Recombinant Human Leukosialin (SPN) Protein (His)

Name: Recombinant Human Leukosialin (SPN) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00348P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Cluster of differentiation (cd) proteins, Featured cd protein molecules, Recombinant proteins

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Product Overview

Description	Recombinant Human Leukosialin (SPN) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P16150
Target Symbol	SPN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	C-6His
Target Protein Sequence	STTAVQTPTSGEPLVSTSEPLSSKMYTTSITSDPKADSTGDQTSALPPSTSINEGSPLWTSIGASTGSPLPEPTTYQEVSIKMSSVPQETPHATSHPAVPITANSLGSHTVTGGTITTNSPETSSRTSGAPVTTAASSLETSRGTSGPPLTMATVSLETSKGTSGPPVTMATDSLETSTGTTGPPVTMTTGSLEPSSGASGPQVSSVKLSTMMSPTTSTNASTVPFRNPDENSR
Expression Range	20-253aa
Protein Length	Partial
Mol. Weight	30.4 kDa
Research Area	Immunology
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	Predominant cell surface sialoprotein of leukocytes which regulates multiple T-cell functions, including T-cell activation, proliferation, differentiation, trafficking and migration. Positively regulates T-cell trafficking to lymph-nodes via its association with ERM proteins (EZR, RDX and MSN). Negatively regulates Th2 cell differentiation and predisposes the differentiation of T-cells towards a Th1 lineage commitment. Promotes the expression of IFN-gamma by T-cells during T-cell receptor (TCR) activation of naive cells and induces the expression of IFN-gamma by CD4(+) T-cells and to a lesser extent by CD8(+) T-cells. Plays a role in preparing T-cells for cytokine sensing and differentiation into effector cells by inducing the expression of cytokine receptors IFNGR and IL4R, promoting IFNGR and IL4R signaling and by mediating the clustering of IFNGR with TCR. Acts as a major E-selectin ligand responsible for Th17 cell rolling on activated vasculature and recruitment during inflammation. Mediates Th17 cells, but not Th1 cells, adhesion to E-selectin. Acts as a T-cell counter-receptor for SIGLEC1.; Protects cells from apoptotic signals, promoting cell survival.
Subcellular Location	Membrane; Single-pass type I membrane protein. Cell projection, microvillus. Cell projection, uropodium.; [CD43 cytoplasmic tail]: Nucleus. Nucleus, PML body.
Database References	HGNC: 11249 OMIM: 182160 KEGG: hsa:6693 STRING: 9606.ENSP00000353238 UniGene: Hs.632188
Tissue Specificity	Cell surface of thymocytes, T-lymphocytes, neutrophils, plasma cells and myelomas.

