오늘본 상품

Product Name :
CymaxTM Mouse IL-1α ELISA Kit
Product Type :
Kits
Application(추가정보) :
sELISA
Reactivity :
Mouse
Storage :
All kit components of this kit are stable at 2 to 8°C. Any unused reconstituted standard should be discarded or frozen at -70°C. Standard can be frozen and thawed one time only without loss of immunoreactivity.
Sensitivity :
< 0.356 pg/ml
Sample Type :
Mouse serum, plasma, cell lysate, culture supernatants, buffered soltuion
Form :
Pre-coated plate
Detection range :
1.56~100 pg/ml
Background :
Interleukin-1 alpha (IL-1α) is a protein of the interleukin-1 family that in humans is encoded by the IL1A gene. In general, Interleukin 1 is responsible for the production of inflammation, as well as the promotion of fever and sepsis. IL-1α inhibitors are being developed to interrupt those processes and treat diseases. IL-1α is produced mainly by activated macrophages, as well as neutrophils, epithelial cells, and endothelial cells. It possesses metabolic, physiological, haematopoietic activities, and plays one of the central roles in the regulation of the immune responses. It binds to the interleukin-1 receptor. It is on the pathway that activates tumor necrosis factor-alpha. IL-1α is a cytokine of the interleukin-1 family. IL-1α is a unique member in the cytokine family in the sense that the structure of its initially synthesized precursor does not contain a signal peptide fragment (same is known for IL-1β and IL-18). After processing by the removal of N-terminal amino acids by specific proteases, the resulting peptide is called "mature" form. Calpain, a calcium-activated cysteine protease, associated with the plasma membrane, is primarily responsible for the cleavage of the IL-1α precursor into a mature molecule. Both the 31kDa precursor form of IL-1α and its 18kDa mature form are biologically active. The 31 kDa IL-1α precursor is synthesized in association with cytoskeletal structures (micro-tubules), unlike most proteins, which are translated in the endoplasmic reticulum. The three-dimensional structure of the IL-1α contains an open-ended barrel composed entirely of beta-pleated strands. Crystal structure analysis of the mature form of IL-1α shows that it has two sites of binding to IL-1 receptor. There is a primary binding site located at the open top of its barrel, which is similar but not identical to that of IL-1β.
Background reference :
1) Nicklin MJ, Weith A, Duff GW (Jun 1994). "A physical map of the region encompassing the human interleukin-1 alpha, interleukin-1 beta, and interleukin-1 receptor antagonist genes". Genomics 19 (2): 382–4.
2) March CJ, Mosley B, Larsen A, Cerretti DP, Braedt G, Price V, Gillis S, Henney CS, Kronheim SR, Grabstein K, et al. (Aug 1985). "Cloning, sequence and expression of two distinct human interleukin-1 complementary DNAs". Nature 315 (6021): 641–7
3) Bankers-Fulbright JL, Kalli KR, McKean DJ (1996). "Interleukin-1 signal transduction". Life Sci. 59 (2): 61–83.
4) Dinarello CA (June 1997). "Induction of interleukin-1 and interleukin-1 receptor antagonist". Semin. Oncol. 24 (3 Suppl 9): S9–81–S9–93.
5) Gery I, Gershon RK, Waksman BH (July 1972). "Potentiation of the T-lymphocyte response to mitogens. I. The responding cell". J. Exp. Med. 136 (1): 128–42.
Research area :
Cytokine 
Database link - SwissProt no.
P01582