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ACROBiosystems Biotinylated Human IL-17 RA / CD217 Protein, Fc, Avitag™

Biotinylated Protein

457.25€ - 2011.89€

Specifications

Accession Number NP_055154.3
Molecular Weight (g/mol) 61.9 kDa
Source Biotinylated Human IL-17 RA, Fc,Avitag (ILA-H82F1) is expressed from human 293 cells (HEK293). It contains AA Leu 33 - Trp 320 (Accession # Q96F46-1).
Immunogen Leu 33 - Trp 320
Storage Requirements -20°C
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Product Code Brand Quantity Price Quantity & Availability  
15817087
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ACROBiosystems
ILA-H82F1-200UG
200 μg
2011.89€
200µg
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15827087
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ACROBiosystems
ILA-H82F1-25UG
25 μg
457.25€
25µg
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Estimated Shipment: 06-05-2024
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Description

Description

Interleukin 17 receptor A (IL17RA) is also known as cluster of differentiation w217 (CDw217), is a pro-inflammatory cytokine secreted by activated T-lymphocytes, belong to ubiquitous type I membrane glycoprotein, and binds with low affinity to interleukin 17A (IL17A). IL 17R mRNA exhibits a broad tissue distribution, and has been detected in virtually all cells and tissues tested . IL 17RA associates with IL 17RC to form a signaling receptor complex for IL 17 and IL 17F . Ligand and IL 17RA ligation promotes T cell activation and the production of IL - 6, G-CSF, SCF, and multiple pro-inflammatory chemokines. Defects in IL17RA are the cause of familial candidiasis type 5 (CANDF5).

This protein carries a human IgG1 Fc tag at the C-terminus, followed by a Avi tag (Avitag™). The protein has a calculated MW of 61.9 kDa. As a result of glycosylation, the protein migrates as 80-115 kDa under reducing (R) condition, and 150-200 kDa under
Specifications

Specifications

NP_055154.3
Biotinylated Human IL-17 RA, Fc,Avitag (ILA-H82F1) is expressed from human 293 cells (HEK293). It contains AA Leu 33 - Trp 320 (Accession # Q96F46-1).
-20°C
IL-17 RA
Human
Tris with Glycine, Arginine and NaCl, pH7.5
HEK293
MABSol™ Biotin Labeled Proteins
61.9 kDa
Leu 33 - Trp 320
CD217,CDw217,IL-17 RA,IL17R,CANDF5,hIL-17 R
Precision Avi
Fc Tag and Avi Tag
Less than 1.0 EU / μg by the LAL method.
Powder
>95% as determined by SDS-PAGE
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