Recombinant Rat Urokinase Plasminogen Activator Surface Receptor (PLAUR) Protein (His)

Name: Recombinant Rat Urokinase Plasminogen Activator Surface Receptor (PLAUR) Protein (His)
Brand: Beta LifeScience
SKU: BLC-04658P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Rat Urokinase Plasminogen Activator Surface Receptor (PLAUR) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P49616
Target Symbol	PLAUR
Synonyms	PlaurUrokinase plasminogen activator surface receptor; U-PAR; uPAR; CD antigen CD87
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	LRCIQCESNQDCLVEECALGQDLCRTTVLREWEDAEELEVVTRGCAHKEKTNRTMSYRMGSVIVSLTETVCATNLCNRPRPGARGRPFPRGRYLECASCTSLDQSCERGREQSLQCRYPTEHCIEVVTLQSTERSVKDEPYTKGCGSLPGCPGTAGFHSNQTFHFLKCCNFTQCNGGPVLDLQSLPPNGFQCYSCEGNSTFGCSYEETSLIDCRGPMNQCLEATGLDVLGNRSYTVRGCATASWCQGSHVADSFQTHVNLSISCCNGSGCNRPTG
Expression Range	25-299aa
Protein Length	Full Length of Mature Protein
Mol. Weight	34.1 kDa
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.
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	Acts as a receptor for urokinase plasminogen activator. Plays a role in localizing and promoting plasmin formation. Mediates the proteolysis-independent signal transduction activation effects of U-PA.
Subcellular Location	[Isoform 1]: Cell membrane; Lipid-anchor, GPI-anchor.; [Isoform 2]: Secreted.
Database References	KEGG: rno:50692 STRING: 10116.ENSRNOP00000063960 UniGene: Rn.82711

Gene Functions References

Increased postmortem PLAUR expression could serve as a biomarker to aid diagnosis of early myocardial infarction. PMID: 24935436
Rapamycin could promote podocyte migration through the up-regulation of uPAR leading to proteinuria. PMID: 24815166
uPA, uPAR, MMP-2 and MMP-9 play an important role in GBM growth. Blockade of uPA and interruption of the proteolytic cascade could become a useful tool in the therapy of GBM PMID: 22773570
uPAR associates with activating enhancer-binding protein 2alpha (AP2a) and mediates beta-catenin gene transcription. PMID: 22511755
study examines the expression and function of uPAR in developing rat ventral prostates PMID: 11798065
Expression pattern of the urokinase-plasminogen activator system in rat DS-sarcoma: role of oxygenation status and tumour size PMID: 11953898
Decreased expression of intercellular adhesion molecule-1 (ICAM-1) is associated with tumor cell spreading in vivo. PMID: 12198772
demonstrated focused activation of proteolytic enzymatic activity in several cell types and showed that the uPA/uPAR system is an important contributor to focal pericellular proteolysis PMID: 15042374
Altered expression of uPAR in diabetic nephropathy was associated with mesangial expansion. PMID: 15322501
Domain 2 of the urokinase receptor plays a pivotal role in the regulation of uPAR-integrin alphavbeta3 interactions PMID: 15863511
The members of caspases, MEK1/2, PKC, and NF-kappaB are involved in TRAIL-induced expression of uPA, IL-8, MMP-7 and MMP-9. PMID: 18397859
In animals undergoing SE, uPAR expression increased dramatically, peaking at 1 and 4 days after SE. Increased uPAR expression during post-injury phase supports its contribution to tissue remodeling in the brain. PMID: 19527776

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.