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首页 > 产品中心 > 重组蛋白 > 白细胞介素(Interleukins)及其受体 > Recombinant Human Interleukin-1 alpha Protein

Recombinant Human Interleukin-1 alpha Protein

rHuIL-1α
TDSSDS
价格:
询价
货号:
110101
数量:
-
+
img

技术参数

DESCRIPTION

Expression system

E. coli

Accession number

Ser113-Ala271, Accession #P01583

Amino acid sequence SAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAVKFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITGSETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILENQA
Molecular mass

Recombinant Human IL-1 alpha Protein, a monomer containing 159 amino acid residues, has a predicted molecular mass of approximately 18.1 kDa.

SPECIFICATIONS

Purity

> 98% by SDS-PAGE gel and HPLC analyses.

Endotoxin

Less than 0.1 EU/μg of rHuIL-1α as determined by LAL test.

Activity

The ED50 as determined by a cell proliferation assay using murine D10S cells is less than 1.0 pg/ml, corresponding to a specific activity of > 1.0 × 109 U/mg.

Formulation

Lyophilized from a 0.22 μm filtered solution in PBS. See CoA for details.

Reconstitution

Always centrifuge tubes before opening. Do not mix by vortex or pipetting. Reconstitute in sterile distilled water to a concentration of 0.1-1.0 mg/mL. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

SHIPPING & STORAGE

Shipping

The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.

Storage

Please use a manual defrost freezer and avoid repeated freeze-thaw cycles.

  • Lyophilized protein should be stored at ≤ -20°C, stable for 12 months after receipt.
  • Reconstituted protein solution can be stored at 2-8°C for 1 month.
  • Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.

BACKGROUND

Human IL‑1α is a vital pro‑inflammatory cytokine encoded by the IL1A gene, belonging to the IL‑1 superfamily and participating in immune reactions, inflammatory cascades and hematopoiesis. It can be recombinantly expressed in Escherichia coli. Predominantly secreted by monocytes, macrophages and dendritic cells, IL‑1α is initially synthesized as a precursor. Upon cellular injury, it undergoes proteolytic cleavage and release to trigger apoptosis, exerting effects via two shared receptors (IL‑1RI and IL‑1RII) also used by IL‑1β. As a pleiotropic mediator, IL‑1α activates NF‑κB and MAPK signaling cascades, upregulates IL‑6 and cyclooxygenase‑2 expression, and boosts nitric oxide production. Physiologically, it is enriched in barrier‑forming tissues including epidermal keratinocytes and pulmonary epithelial cells, acting as an alarm hormone to initiate local inflammation. Additionally, IL‑1α suppresses preadipocyte differentiation, lipid deposition and osteoblast maturation. Given its multifunctional biological roles, recombinant human IL‑1α is extensively applied in basic research. It serves as a key reagent for investigating inflammatory mechanisms, immune regulation, and establishing relevant disease models.

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