IL-1a/IL-1F1 was detected in immersion fixed human peripheral blood mononuclear cells (PBMCs) stimulated with LPS and monensin using Human IL-1a/IL-1F1 Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog ...read more
IL-1a/IL-1F1 was detected in immersion fixed human peripheral blood mononuclear cells (PBMCs) stimulated with LPS and monensin using Human IL-1a/IL-1F1 Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog ...read more
E. coli-derived recombinant human IL-1 alpha /IL-1F1 (R&D Systems, Catalog # 200-LA) Ser113-Ala271 Accession # Q53QF9
Specificity
Detects human IL-1 alpha /IL-1F1 in ELISAs and Western blots. In sandwich immunoassays, less than 0.05% cross-reactivity with recombinant mouse IL‑1 alpha , recombinant porcine IL‑1 alpha , recombinant rat IL‑1 alpha , recombinant human (rh) IL-1 sRI, and rhIL-1 sRII is observed.
Source
N/A
Isotype
IgG
Clonality
Polyclonal
Host
Goat
Gene
IL1A
Purity Statement
Antigen Affinity-purified
Innovator's Reward
Test in a species/application not listed above to receive a full credit towards a future purchase.
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Preservative
No Preservative
Concentration
LYOPH
Reconstitution Instructions
Reconstitute at 0.2 mg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for IL-1 alpha/IL-1F1 Antibody [Biotin]
BAF
Hematopoietin-1
IL1 alpha
IL-1 alpha
IL1
IL1A
IL-1A
IL1-ALPHA
IL1F1
IL-1F1
IL1F1hematopoietin-1
interleukin 1, alpha
interleukin-1 alpha
LAF
LEM
preinterleukin 1 alpha
pro-interleukin-1-alpha
Background
Interleukin 1 (IL-1) is a name that designates two proteins, IL-1 alpha and IL-1 beta , which are the products of distinct genes, but which show approximately 25% amino acid sequence identity and which recognize the same cell surface receptors. Although IL-1 production is generally considered to be a consequence of inflammation, recent evidence suggests that IL-1 is also temporarily 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. Cells in particular known to produce IL-1 include osteoblasts, monocytes, macrophages, keratinocytes, Kupffer cells, hepatocytes, thymic and salivary gland epithelium, Schwann cells, fibroblasts, and glia (oligodendroglia, astrocytes, and microglia).
IL-1 alpha and IL-1 beta 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-1 alpha remains in the cytosol of cells, although there is evidence for a membrane-bound form of the precursor form of IL-1 alpha . The IL-1 alpha precursor reportedly shows full biological activity in the EL-4 assay. Among various species, the amino acid sequence of mature IL-1 alpha is conserved 60% to 70% and human IL-1 has been found to be biologically active on murine cell lines. Both forms of IL-1 bind to the same receptors, designated type I and type II. Evidence suggests that only the type I receptor is capable of signal transduction and that the type II receptor may function as a decoy, binding IL-1 and thus preventing binding of IL-1 to the type I receptor.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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