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Merck
CN

11457756001

Roche

Interleukin-1β, human (hIL-1β)

recombinant (E. coli)

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UNSPSC Code:
12352207
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biological source

human

recombinant

expressed in E. coli

assay

>95% (HPLC)

form

solution

potency

≤0.02 ng/mL EC50

mol wt

17,000 Da

packaging

pkg of 100,000 U (2 μg, 1 ml)

manufacturer/tradename

Roche

storage condition

avoid repeated freeze/thaw cycles

impurities

<0.1 EU/μgtested (LAL test)

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... IL1B(3553)

General description

Recombinant Interleukin-1β, human (hIL-1β) is produced in E. coli and purified by standard chromatographic techniques.

Contents
100,000 U/ml (2 μg/ml) in PBS (phosphate buffered saline) and 1 mg/ml BSA (bovine serum albumin), [purity of BSA: >98%, endotoxin (LAL): <1 EU/mg BSA], filtered through 0.2 μm pore size membrane.

Application

Interleukin-1 (IL-1), secreted by activated monocytes or macrophages and other cell types, is a pleiotropic factor for a variety of sensitive cells.

Biochem/physiol Actions

Recombinant IL-1β, human is effective on mouse and human cells. Interleukin-1 (IL-1) is produced by a number of cell types, including activated macrophages, B-cells, fibroblasts, and keratinocytes. It mediates a wide range of biological activities, such as stimulation of thymocyte proliferation via induction of interleukin-2 (IL-2) release, stimulation of B-lymphocyte maturation and proliferation, fibroblast growth factor activity, and induction of acute-phase protein synthesis by hepatocytes. IL-1 has also been reported to stimulate prostaglandin and collagenase release from synovial cells, and to be identical to endogenous pyrogen and catabolin.
Two types of human interleukin-1 (hIL-1α and hIL-1β) have been described.
Both types of hIL-1 stimulate proliferation and differentiation of T- and B-lymphocytes. Recently, it has been shown that two different high-affinity IL-1 receptor molecules exist on different cell types. In both, human and mouse, T-cells and fibroblasts express an 80 kDa receptor molecule, whereas an 60 kDa receptor molecule was found on B-cells and neutrophils. The action of hIL-1a and hIL-1β is mediated by both receptor molecules. IL-1 appears to have a wide range of stimulatory effects on the maturation, differentiation, and growth of many cell types involved in inflammation and development. Cells whose growth is directly or indirectly stimulated by IL-1 are fibroblasts, synovial cells, endothelial cells, epithelial cells, bone marrow cells, T-lymphocytes, and B-lymphocytes.

Preparation Note

Working concentration: 5-500 U/ml
hIL-1β exerts its biological activity in the concentration range of 5–500 U/mI (0.1–1 ng/ml).
Working solution: Dilute the concentrated IL-1β solution (100,000 U/ml) with PBS or culture medium containing 1 mg/ml BSA [or HSA (human serum albumin)] or 1 –10% serum.
Storage conditions (working solution): -15 to -25 °C
Store the solution in aliquots at -15 to -25 °C.
Note: Avoid repeated freezing and thawing.

Other Notes

For life science research only. Not for use in diagnostic procedures.
One polypeptide chain (154 amino acids), identical to natural human IL-1β (153 amino acids), but with an extra methionine at the amino-terminus.
Chain Length 154 AA
EC50 definition: The amount of hIL-1β that is required to support half-maximal stimulation of DNA synthesis (BrdU incorporation) with mouse C3H/HeJ thymocytes in the presence of saturating amounts of hIL-2 (50 U/ml, 25 ng/ml) (1 unit equals ≤0.02 ng).

存储类别

12 - Non Combustible Liquids

wgk

nwg

flash_point_f

No data available

flash_point_c

No data available

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Biomedical reports, 13(1), 55-60 (2020-05-23)
The production of pro-inflammatory cytokines and chemokines is increased during inflammatory bowel disease (IBD). Previously, it was demonstrated that brain derived neurotrophic factor (BDNF) expression is increased in experimental models of colitis. BDNF is partially responsible for the structural and
Poole S. &amp; Gaines Das R.E
Journal of Immunological Methods, 142, 1-13 (1991)
Allison AC
Bioessays, 3 (1986)
Remvig L,et al.
Allergy, 46, 59-67 null
March CJ, et al.
Nature, 315, 641-647 null

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