ARG70684

Human IL17 / IL17A recombinant protein (His-tagged, C-ter)

Human IL17 / IL17A recombinant protein (His-tagged, C-ter) for SDS-PAGE

Overview

Product Description CHO expressed, His-tagged (C-ter) Human IL17 / IL17A recombinant protein
Tested Application SDS-PAGE
Target Name IL17 / IL17A
Species Human
A.A. Sequence Ala26 - Ala158
Expression System CHO
Alternate Names IL-17A; Interleukin-17A; IL-17; CTLA8; IL17; CTLA-8; Cytotoxic T-lymphocyte-associated antigen 8

Properties

Form Powder
Purification Note Endotoxin level is less than 0.1 EU/µg of the protein, as determined by the LAL test.
Purity > 95% (by SDS-PAGE)
Buffer PBS (pH 7.4)
Reconstitution It is recommended to reconstitute the lyophilized protein in sterile water to a concentration not less than 200 μg/mL and incubate the stock solution for at least 20 min at room temperature to make sure the protein is dissolved completely.
Storage Instruction For long term, lyophilized protein should be stored at -20°C or -80°C. After reconstitution, aliquot and store at -20°C or -80°C for up to one month. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening.
Note For laboratory research only, not for drug, diagnostic or other use.

Bioinformation

Gene Symbol IL17A
Gene Full Name interleukin 17A
Background The protein encoded by this gene is a proinflammatory cytokine produced by activated T cells. This cytokine regulates the activities of NF-kappaB and mitogen-activated protein kinases. This cytokine can stimulate the expression of IL6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO). High levels of this cytokine are associated with several chronic inflammatory diseases including rheumatoid arthritis, psoriasis and multiple sclerosis. [provided by RefSeq, Jul 2008]
Function Induces stromal cells to produce proinflammatory and hematopoietic cytokines. Enhances the surface expression of ICAM1/intracellular adhesion molecule 1 in fibroblasts. [UniProt]
PTM Found both in glycosylated and nonglycosylated forms.