Recombinant Human CD93 Protein (Fc Tag)

Name: Recombinant Human CD93 Protein (Fc Tag)
Brand: Beta LifeScience
SKU: BLPSN-1160
Availability: InStock

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

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Product Overview

Tag	Fc
Host Species	Human
Accession	Q9NPY3
Synonym	C1qR, C1qR(P), C1QR1, C1qRP, CDw93, dJ737E23.1, ECSM3, MXRA4
Background	CD93 or C1q receptor 1 (C1qR) is an about 12 kDa O-sialoglycoprotein that within the hematopoietic system is selectively expressed on cells of the myeloid lineage. CD93/C1qR is a highly glycosylated transmembrane protein expressed on monocytes, neutrophils, endothelial cells, and stem cells. CD93 was originally identified as a myeloid cell-surface marker and subsequently associated with an ability to modulate phagocytosis of suboptimally opsonized immunoglobulin G and complement particles in vitro. CD93/C1qR, a receptor expressed during early B-cell development, is reinduced during plasma-cell differentiation. High CD93/CD138 expression was restricted to antibody-secreting cells both in T-dependent and T-independent responses as naive, memory, and germinal-center B cells remained CD93-negative. CD93 was expressed on (pre)plasmablasts/plasma cells, including long-lived plasma cells that showed decreased cell cycle activity, high levels of isotype-switched Ig secretion, and modification of the transcriptional network. CD93 is important for the maintenance of plasma cells in bone marrow niches.
Description	A DNA sequence encoding the human CD93 (Q9NPY3) extracellular domain (Met 1-Lys 580) was fused with the Fc region of human IgG1 at the C-terminus.
Source	HEK293
Predicted N Terminal	Thr 22
AA Sequence	Met 1-Lys 580
Molecular Weight	The recombinant human CD93/Fc is a disulfide-linked homodimer. The reduced monomer consists of 800 a.a. after removal the signal peptide and has a predicted molecular mass of 85.2 kDa. As a result of glycosylation, rh CD93/Fc monomer migrates as an approximately 125 kDa band in SDS-PAGE under reducing conditions.
Purity	>85% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the 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	Receptor (or element of a larger receptor complex) for C1q, mannose-binding lectin (MBL2) and pulmonary surfactant protein A (SPA). May mediate the enhancement of phagocytosis in monocytes and macrophages upon interaction with soluble defense collagens. May play a role in intercellular adhesion.
Subcellular Location	Membrane; Single-pass type I membrane protein.
Database References	HGNC: 15855 OMIM: 120577 KEGG: hsa:22918 STRING: 9606.ENSP00000246006 UniGene: Hs.97199
Tissue Specificity	Highly expressed in endothelial cells, platelets, cells of myeloid origin, such as monocytes and neutrophils. Not expressed in cells of lymphoid origin.

Gene Functions References

Report increased CD93 expression in patients with chronic plaque psoriasis and propose the C allele of rs2749817 as a new risk allele for psoriasis. PMID: 28421233
Results show that CD93 and MMRN2 are co-expressed in the blood vessels of various tumors and their interaction modulates the angiogenic process. PMID: 28912033
These findings identify novel protein interactions involving CLEC14A, CD93 and CD248 with MMRN2 as targetable components of vessel formation PMID: 28671670
CD93 and Other Plasma Cell Survival Factor Genes Associated with Measles-Specific Antibody Response after Vaccination PMID: 27529750
Soluble expression of disulfide-bonded C-type lectin like domain of human CD93 in the cytoplasm of Escherichia coli. The recombinant protein could alter LPS pro-inflammatory activity on THP1 cells. PMID: 27742562
Vascular CD93 expression is elevated in nasopharyngeal carcinoma and is correlated with T classification, N classification, distant metastasis, clinical stage and poor prognosis (all P < 0.05). In addition, overexpression of CD93 promoted angiogenesis in vitro. PMID: 27255994
both transmembrane and soluble CD93 are overexpressed in patients with neovascular Age-Related Macular Degeneration. PMID: 27859225
Elevated serum sCD93 levels reflected exacerbated status of allergic diseases, including CSU [chronic spontaneous urticaria ], AR[allergic rhinitis], and asthma. ICS [inhaled corticosteroid] use significantly diminished serum sCD93 levels in steroid-naive patients with BA[Bronchial asthma]. This result may suggest sCD93 in serum as a therapeutic marker for allergic inflammation. PMID: 28332366
Data show that CD93 antigen proved to be phosphorylated on tyrosine 628 and 644 following cell adhesion on laminin through dystroglycan. PMID: 26848865
CD93 expression identifies a predominantly cycling, non-quiescent leukemia-initiating cell population in MLL-rearranged AML, providing opportunities for selective targeting and eradication of LSCs. PMID: 26387756
The T/T genotype of SNP rs2749817 of CD93 is associated with disseminated cancer. PMID: 26008729
CD93 is a key regulator of glioma angiogenesis and vascular function, acting via cytoskeletal rearrangements required for cell-cell and cell-matrix adhesion. PMID: 26363010
These data support a mechanism whereby gC1qR plays an important role in HPV-16 E2-induced human cervical squamous carcinoma cell apoptosis via a mitochondria-dependent pathway. PMID: 25288439
The data indicate that gC1qR inhibits viability, migration and proliferation of cervical squamous cells carcinoma via the p38 MAPK signalling pathway. PMID: 23052251
Antibody-dependent enhancement of parvovirus B19 involves an alternative mechanism mediated by the heat-sensitive complement factor C1q and its receptor, CD93. PMID: 24807719
Expression of CD93 on the lymphocyte population of peripheral blood cells from infants at 1 month after birth was also significantly decreased, compared with that for neonatal umbilical cord blood. PMID: 24033555
HPV 16 E2 induces apoptosis by silencing the gC1qR gene or inhibiting p38 MAPK/JNK signalling in cervical squamous cell carcinoma PMID: 23651874
These data support a mechanism whereby gC1qR induces apoptosis through the mitochondrial and p53-dependent pathways in cervical squamous cell carcinoma. PMID: 23268996
soluble EGF-like domain containing CD93 protein is a novel angiogenic factor acting on the endothelium PMID: 23272129
[review] Following a comprehensive summary of CD93 expression patterns, this review focuses on recent findings that address the putative function of CD93 in inflammation and innate immunity. PMID: 22206251
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
Results suggest that the plasma concentration of soluble CD93 is a potential novel biomarker for Coronary Artery Disease (CAD), including MI. PMID: 21332844
expression on naive T lymphocytes (CD4(+)CD45RA (+) cells) in human neonatal umbilical cord blood PMID: 20512406
both B1 receptor and gC1q receptor are involved in the vascular leakage induced by hereditary and acquired angioedema plasma. PMID: 19796797
To clarify the cellular and molecular properties of C1qRp it has been demonstrated that C1q does not show enhanced binding to C1qRp-transfected cells, is not a receptor for C1q, and is identical to CD93 with functions relevant to intercellular adhesion. PMID: 11994479
C1qRp defines a new human stem cell population with hematopoietic and hepatic potential PMID: 12140365
O-glycosylation is important in the stable cell surface expression of C1qRP/CD93 PMID: 12891708
Taken together, these findings indicate that the expression of the CD93 molecule identified by CD93 mAb (mNI-11) is dramatically decreased on U937 cells with apoptotic properties PMID: 18094537
RNAi-mediated suppression of gC1qR/p32 markedly reduced HTNV binding and infection in human lung epithelial A549 cells PMID: 18834607

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.