Mouse PSGL-1 Protein 3029

$315.00 – $1,050.00

Summary

Expression: HEK293
Pure: Yes (HPLC)
Amino Acid Range: Gln42-Cys307

SKU: 3029parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	Q62170
express system	HEK293
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	P-selectin glycoprotein ligand-1 (PSGL-1) has long been studied as an adhesion molecule involved in immune cell trafficking and is recognized as a regulator of many facets of immune responses by myeloid cells. PSGL-1 also regulates T cell migration during homeostasis and inflammatory settings.
molecular weight	The protein has a predicted MW of 28.74 kDa. Due to glycosylation, the protein migrates to 68-108 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Mouse PSGL-1 Protein 3029

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
P-selectin glycoprotein ligand-1 (PSGL-1) has long been studied as an adhesion molecule involved in immune cell trafficking and is recognized as a regulator of many facets of immune responses by myeloid cells. PSGL-1 also regulates T cell migration during homeostasis and inflammatory settings.
Protein names P-selectin glycoprotein ligand 1 (PSGL-1) (Selectin P ligand) (CD antigen CD162)
Gene names Selplg,Selplg Selp1 Selpl
Mass 10090Da
Function A SLe(x)-type proteoglycan, which through high affinity, calcium-dependent interactions with E- and P-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation. Critical for the initial leukocyte capture.
Subellular location Cell membrane ; Single-pass membrane protein .
Tissues Highly expressed in blood, bone marrow, brain, adipose tissue, spleen, and thymus. Also expressed in heart, kidney, liver, muscle, ovary, and stomach.
Structure Homodimer; disulfide-linked. Interacts with P- and E-selectins, through their lectin/EGF domains. Interaction with P-selectin requires sialyl Lewis X glycan modification and tyrosine sulfation, probably on Tyr-54, for high affinity binding (By similarity). Dimerization appears not to be required for P-selectin/SELP binding (By similarity). Interacts with SNX20 (By similarity). Interacts with MSN and SYK; mediates SYK activation downstream of SELPLG (By similarity). Interacts with HAVCR1 (By similarity).
Post-translational modification Displays complex, core-2, sialylated and fucosylated O-linked oligosaccharides, at least some of which appear to contain poly-N-acetyllactosamine with varying degrees of substitution. Mainly disialylated or neutral forms of the core-2 tetrasaccharide, Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH. The GlcN:GalN ratio is approximately 2:1 and the Man:Fuc ratio 3:5. Contains about 14% fucose with alpha-1,3 linkage present in two forms: One species is a disialylated, monofucosylated glycan, and the other, a monosialylated, trifucosylated glycan with a polylactosamine backbone. The fucosylated forms carry the Lewis antigen and are important for interaction with selectins and for functioning. No sulfated O-glycans. Some N-glycosylation (By similarity).
Target Relevance information above includes information from UniProt accession: Q62170
The UniProt Consortium

The purity of Mouse PSGL-1 is greater than 95% as determined by SEC-HPLC.

Mouse PSGL-1 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.