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TSLP (R127A, R130A) Avi-His-Tag Recombinant

Recombinant human TSLP (thymic stromal lymphopoietin), encompassing amino acids 29-159. This construct contains mutations R127A and R130A that impact the putative furin cleavage site present in the protein. This construct contains a C-terminal Avi-tag™ followed by a His-tag (6xHis) .

Product Specifications

Background

TSLP (thymic stromal lymphopoietin) is a protein that functions as a type I cytokine, as an alarmin and growth factor in the immune system. It is involved in type 2 immune responses, TH2 (T helper 2 cells) responses, and the maturation and recruitment of dendritic cells (DCs), T cells, B cells, neutrophils, mast cells, and other lymphoid cells.  It can be produced by epithelial and stromal cells in lung, skin, and gastric system, but also by DCs, basophils and mast cells. Its expression can be induced by infections, pro-inflammatory cytokines, proteases, and even mechanical injury. For instance, it can be produced in the lungs in response to infection with influenza or rhinovirus. Its role as alarmin can result in increasing inflammation. TSLP is linked to allergic reactions such as asthma, atopic dermatitis, and food allergies, by inducing the expression of OX40L, CD80 and CD86 and stimulating CD4+T cells. The mutations R127A and R130A function to remove a putative furin site and further stabilize the full-length protein in HEK293 cells. In 2021, the TLSP-neutralizing antibody tezepelumab was approved for the treatment of severe asthma. Targeting TSLP is an active area of investigation with ongoing clinical trials for the treatment of autoimmune disorders.

UniProt

Q969D9

Tag

C-terminal Avi-Tag™, His-Tag

Applications

Useful for binding assays.

Endotoxin

55.3 EU/mg

Purity

≥ 90%

Format

Aqueous buffer solution

Shipping Conditions

-80°C

Storage Conditions

> 6 months at –80°C.

Calculated Molecular Weight

18.1 kDa + glycans

Formulation

8 mM phosphate, pH7.4,110 mM NaCl, 2.2 mM KCl, and 20% glycerol

Glycosylation

This protein runs at a higher MW by SDS-PAGE due to glycosylation.

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