Recombinant Human IL-1 beta Protein, HEK293

Référence 230-30051-250

Conditionnement : 250ug

Marque : RayBiotech

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Recombinant Human IL-1 beta Protein, HEK293

Recombinant Human IL-1 beta, derived from the transfected human HEK293 cells.
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Product Description

Specifications

Size10 µg, 50 µg, 100 µg, 250 µg
SpeciesHuman
Accession Number
P01584
Gene Id
3553
Gene Symbols
IL1B, IL1F2
Protein Name / Synonyms
Interleukin-1 beta (IL-1 beta) (Catabolin), Interleukin-1 beta, IL-1 beta, Catabolin, Interleukin 1 Beta, IL1F2, Pro-Interleukin-1-Beta, Preinterleukin 1 Beta, IL1-BETA, IL-1
Expressed Region
Ala117-Ser269
Expression SystemHEK293 cells
TagN-terminal histidine tag
Purity
>95%
Purity Determined BySDS-PAGE under reducing conditions and visualized by Coomassie blue staining
Molecular Weight (kDa)
Recombinant protein has a calculated molecular weight of about 17 kDa. Due to the post-translation modifications, it migrates as approximately 25 kDa protein band in SDS-PAGE under DTT, beta-mercaptoethanol reducing conditions.
Format
Lyophilized powder
Formulation
Lyophilized from a 0.2 µm filtered solution in PBS
Concentration (lot specific)
Determined by Pierce BCA protein assay kit
Preservative
None
Reconstitution
Briefly spin the vial and bring the contents to the bottom prior to opening. It is recommended to reconstitute at 0.5 - 1 mg/mL with sterile deionized water.
Endotoxin LevelNot determined
Research AreaAngiogenesis, Inflammation
Shipping TypeAmbient temperature
Storage-20°C

Introduction

Interleukin-1 Beta (IL-1β) is a pro-inflammatory cytokine predominantly produced by activated macrophages. It plays a pivotal role in mediating immune and inflammatory responses by inducing the expression of various genes involved in inflammation, immunity, and hematopoiesis. IL-1β is synthesized as an inactive precursor and requires cleavage by caspase-1 to become active. Dysregulation of IL-1β production or signaling is associated with various pathological conditions, including autoimmune diseases, chronic inflammatory diseases, and sepsis.

Reference: https://pubmed.ncbi.nlm.nih.gov/8630372/

SDS-PAGE Image
SDS-PAGE
Figure 1. Deglycosylation of purified recombinant proteins. Purified proteins were untreated (Lane 2) or treated with protein deglycosylation enzymes under native (Lane 3) or reducing (Lane 4) conditions. Deglycosylation treatment resulted in a mobility shift of the protein to produce one major band at the expected size, thus indicating that the untreated recombinant protein (Lane 2) was glycosylated.
Lane 1: Protein standard ladder (kDa).
Lane 2: Untreated protein under reducing conditions.
Lane 3: Treated protein with deglycosylation enzymes under native conditions.
Lane 4: Treated protein with deglycosylation enzymes under reducing conditions.
Lane 5: Deglycosylation mixture only without target proteins.
Activity
Stimulating cell growth significantly. Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The EC50 for this effect is 5.8 ng/mL.
Storage/Stability
Upon arrival, the lyophilized protein may be stored for 2 weeks at 4°C. For long term storage, it is recommended to store desiccated below -20°C in a manual defrost freezer. Following reconstitution, the protein may be stored for 2 weeks under sterile conditions at -20°C. For long term storage, it is recommended to make appropriate aliquots and store at -80°C. Avoid repeated freeze-thaw cycles.

Custom Labeling Request

We can custom label this protein with biotin or fluorescent dyes (choose from violet, blue, green or red). Request now.

citations

  • Transcriptional activation of hepcidin by the microphthalmia/transcription factor E family

    Year:
    2022
    Journal Name:
    Cell Biochemistry and Function

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