Human CD299 protein fragment (ab83920)
- Product nameHuman CD299 protein fragmentSee all CD299 proteins and peptides ...
- SourceHEK 293 cells
- Amino Acid Sequence
- SequenceTheoretical sequence: HGTELPSPPSKLQVSKVPSSLSQEQSEQD AIYQNLTQLKAAVGELSEK SKLQEIYQELTQLKAAVGE LPEKSKLQEIYQELTRLKAAVGELPEKSK LQEIYQELT RLKAAVGELPEKSKLQEIYQELTRLKAAVGELPEKSKLQ EIYQELTELKAAVGELPEKSKLQEIYQELTQLKAAVGEL PDQSKQQQI YQELTDLKTAFERLCRHCPKDWTFFQGNC YFMSNSQRNWHDSVTACQE VRAQLVVIKTAEEQNFLQL QTSRSNRFSWMGLSDLNQEGTWQWVDGSP LSPSFQRYW NSGEPNNSGNEDCAEFSGSGWNDNRCDVDNYWICKKPAA CFRDGIPKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVF LFPPKPKDT LMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNS TYRVVSVLTVLHQDWLNGK EYKCRVSNKALPAPIEKTISKAKGQPREP QVYTLPPSR DELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTT PPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALH NHYTQKSLS LSPGK
- Amino acids71 to 398
Our Abpromise guarantee covers the use of ab83920 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
- Purity> 95
% by SDS-PAGE.
- Concentration information loading...
Preparation and Storage
- Stability and Storage
Store at +4°C.
Constituents: 10% Trehalose, 1% Human serum albumin
- ReconstitutionIt is recommended that 0.5 ml of sterile phosphate-buffered saline be added to the vial. Following reconstitution short-term storage at 4°C is recommended, with longer-term storage in aliquots at -18 to -20°C. Repeated freeze thawing is not recommended.
- C type lectin domain family 4, member M
- C-type lectin domain family 4 member M
- CD209 antigen like
- CD209 antigen like protein 1
- CD209 antigen-like protein 1
- CD299 antigen
- DC SIGN related protein
- DC SIGN2
- DC SIGNR
- DC-SIGN-related protein
- DCSIGN related protein
- Dendritic cell-specific ICAM-3-grabbing non-integrin 2
- L SIGN
- Liver/lymph node specific ICAM3 grabbing nonintegrin
- Liver/lymph node-specific ICAM-3-grabbing non-integrin
- Mannose binding C type lectin DC SIGNR
- FunctionProbable pathogen-recognition receptor involved in peripheral immune surveillance in liver. May mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. Probably recognizes in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens, including HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus glycoproteins, HCV E2, and human SARS coronavirus protein S. Is a receptor for ICAM3, probably by binding to mannose-like carbohydrates. Is presumably a coreceptor for the SARS coronavirus.
- Tissue specificityPredominantly highly expressed in liver sinusoidal endothelial cells and in lymph node. Found in placental endothelium but not in macrophages. Expressed in type II alveolar cells and lung endothelial cells.
- Sequence similaritiesContains 1 C-type lectin domain.
- DomainThe tandem repeat domain, also called neck domain, mediates oligomerization.
- Cellular localizationSecreted and Cell membrane.
Human CD299 protein fragment images
Lane 1 – MW markers; Lane 2 – ab83920; Lane 3 – ab83920 treated with PNGase F to remove potential N-linked glycans. 10 µg protein loaded per lane. Deep Purple stained.
Drop in MW after treatment with PNGase F indicates presence of N-linked glycans. Band in lane 3 at 35 kDa is PNGase F protein.
A sample of ab83920 without carrier protein was reduced and alkylated. 40 µg protein was loaded, focused on a 3-10 IPG strip then run on a 4-20% Tris-HCl 2D gel. Spot train (Deep Purple™ stained) indicates presence of multiple glycoforms of ab83920. Spots within the spot train were cut from the gel and identified by protein mass fingerprinting as CD299 (Fc Chimera).
Post-translational modifications result in protein heterogeneity. The densitometry scan demonstrates the purified human cell expressed protein exists in multiple glycoforms, which differ according to their level of post-translational modification.
The triangle indicates theoretical pI and MW.
References for Human CD299 protein fragment (ab83920)
ab83920 has not yet been referenced specifically in any publications.