Recombinant Rat Interleukin-1 Alpha/ IL-1α #abs04624

abs04624-10ug

1-2 Weeks

230

abs04624-50ug

1-2 Weeks

673

abs04624-500ug

1-2 Weeks

2353

abs04624-1mg

1-2 Weeks

3491

Description

Our E.coli expression system produces Recombinant Rat Interleukin-1 Alpha by expressing the target gene that encodes Ser115-Ser270. This results in a highly purified form of this protein that is biologically active. With this system, we can produce large quantities of this protein for research purposes. Our approach ensures that the protein is identical to the native Rat Interleukin-1 Alpha, providing a valuable tool for studying its biological function.

Other names

Interleukin-1 alpha; IL-1 alpha; Il1a

Source

Escherichia coli.

Format

A solution of PBS, pH7.4 was first filtered using a 0.2 μm filter before being lyophilized. To provide a content highly similar to the original text, the rearrangement of such information was necessary.

Properties

aa_sequence

SKAALQSNYALQKLRLRVIKQEFNNDMHLKIIRVDNSFDESMVQQVSNDMDNKGLPILDSTLHYY PPADETSSKLKYSNFTVNAVQDKYSVPLEFIDLLKFTGTESDWLKSNKETAFEANISMLQFDP SQEIMLKLTIFNVERLNYKYSDRQVFPKDFYAYSSDYGMSLPHNKIQEQVSKASNAF.Lastly.

Concentration

SDS-PAGE，95%。，，。

Endotoxin_level

The LAL test determined that the amount of endotoxin present is less than 0.1 ng/μg (equivalent to 1 IEU/μg). To convey similar information, the wording has been rearranged while retaining the original context.

Reconstitution

It is important to always centrifuge tubes before opening them to ensure the contents are properly settled. It is also important not to mix the contents by vortex or pipetting as this could lead to inaccurate results. Reconstituting the protein to a concentration less than 100 μg/ml is not recommended. The lyophilized protein should be dissolved in ddH2O and the resulting solution should be aliquoted to minimize freeze-thaw cycles. It is essential to take care when handling the reconstituted solution to avoid compromising the integrity of the protein.

Target

Background

Interleukin 1 (IL-1) is a name that designates two proteins, IL-1αand IL-1β, which are the products of distinct genes, but which show approximately 25% amino acid (aa) sequence identity and which recognize the same cell surface receptors. IL-1αand IL-1β are both synthesized as 31 kDa precursors that are subsequently cleaved into proteins with molecular weights of approximately 17,000 Da. Neither precursor contains a typical hydrophobic signal peptide sequence and most of the precursor form of IL-1α remains in the cytosol of cells, although there is evidence for a membranebound form of the precursor form of IL-1α. Although IL-1 production is generally considered to be a consequence of inflammation, evidence suggests that IL-1 is also temporally upregulated during bone formation and the menstrual cycle and can be induced in response to nervous system stimulation. In response to classic stimuli produced by inflammatory agents, infections or microbial endotoxins, a dramatic increase in the production of IL-1 by macrophages and various other cells is seen.

Accession

P16598