Human IFN gamma Receptor beta protein fragment (ab83988)
- Product nameHuman IFN gamma Receptor beta protein fragmentSee all IFN gamma Receptor beta proteins and peptides ...
- SourceHEK 293 cells
- Amino Acid Sequence
- SequenceTheoretical sequence: SQLPAPQHPKIRLYNAEQVLSWEPVALSNSTRPVVYRV QFKYTDSKWF TADIMSIGVNCTQITATECDFTAASPSA GFPMDFNVTLRLRAELGALH SAWVTMPWFQHYRNVTVG PPENIEVTPGEGSLIIRFSSPFDIADTSTA FFCYYVHY WEKGGIQQVKGPFRSNSISLDNLKPSRVYCLQVQAQLLWN KSNIFRVGHLSNISCYETMADASTELQQGSSNTKVDKK VEPKSCDKTH TCPPCPAPELLGGPSVFLFPPKPKDTLM ISRTPEVTCVVVDVSHEDPE VKFNWYVDGVEVHNAKTK PREEQYNSTYRVVSVLTVLHQDWLNGKEYK CKVSNKAL PAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCL VKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFL YSKLTVDKSR WQQGNVFSCSVMHEALHNHYTQKSLSLS PGK
- Amino acids28 to 247
Our Abpromise guarantee covers the use of ab83988 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
- Purity> 95
% by SDS-PAGE.
- Concentration information loading...
Preparation and Storage
- Stability and Storage
Store at +4°C.
Constituents: 10% Trehalose, 1% Human serum albumin
- ReconstitutionIt is recommended that 0.5 ml of sterile phosphate-buffered saline be added to the vial. Following reconstitution short-term storage at 4°C is recommended, and longer-term storage of aliquots at -18 to -20°C. Repeated freeze thawing is not recommended.
- AF 1
- IFGR 2
- IFN-gamma receptor 2
- IFNGR 2
- IFNGT 1
- Interferon gamma receptor 2
- Interferon gamma receptor accessory factor 1
- Interferon gamma receptor beta chain
- Interferon gamma receptor chain 2
- Interferon gamma transducer 1
- FunctionPart of the receptor for interferon gamma. Required for signal transduction. This accessory factor is an integral part of the IFN-gamma signal transduction pathway and is likely to interact with GAF, JAK1, and/or JAK2.
- Involvement in diseaseDefects in IFNGR2 are a cause of mendelian susceptibility to mycobacterial disease (MSMD) [MIM:209950]; also known as familial disseminated atypical mycobacterial infection. This rare condition confers predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine and environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections, with the exception of Salmonella which infects less than 50% of these individuals. The pathogenic mechanism underlying MSMD is the impairment of interferon-gamma mediated immunity, whose severity determines the clinical outcome. Some patients die of overwhelming mycobacterial disease with lepromatous-like lesions in early childhood, whereas others develop, later in life, disseminated but curable infections with tuberculoid granulomas. MSMD is a genetically heterogeneous disease with autosomal recessive, autosomal dominant or X-linked inheritance.
- Sequence similaritiesBelongs to the type II cytokine receptor family.
Contains 2 fibronectin type-III domains.
- Cellular localizationMembrane.
Human IFN gamma Receptor beta protein fragment images
Lane 1 – ab83988; Lane 2 – ab83988 treated with PNGase F to remove potential N-linked glycans; Lane 3 – ab83988 treated with a glycosidase cocktail to remove potential N- and O-linked glycans; Lane 4 – MW markers. 10 µg of protein was loaded per lane; Gel was stained with Coomassie G250.
Drop in MW after treatment with PNGase F indicates the presence of N-linked glycans. Faint bands in lane 2 and lane 3 are glycosidase enzymes.
Post-translational modifications result in protein heterogeneity. The densitometry scan demonstrates the purified human cell expressed protein exists in multiple glycoforms, which differ according to their level of post-translational modification.
The triangle indicates theoretical pI and MW of the protein.
References for Human IFN gamma Receptor beta protein fragment (ab83988)
ab83988 has not yet been referenced specifically in any publications.