Recombinant Human T-Cell Surface Glycoprotein Cd1C (CD1C) Protein (His)

Name: Recombinant Human T-Cell Surface Glycoprotein Cd1C (CD1C) Protein (His)
Brand: Beta LifeScience
SKU: BLC-04081P
Price: 299.0 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Price Save $250

Size

100ug

Product Overview

Description	Recombinant Human T-Cell Surface Glycoprotein Cd1C (CD1C) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P29017
Target Symbol	CD1C
Synonyms	BDCA1; CD1; CD1A; CD1c; CD1c antigen; CD1C antigen c polypeptide; CD1c molecule; CD1C_HUMAN; Cortical thymocyte antigen CD1C; Differentiation antigen CD1 alpha 3; R7; T cell surface glycoprotein CD1c; T-cell surface glycoprotein CD1c
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	NADASQEHVSFHVIQIFSFVNQSWARGQGSGWLDELQTHGWDSESGTIIFLHNWSKGNFSNEELSDLELLFRFYLFGLTREIQDHASQDYSKYPFEVQVKAGCELHSGKSPEGFFQVAFNGLDLLSFQNTTWVPSPGCGSLAQSVCHLLNHQYEGVTETVYNLIRSTCPRFLLGLLDAGKMYVHRQVRPEAWLSSRPSLGSGQLLLVCHASGFYPKPVWVTWMRNEQEQLGTKHGDILPNADGTWYLQVILEVASEEPAGLSCRVRHSSLGGQDIILYWGHHFSM
Expression Range	18-302aa
Protein Length	Partial
Mol. Weight	36.2kDa
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	Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells.
Subcellular Location	Cell membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein. Lysosome.
Database References	HGNC: 1636 OMIM: 188340 KEGG: hsa:911 STRING: 9606.ENSP00000357152 UniGene: Hs.132448
Tissue Specificity	Expressed on cortical thymocytes, on certain T-cell leukemias, and in various other tissues.

Gene Functions References

these results demonstrated the mechanism that suppression of CD1c by BCG infection is mediated by miR-381-3p PMID: 27296666
We found a significant difference in the density of intraepidermal CD1c+ cells between the examined lesions; the mean CD1c cell count was 7.00/mm(2) for invasive melanomas, 2.94 for in situ melanomas, and 13.35 for dysplastic nevi PMID: 28331853
Stressed beta-cells have little effect on human BDCA1-expressed dendritic cells activation and function, while enterovirus-infected beta-cells impact these cells significantly. PMID: 26888163
Circulating atopic dermatitis pre-dendritic CD1c+ cells are premature and bear atopic characteristics even without tissue-specific stimulation, suggesting that their development is not only influenced by the skin microenvironment, but also by the local milieu in the blood. PMID: 27701668
human CD1c adopts different conformations dependent on ligand occupancy of its groove, with CE and ASG stabilizing CD1c conformations that provide a footprint for binding of CD1c self-reactive T-cell receptors PMID: 26884207
There was a significant increase of blood CD1c(+) myeloid dendritic cells in autoimmune uveitis patients. The mature phenotype and function of CD1c(+) mDC1 were regulated by TNFalpha via a p38 MAPK-dependent pathway. PMID: 25784146
decidual CD1c(+) dendritic cells with Toxoplasma gondii infection have enhanced cytotoxicity of decidual natural killer cells PMID: 24573986
hMPV-infected BDCA-1(+) and BDCA-3(+) mDCs induced expansion of Th17 cells, in response to RSV, BDCA-1(+) mDCs induced expansion of Th1 cells and BDCA-3(+) mDCs induced expansion of Th2 cells and Tregs PMID: 24918929
mLPA-specific T cells efficiently kill CD1c(+) acute leukemia cells, poorly recognize nontransformed CD1c-expressing cells, and protect immunodeficient mice against CD1c(+) human leukemia cells. PMID: 24935257
Activated dendritic cell subsets expressing CD141/CLEA9A/CD1c, likely recruited into the tubulointerstitium, are positioned to play a role in the development of fibrosis and, thus, progression to chronic kidney disease. PMID: 24049150
CD1c+ myeloid dendritic cells were increased in idiopathic pulmonary fibrosis patients versus controls. PMID: 19556741
RSV infection induces a distinct pattern of costimulatory molecule expression and cytokine production by BDCA-1(+) and BDCA-3(+) mDCs, and impairs their ability to stimulate T cell proliferation. PMID: 23829893
Downregulation of both CD1c and CD1d expression through a Vpu-dependent and Nef-independent mechanism, and the concomitant HIV-1-induced production of host cholesterol decreased the extent of CD1c and CD1d modulation. PMID: 23347583
Molecular mechanisms by which CD1c captures distinct classes of self- and mycobacterial antigens are reviewed. Review. PMID: 23468110
CD1c-PM complexes stain T cell receptors (TCRs), providing direct evidence for a ternary interaction among CD1c-lipid-TCR. PMID: 23530121
Data suggest that when CD1c is up-regulated, ILT4 is recruited to CD1c, thus reducing the inhibitory effect of immunoglobulin-like transcript 4 (ILT4) on CD1d recognition. PMID: 22888216
Escherichia coli-activated CD1c(+) dendritic cells suppressed T-cell proliferation in an IL-10-dependent manner PMID: 22678905
Identification of self-lipids presented by CD1c and CD1d proteins. PMID: 21900247
Accumulation of BDCA-1 and BDCA-2 around neovessels showed that mDCs and pDCs are recruited to advanced arteriosclerotic plaques. PMID: 21436634
both CD1d and CD1c are upregulated by retinoic acid receptor alpha signaling in human B cells PMID: 21451111
Expression of dendritic cell markers CD11c/BDCA-1 and CD123/BDCA-2 in coronary artery disease upon activation in whole blood. PMID: 20888334
B cell chronic lymphocytic leukemia cells significantly down-regulated transcripts from CD1c and CD1d genes, permitting cells to evade the immune response PMID: 12454749
CD1c expression was detected on monocytes in the majority of sickle cell anemia patients, and was highly expressed in Sbeta thalassemia patients. PMID: 15556687
Data show that CD1c represents the second member of the CD1 family to present lipopeptides. PMID: 19468063
A model of CD1c with bound mannosyl-beta(1)-phosphomycoketide was constructed and analyzed through molecular dynamics simulations. PMID: 19828201

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.