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IL1A Protein (AA 115-270)

This Recombinant IL1A protein is produced in Escherichia coli (E. coli).
Catalog No. ABIN2667484

Quick Overview for IL1A Protein (AA 115-270) (ABIN2667484)

Target

See all IL1A Proteins
IL1A (Interleukin 1 alpha (IL1A))

Protein Type

Recombinant

Biological Activity

Active

Origin

  • 25
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  • 3
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  • 1
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Mouse

Source

  • 44
  • 13
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  • 2
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  • 1
Escherichia coli (E. coli)

Application

Flow Cytometry (FACS)

Purity

Purity is >98 % , as determined by Coomassie stained SDS-PAGE.
  • Protein Characteristics

    AA 115-270

    Sterility

    0.22 μm filtered

    Endotoxin Level

    Endotoxin level is <0.1 EU/μg (<0.01ng/μg) protein as determined by the LAL method.

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  • Application Notes

    Optimal working dilution should be determined by the investigator.

    Comment

    Biological activity: ED50 =1- 5 pg/ml, corresponding to a specific activity of 1- 0.2 x 109 units/mg, as determined by the dose dependent stimulation of D10S cells proliferation

    Restrictions

    For Research Use only
  • Format

    Liquid

    Reconstitution

    For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored from -20 °C to -70 °C. Stock solutions can also be prepared at 50-100 μg/mL in sterile buffer (PBS, HPBS, DPBS, or EBSS) containing carrier protein such as 0.2-1 % BSA or HSA and stored in working aliquots at -20 °C to -70 °C.

    Buffer

    0.22 μm filtered protein solution is in 10 mM NaH2PO4, 150 mM NaCl, pH 7.2.

    Handling Advice

    Avoid repeated freeze/thaw cycles.

    Storage

    -20 °C

    Storage Comment

    Unopened vial can be stored between 2°C and 8°C for one month, at -20°C for six months, or at -70°C for one year.
  • Target

    IL1A (Interleukin 1 alpha (IL1A))

    Alternative Name

    IL-1alpha

    Background

    IL-1 was isolated from human blood that had been exposed to a pathogenic bacterium. IL-1 is a pyrogen, and it is an activating factor for lymphocytes. It also damaged joints and influenced liver proteins (3). IL-1α binds to the cell surface type I and II IL-1 receptors (IL-1RI and IL-1RII). IL-1 and -β and IL-1RA can compete for binding to these receptors. However, only IL-1RI, not IL-1RII, is functional because IL-1RII lacks a cytoplasmic domain and is thus unable to transmit signals to downstream steps (4). During ovarian inflammatory response, proinflammatory cytokine production such as IL-1 is augmented in granulosa cells and can induce local chemokine synthesis, which in turn may affect ovarian function (1). Also, IL-1 is involved in regulating tissue chemokine expression and leukocyte accumulation. The abundant influx of leukocytes into the ovary varies with the stage of the cycle and the leukocytes are thought to have a central role in influencing follicular atresia, ovulation, and luteal function and are potentially involved in ovarian disorders such as premature ovarian failure and polycystic ovary syndrome (1). IL-1a induces CXCl1 RNA and protein in mouse granulose cells.

    Molecular Weight

    The 156 amino acid recombinant protein has a predicted molecular mass of 17,990 Da. The DTT-reduced and the non-reduced protein migrate at approximately 18kDa by SDS-PAGE. The N-terminal amino acid is Serine.

    Pathways

    NF-kappaB Signaling, Autophagy, Cancer Immune Checkpoints
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