trophoblast invasion PMID: 28412444 The correlation between LIM and SH3 domain-containing protein expression levels in cancer and the poor outcome and metastatic behavior of tumors denotes the clinical significance of this protein and hints its potential value as a new cancer prognostic or even diagnostic biomarker PMID: 28621232 LASP-1 contributes to the formation and progression of prostate cancer through a NF-kappaappa B pathway. PMID: 27840958 High expression of miR218 is associated with gastric cancer. PMID: 27696291 LASP-1 may essentially involve in the metastasis and growth of CCA and clinical significance of LASP-1 may reside in function as a biomarker to predict prognosis and as a promising therapeutic strategy for CCA patients by the inhibition of LASP-1 expression PMID: 26729195 It is a target gene of miR-1. PMID: 26414725 LASP-1 associated with UHRF1, G9a, Snail1 and di- and tri-methylated histoneH3 in a CXCL12-dependent manner based on immunoprecipitation and proximity ligation assays PMID: 25982273 LASP-1 induces proliferation, metastasis and cell cycle arrest at the G2/M phase in gallbladder cancer by down-regulating S100P via the PI3K/AKT pathway. PMID: 26797416 LASP-1, mediated by miR-203, has crucial functions in the proliferation, migration and invasion of human non-small cell lung cancer PMID: 26683818 Detecting an affection of migratory processes after LASP-1 silencing, we propose that LASP-1 could impact on metastasis of CC [choriocarcinoma]cells. PMID: 26232936 Results identified LASP1 as a hitherto unknown protein in melanocytes and as novel partner of dynamin in the physiological process of membrane constriction and melanosome vesicle release. PMID: 26061439 Our results suggest that LASP-1 mRNA overexpression may be mainly implicated in female hepatocellular carcinoma (HCC) and cirrhotic HCCs; and that LASP1 may play its role with vimentin in HCC cells. PMID: 25760690 LASP-1 overexpression was associated with aggressive phenotype in clear cell renal cell cancer. PMID: 24955835 LASP1 plays key roles in cell structure, physiological processes, and cell signaling; overexpression contributes to cancer aggressiveness [review] PMID: 25622104 LIM and SH3 protein 1 induces TGFbeta-mediated epithelial-mesenchymal transition in human colorectal cancer by regulating S100A4 expression. PMID: 25252758 Study revealed that LASP1 phosphorylation results in an association with CRKL - another specific BCR-ABL substrate and bona fide biomarker for BCR-ABL activity. PMID: 24913448 Results defined LASP1 as a direct target gene for HIF1alpha upregulation that is critical for metastatic progression of PDAC. PMID: 25385028 LASP-1, overexpressed in gastric cancer and associated with poor prognosis, plays an important role in the growth and metastasis of gastric cancer. PMID: 24990592 Results show significant upregulation of LASP1 and SCAD protein levels in acute psychotic bipolar disorder samples. PMID: 24554194 LASP1 was a direct target of miR-218 in prostate cells. PMID: 24815849 LASP-1 is linked closely to tumourigenicity in oral cancer. PMID: 24386158 Data indicate decreased cell migratory potential accompanied by enhanced cell adhesion, but no significant inhibition of cell proliferation as measured by in T24 cells upon LIM and SH3 (LASP)-1 protein (LASP-1) knockdown. PMID: 22481019 LASP1 may play an important role in the pathogenesis of esophageal squamous cell carcinoma. PMID: 23254782 Data show that miR-133a can target the 3' untranslated region (3'UTR) of LIM and SH3 protein 1 (LASP1) mRNA and suppress the expression of LASP1. PMID: 23968734 Phosphorylation of LASP-1 by PKA at serine 146 induces translocation of the LASP-1/ZO-2 complex from the cytoplasm to the nucleus. PMID: 22665060 A single-nucleotide polymorphism in the LASP1 gene promoter region is associated with schizophrenia susceptibility. PMID: 23040864 High cytosolic LASP-1 expression is associated with hepatocellular carcinoma. PMID: 23084841 miR-203 inhibits the migration and invasion of esophageal squamous cell carcinoma by regulating LASP1. PMID: 22940702 Up-regulated of BIRC5 and LASP1 was able to abrogate the effects induced by transfection with the miR-203 precursor in triple negative breast cancer. PMID: 22713668 These results demonstrated that hepatitis B virus X protein could upregulate LASP-1 through PI3-K pathway to promote the proliferation and migration of hepatoma cells. PMID: 22897902 Data indicate that LASP1 may have an oncogenic function and that it might be regulated by miR-1, miR-133a, and miR-218, which may function as tumor suppressive miRNAs in bladder cancer (BC). PMID: 20843712 Data indicate that Lasp-1 is a novel component of podosomes and is involved in the regulation of podosomal function. PMID: 22514729 LASP-1 has an essential role in growth and migration of ovarian carcinoma cells, possibly by influencing the localization of zyxin. PMID: 17211471 LASP-1 gene expression enhances proliferation of colorectal cancer cells and may serve as a useful marker for colorectal cancer progression. PMID: 21215099 LASP-1 interaction with CXCR2 is critical for CXCR2-mediated chemotaxis PMID: 20419088 LASP1 knockdown by small interfering RNA-mediated silencing indicates its funcion role in progression and metastasis of medulloblastoma. PMID: 20924110 LASP-1, S100A9 and RhoGDI were detected by proteomic analysis to be differentially expressed between normal mucosa, non-metastatic colorectal carcinoma and metastatic CRC tissue PMID: 20812987 Overexpression of LASP-1 was found in metastatic colorectal cancer (CRC) tissues (p=0.002), and its expression level was closely correlated with overall survival of patients with CRC (p=0.002). PMID: 20660701 Nuclear LASP-1-positivity may serve as a negative prognostic indicator for long-term survival of breast cancer patients. PMID: 20461080

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.