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  6. IL-1 beta Protein, Human (Biotinylated, His-Avi)

IL-1 beta Protein, Human (Biotinylated, His-Avi)

Cat. No.: HY-P78143
COA Handling Instructions

IL-1 beta is a potent proinflammatory cytokine expressed by monocytes, macrophages, and dendritic cells. IL-1 beta plays a key role in inflammation and immunologic reactions.  IL-1 beta Protein, Human (Biotinylated, His-Avi), a Biotinylated  IL-1 beta protein, is produced in  E. coli with a C-Terminal His-tag and a C-Terminal Avi-tag. It consists of 153 amino acids (A117-S269).

For research use only. We do not sell to patients.

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20 μg $300 In-stock
50 μg $560 In-stock
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Description

IL-1 beta is a potent proinflammatory cytokine expressed by monocytes, macrophages, and dendritic cells. IL-1 beta plays a key role in inflammation and immunologic reactions[1][2]IL-1 beta Protein, Human (Biotinylated, His-Avi), a Biotinylated  IL-1 beta protein, is produced in  E. coli with a C-Terminal His-tag and a C-Terminal Avi-tag. It consists of 153 amino acids (A117-S269).

Background

Interleukin-1β (IL-1β) is one of the pro-inflammatory cytokines and is produced and secreted by a variety of cell types although the vast majority of studies have focussed on its production within cells of the innate immune system, such as monocytes and macrophages[1][2].
IL-1β is produced as inactive pro-IL-1β (encoded by pro-Il-1b) in response to inflammatory stimuli, including both microbial products and endogenous danger-associated molecules. IL-1β gene expression and synthesis of pro-IL-1β occurs after activation of pattern recognition receptors (PRRs). Inflammatory stimuli also drive activation of cytosolic CARD and PYHIN domain-containing PRRs that recruit ASC and caspase-1 (Casp-1) to assemble into the multiprotein complex inflammasome. Pro-Casp-1 (encoded by pro-Casp-1), activated by the inflammasome, cleaves pro-IL-1β into the bioactive IL-1β. IL-1β acts in an autocrine/paracrine manner via the type I IL-1 receptor (IL-1R1)[1][2][3].
IL-1β could regulate the inflammatory response, and is involved in a variety of cellular activities, including cell proliferation, differentiation, and apoptosis. IL-1β also plays a significant regulator of reproduction in females[1][2][3].

In Vitro

IL-1β (1-15625 pg/mL; 12 hours) dose-dependently increases production of the NF-κB-dependent inflammatory cytokine TNF-α, and a significant effect of IL-1β is observed at concentrations as low as 5 pg/mL in immortalized murine RAW264.7 macrophages[1].
IL-1β (1, 10 and 100 ng/mL; 24 hours) results in a dose-dependent increase of cell proliferation in pig heart cells. IL-1β increases the gene expression of caspase-3, and increases the enzymatic activities of MMP-2 and MMP-9[2].

In Vivo

IL-1β (8 ng; i.p.; daily; for 3 days) rescues Casp1−/− mice, restores survival and reduces lung bacterial load (i.e. days 0, 1, and 2 post-infection) in Chlamydia pneumoniae infected Casp1−/− mice. Yet, mice treated later (days 2, 3 and 4 post-infection) shows significantly increased bacterial counts relative to early-treated mice[3].

Biological Activity

1. Immobilized Human IL-1 RII hFc at 1 μg/mL (100 μL/Well) on the plate. Dose response curve for Biotinylated Human IL-1 Beta His with the EC50 of 9.7 ng/mL determined by ELISA.
2. Immobilized Human IL-1R2, hFc Tag at 0.5 μg/mL (100 μl/well) on the plate. Dose response curve for Biotinylated Human IL-1 Beta, His Tag with the EC50 of 7.3 ng/mL determined by ELISA.

Species

Human

Source

E. coli

Tag

C-Avi;C-His

Accession

P01584 (A117-S269)

Gene ID
Molecular Construction
N-term
IL-1β (A117-S269)
Accession # P01584
His-Avi
C-term
Synonyms
Interleukin-1 beta; IL-1 beta; IL1F2; IL1B; IL-1BETA; IL1F2; IL-1β; IL-1 beta; IL-1B ; Interleukin-1 β; IL-1 β; IL-1β; IL-1 β
AA Sequence

APVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKMEKRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS

Molecular Weight

Approximately 20.1 kDa

Purity

Greater than 95% as determined by Tris-Bis PAGE.

Appearance

Lyophilized powder.

Formulation

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4. Normally 5% trehalose is added as protectant before lyophilization.

Endotoxin Level

<1 EU/μg, determined by LAL method.

Reconstitution

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O.

Storage & Stability

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Shipping

Room temperature in continental US; may vary elsewhere.

Documentation
References
Help & FAQs
  • Do most proteins show cross-species activity?

    Species cross-reactivity must be investigated individually for each product. Many human cytokines will produce a nice response in mouse cell lines, and many mouse proteins will show activity on human cells. Other proteins may have a lower specific activity when used in the opposite species.

  • Reconstitution Calculator

  • Dilution Calculator

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The reconstitution calculator equation

Volume (to add to vial) = Mass (in vial) ÷ Desired Reconstitution Concentration

Volume (to add to vial) = Mass (in vial) ÷ Desired Reconstitution Concentration
= ÷

The dilution calculator equation

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)

This equation is commonly abbreviated as: C1V1 = C2V2

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
× = ×
C1   V1   C2   V2

The specific activity calculator equation

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)
Unit/mg = 106 ÷ ng/mL

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IL-1 beta Protein, Human (Biotinylated, His-Avi)
Cat. No.:
HY-P78143
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