Recombinant Human LSP1 Protein (His Tag)

Name: Recombinant Human LSP1 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-3252
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	AAH01785.1
Synonym	pp52, WP34
Background	LSP1 is a lymphocyte-specific intracellular Ca2(+)-binding protein.Leukocyte-specific protein 1 (LSP1) localizes to nascent phagocytic cups during Fcgamma receptor-mediated phagocytosis, where it displays the same spatial and temporal distribution as the actin cytoskeleton. Down-regulation of LSP1 severely reduces the phagocytic activity of macrophages, clearly demonstrating a crucial role for this protein in Fcgamma receptor-mediated phagocytosis.Leukocyte-specific protein 1 (LSP1), expressed in endothelial cells, plays a pivotal role in regulating subsequent recruitment steps following leukocyte adhesion.
Description	A DNA sequence encoding the human LSP1 (AAH01785.1) (Met1-Pro339) was expressed with a His tag at the C-terminus.
Source	HEK293
Predicted N Terminal	Met
AA Sequence	Met1-Pro339
Molecular Weight	The recombinant human LSP1 consists 350 a.a. and predicts a molecular mass of 38.7 kDa.
Purity	>85% as determined by SDS-PAGE.
Endotoxin	< 1.0 EU per μg protein as determined by the LAL method.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile PBS, pH 7.4..
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	May play a role in mediating neutrophil activation and chemotaxis.
Subcellular Location	Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Database References	HGNC: 6707 OMIM: 153432 KEGG: hsa:4046 STRING: 9606.ENSP00000308383 UniGene: Hs.56729
Tissue Specificity	Activated T-lymphocytes.

Gene Functions References

LSP1 rs3817198 T > C polymorphism is associated with increased risk of breast cancer, especially in Caucasian and Asian populations [meta-analysis] PMID: 27590509
These results show that LSP1 is critical regulator of actomyosin contractility in primary macrophages. PMID: 29410425
Underexpression of LSP1 is associated with Breast Cancer Recurrence. PMID: 27165221
LSP1 rs569550 and rs592373 polymorphisms are both risk factors for breast cancer. PMID: 26191300
the importance of LSP1 Copy number variations and LSP1 insufficiency in the pathogenesis of rheumatoid arthritis, is reported. PMID: 26554018
The breast cancer SNP LSP1 rs3817198 was associated with an increased risk of lung cancer (odds ratio: 1.10) This association was strongest for women with adenocarcinoma (P = 1.2x10(-4)). PMID: 24681604
Data indicate that slit2N alters the localization and binding of Robo1 to WASp and LSP1 in HIV-1-gp120-treated immature dendritic cells (iDCs). PMID: 23119100
Single nucleotide polymorphism in LSP1 is associated with breast cancer. PMID: 22454379
The LSP1 rs3817198T>C polymorphism is a low-penetrant risk factor for developing breast cancer but may not be in Africans. PMID: 21127985
Low-risk variants of LSP1 is associated with familial breast cancer. PMID: 19856316
The LSP1 and 2q35 SNPs appear to interact multiplicatively on breast cancer risk for BRCA2 mutation carriers. PMID: 19656774
LSP1 interacts with F-actin and the cytoskeleton through residues downstream of amino acid residue 230. The cytoskeleton binding site of mouse LSP1 maps to the 300-330 interval. PMID: 12972289
Leukocyte-specific protein 1 is a cytoskeletal targeting protein for the ERK/MAP kinase pathway PMID: 15090600
LSP1 protein facilitates virus transport into the proteasome after its interaction with DC-SIGN through its interaction with cytoskeletal proteins. PMID: 17296787
MK2-regulated LSP1 phosphorylation is involved in stabilization of F-actin polarization during neutrophil chemotaxis. PMID: 17481585
DC-SIGN was constitutively associated with a signalosome complex consisting of the scaffold proteins LSP1, KSR1 and CNK and the kinase Raf-1 PMID: 19718030

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.