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Adipogen/UFM1 (human) (rec.) (His) (Rhodamine)/AG-40T-0531RH-C050/50 µg
来自 : 发布时间:2024-05-12
More Information Product Details Synonyms Product Type Properties Source/Host Sequence Crossreactivity Label/Conjugates Formulation Other Product Data Declaration Shipping and Handling Shipping Short Term Storage Long Term Storage Handling Advice Use/Stability Documents MSDS Product Specification Sheet Datasheet
Ubiquitin-fold Modifier 1; C13orf20
Protein
E. coli
Human UFM1 (Accession Nr. NP_057701) fused to a N-terminal His-tag and conjugated to Rhodamine.
Human
Rhodamine
Liquid. In 50mM Hepes pH 7.5, 100mM NaCl.
Use: Modified with rhodamine red via primary amine coupling, resulting in the modification of lysine residues as well as the N-terminus. This labeled Ufm1 allows for direct detection spectophotometrically with higher efficiency and sensitivity than with antibodies. Ideal for use in assays requiring fluorescent detection. Optimal fluorescence at pH 8.0 is monitored with an excitation wavelength of 570nM and an emission wavelength of 590nM. Reaction conditions will need to be optimized for each specific application. We recommend an initial protein concentration of 0.1-1µM.
Manufactured by Boston Biochem
DRY ICE
-20°C
-80°C
Aliquot to avoid freeze/thaw cycles.Protect from light.
Stable for at least 1 year after receipt when stored at -80°C.
No
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Ubiquitin-fold Modifier 1 (UFM1), also known as BM-002, is an 85 amino acid (aa) member of the ubiquitin-like protein family that has a predicted molecular weight of 9.1 kDa. Human and mouse UFM1 share 100% aa sequence identity and are primarily localized in the nucleus, but can also be detected in the cytoplasm and the endoplasmic reticulum (ER). ER localization of UFM1 appears to be dependent on the co-expression of UFBP1. Initially expressed as an inactive precursor, UFM1 undergoes proteolytic cleavage at the C-terminus to expose a conserved glycine residue that is necessary for UFM1 conjugation to target proteins. Conjugation of UFM1 to target proteins requires a UFM1-activating (E1) enzyme, a UFM1-conjugating (E2) enzyme and a UFM1 ligase (E3). UFM1 has been shown to be a mediator of ER stress-induced cancer and to promote the pathogenesis of Leishmania.

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发布于 : 2024-05-12 阅读()