Recombinant Human Paired immunoglobulin-like type 2 receptor alpha (PILRA), partial

Product Details

Abbreviation
PILRA
Purity
>85% (SDS-PAGE)
Target Names
PILRA
Uniprot NO.
Alternative Names
Cell surface receptor FDF03; FDF03; Inhibitory receptor PILR-alpha; paired immunoglobulin-like receptor alpha; Paired immunoglobulin-like type 2 receptor alpha; PILRA; PILRA_HUMAN
Species
Homo sapiens (Human)
Source
Yeast
Protein Length
Partial
Tag Info
N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Storage Condition
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 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.

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Target Background

Function(From Uniprot)
Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. PILRA is thought to act as a cellular signaling inhibitory receptor by recruiting cytoplasmic phosphatases like PTPN6/SHP-1 and PTPN11/SHP-2 via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules. Receptor for PIANP.; (Microbial infection) Acts as an entry co-receptor for herpes simplex virus 1.
Gene References into Functions
  1. Data suggest that, although PILRA exhibits essentially the same recognition of different glycopeptides, slight modifications of linker sugar cause significant changes in a wide area of the binding interface, resulting in a reduction of binding affinity; analogs/fragments of gpb were used in these studies. (PILRA = paired immunoglobin like type 2 receptor alpha; gpb = envelope glycoprotein B, Herpes simplex virus type 1) PMID:29046357
  2. The interaction of NK cells with PILRalpha expressing targets lead to elevated IFNgamma secretion and cytotoxicity. In conclusion, PILRalpha is a novel NK activating ligand which binds and activates an unknown NK receptor expressed on a unique NK cell subset. PMID:27029068
  3. Transcriptome wide association study results identified two novel genes as statistically significantly associated with nonobstructive azoospermia susceptibility: PILRA and ZNF676. PMID:29202958
  4. PILRalpha exhibits large conformational change to recognize simultaneously both the sTn O-glycan and the compact peptide structure constrained by proline residues PMID:24889612
  5. These results contribute our knowledge of the biological functions of HBVDNAPTP1 and provide novel data to aid in the further analysis of the regulatory mechanism of this protein. PMID:24253495
  6. We demonstrated that three residues (Y2, R95, and W108) presented on the surface of PILRalpha form the sialic acid binding site equivalent to those in siglecs but are arranged in a unique linear mode. PMID:24843130
  7. The amino terminus of herpes simplex virus 1 gK is functionally and physically associated with the gB-PILRalpha protein complex and regulates membrane fusion of the viral envelope with cellular membranes during virus entry. PMID:23302878
  8. The authors show that the human ocular and highly neurovirulent HSV-1 strain McKrae enters substantially more efficiently into cells via the gB-specific human paired immunoglobulin-like type-2 receptor-alpha (hPILR-alpha). PMID:22695228
  9. Data show that PILRalpha/ligand interactions require conserved PILRalpha arginine (Arg)-133 (mouse) and Arg-126 (human). PMID:22396535
  10. These results suggest that PANP is involved in immune regulation as a ligand of the PILRalpha. PMID:21241660
  11. PILRalpha protein was successfully crystallized at 293 K using the sitting-drop vapour-diffusion method and the crystals diffracted to 1.3 A resolution. PMID:18097101
  12. The results demonstrate that cellular receptors for both gB and gD are required for HSV-1 infection and that PILRalpha plays an important role in HSV-1 infection as a coreceptor that associates with gB. PMID:18358807
  13. viral entry via PILRalpha appears to be conserved but that there is a PILRalpha preference among alphaherpesviruses PMID:19244335
  14. Insertional mutations of gB reduced cell fusion activity when PILRalpha was overexpressed much more than nectin-1. PMID:19457990

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Subcellular Location
[Isoform 1]: Cell membrane; Single-pass type I membrane protein.; [Isoform 2]: Cell membrane; Single-pass type I membrane protein.; [Isoform 3]: Secreted.; [Isoform 4]: Secreted.
Tissue Specificity
Predominantly detected in hemopoietic tissues and is expressed by monocytes, macrophages, and granulocytes, but not by lymphocytes. Also strongly expressed by dendritic cells (DC); preferentially by CD14+/CD1a- DC derived from CD34+ progenitors. Also expr
Database Links

HGNC: 20396

UNIGENE: Hs.444407

KEGG: hsa:29992

STRING: 9606.ENSP00000198536

OMIM: 605341

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