Gene Functions References

CD43 expression was 95.7% in atypical chronic lymphocytic leukemia cases. PMID: 28713070
most non-hematopoietic neoplasms are negative for CD43 expression PMID: 28807337
this study identifies a new signaling pathway for CD43 through the regulation of alternative functions of pyruvate kinase isoform M2, favoring cell survival following activation PMID: 27606486
Forty percent of adenoid cystic carcinomas showed staining for CD43, while no cases of basal cell carcinoma were positive PMID: 25551301
CD43 expression is a novel adverse prognostic factor for patients with diffuse large B-cell lymphomas PMID: 25682152
CD43 polymorphisms are associated with TB susceptibility. PMID: 25078322
Host membrane protein PSGL-1, CD43, and CD44 association with assembling HIV-1 Gag is driven by polybasic sequences present in the cytoplasmic tails of the membrane proteins and in Gag. PMID: 25320329
When used as vaccine in mice, the 2/165 phagotope raised antibodies against the UN1/CD43 antigen, indicating that the 2/165 phagotope mimicked the UN1 antigen structure, and could represent a novel immunogen for cancer immunotherapy PMID: 24356816
CD43 promotes cells transformation by preventing merlin-mediated contact inhibition of growth. PMID: 24260485
We conclude that CD43 is an adverse prognostic marker in DLBCL, and is preferentially expressed in the non-GCB subgroup. PMID: 23617469
CD43 regulates the threshold for T cell activation by targeting Cbl functions. PMID: 21905200
Taken together, these results show that elevated calcium levels induce CD43 capping, and macrophages remove the cells if their nucleolin receptors can bind to the poly-N-acetyllactosaminyl chains of capped CD43. PMID: 23400223
Targeting CD43 in A549 lung cancer cells, increased homotypic adhesion, decreased heterotypic adhesion and transendothelial migration, increased susceptibility to apoptosis and increased vulnerability to lysis by NK cells PMID: 23015282
results suggest that, despite the high CD43 expression in both tumorous and nontumorous Langerhans cells (LCs), the JL1 epitope of CD43 is exposed in immature and neoplastic LCs. PMID: 22790855
Compared to healthy controls, both CD43 mRNA and protein expressions were reduced in T cells from patients with SLE, and were inversely correlated with IgG. PMID: 22613599
CD43 localizes to the nucleus, where it binds chromatin, co-localizes and co-immunoprecipitates with beta-catenin, and enhances the reporter gene expression regulated by beta-catenin PMID: 22576689
The capping of CD43 on the cell surface is a strong signal for phagocytosis that allows phagocytes to differentiate between healthy and apoptotic cells without any additional membrane changes PMID: 22466560
The anti-adhesive function of CD43 in colon carcinoma cells plays a role in the tumorigenesis and metastasis of colorectal carcinoma cells. PMID: 22075155
there exists a negative feedback loop between p53 and CD43: CD43-dependent signaling activates p53, which in turn downregulates the expression of CD43 PMID: 21947346
O-glycosylated CD43 and CD45 molecules on T cells regulates cell adhesion and favors the transmission of HTLV-1 from cell to cell. PMID: 22171268
Data show that Pic, a class 2 SPATE protein produced by Shigella flexneri 2a targets a broad range of human leukocyte glycoproteins including CD43, CD44, CD45, CD93, CD162 and the surface-attached chemokine fractalkine. PMID: 21768350
identification of the tumor antigen UN1 as the transmembrane CD43 sialoglycoprotein PMID: 21372249
Expression of CD43 induces cell rounding, inhibition of cell re-attachment, augmentation of microvilli, and phosphorylation of Ezrin/Radixin/Moesin (ERM)in HEK293T cells. PMID: 21045567
engagement of CD43 may, presumably through the repressing transcription, initiate a Bad-dependent apoptotic pathway. PMID: 11773067
CD43 can be seen as a co-stimulatory cell surface constituent that can modulate HIV-1 expression in T lymphocytes PMID: 12045189
down-regulation of CD43 mRNA levels occurs during activation of the cellline K562. This repression coincides with repression of the transcriptional activity of the CD43 gene promoter. PMID: 12411317
Examination of expression of CD43 in different human cell lines and tumor cell lines PMID: 12499775
Although ezrin-associated CD43 protein is excluded from the inhibitory, i.e., noncytolytic, NK cell immune synapse (IS), it is homogeneously distributed across the IS of activating conjugates. PMID: 12626536
It was also observed that the mucins from colon carcinoma patients had MUC1-type mucins that carried both sialyl-Lewis a and x epitopes and CD43-type sialyl-Lewis a mucins with only low levels of sialyl-Lewis x epitopes. PMID: 12820726
CD43 engagement on normal human T lymphocytes as well as in Jurkat cells results in transient phosphorylation of the zeta-chain and enhanced association of ZAP-70 and Vav to the zeta-chain. PMID: 12902492
Overexpression of SPN causes activation of the tumor suppressor proteins p53 and ARF 1. PMID: 14676827
Four phage antibodies were isolated and used in a preliminary immunohistochemistry study of CD43 expression on frozen colorectal adenoma and carcinoma tissue. PMID: 14719063
findings suggest that the CD43 molecules expressed on CD4+ memory T cells may be capable of enhancing the costimulatory signaling and hence providing accessory functions to TCR-mediated activation processes PMID: 15187099
Microarray analysis of inflammatory genes shows 1 group of genes coregulated by both stimuli and 2 further groups of target genes affected solely by costimulation or primarily by CD43. PMID: 15280197
CD43 is expressed by a variety of carcinoma cell lines, and plays a role in tumour cell-peritoneal adhesion probably via interactions with its putative ligand ICAM-1 PMID: 15449712
Data suggest that PKCtheta plays a critical role in the co-stimulatory functions of CD43 in human T cells. PMID: 15522211
CD43 is a T-cell E-selectin ligand distinct from PSGL-1 which expands the role of CD43 in the regulation of T-cell trafficking. PMID: 16269612
CD43 induces a signaling cascade that prolongs the duration of T cell receptor signaling, thereby supporting the temporality with which certain molecules are engaged as a mechanism to fine tune T cell signal quality, and ultimately immune function. PMID: 16751378
early progenitors committed to hematopoietic development could be identified by surface expression of leukosialin PMID: 16757688
Promotes cell growth and is a potential contributor to tumor development. PMID: 17891181
Lymphoepithelial lesions pattern, CD43 coexpression, and clonal plasma cell component in extranodal marginal zone B-cell lymphoma (EMZL) is site-dependent, and the differences may aid in the diagnosis of EMZLs at different anatomic sites. PMID: 17979485
triggering CD43 and the underlying signaling pathways enhance LFA-1 adhesiveness while CD43 also negatively regulates LFA-1 induction via other receptors by dynamic interaction with either LFA-1 or CD147. PMID: 17996943
CD43 seems to be selectively expressed in a subset of adenoid cystic carcinomas and its significance in salivary tumors is discussed. PMID: 18227725
The cleavage of neutrophil leukosialin (CD43) by cathepsin G releases its extracellular domain and triggers its intramembrane proteolysis by presenilin/gamma-secretase PMID: 18586676
Streptococcus gordonii DL1 surface protein Hsa binds to the host cell membrane glycoproteins CD11b, CD43, and CD50 PMID: 18678668

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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.