Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | NP_004624 |
express system | HEK293 |
product tag | C-His |
purity | > 95% as determined by Tris-Bis PAGE;> 90% as determined by HPLC |
background | Interleukin (IL)-1 has been reported to be involved in the development of tuberculosis (TB). IL1R1 and IL1R2 encode a cytokine receptor that belongs to the IL-1 receptor family.IL1R2 (Interleukin 1 Receptor Type 2) is a Protein Coding gene. Diseases associated with IL1R2 include Endometriosis and Mastitis. Among its related pathways are Hematopoietic cell lineage and IL-1 signaling pathway. Gene Ontology (GO) annotations related to this gene include interleukin-1 receptor activity and interleukin-1, type II, blocking receptor activity. |
molecular weight | The protein has a predicted MW of 38.9 kDa. Due to glycosylation, the protein migrates to 55-65 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Human IL-1R2/IL-1 RII/CD121b Protein 4703
$210.00 – $700.00
Summary
- Expression: HEK293
- Functional: Yes (ELISA)
- Amino Acid Range: Phe14-Glu343
Human IL-1R2/IL-1 RII/CD121b Protein 4703
protein |
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Size and concentration 100, 500µg and lyophilized |
Form Lyophilized |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped at ambient temperature. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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Interleukin (IL)-1 has been reported to be involved in the development of tuberculosis (TB). IL1R1 and IL1R2 encode a cytokine receptor that belongs to the IL-1 receptor family.IL1R2 (Interleukin 1 Receptor Type 2) is a Protein Coding gene. Diseases associated with IL1R2 include Endometriosis and Mastitis. Among its related pathways are Hematopoietic cell lineage and IL-1 signaling pathway. Gene Ontology (GO) annotations related to this gene include interleukin-1 receptor activity and interleukin-1, type II, blocking receptor activity. |
Protein names GTPase KRas (EC 3.6.5.2) (K-Ras 2) (Ki-Ras) (c-K-ras) (c-Ki-ras) [Cleaved into: GTPase KRas, N-terminally processed] |
Gene names KRAS,KRAS KRAS2 RASK2 |
Protein family Small GTPase superfamily, Ras family |
Mass 21656Da |
Function FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (PubMed:20949621). Plays an important role in the regulation of cell proliferation (PubMed:22711838, PubMed:23698361). Plays a role in promoting oncogenic events by inducing transcriptional silencing of tumor suppressor genes (TSGs) in colorectal cancer (CRC) cells in a ZNF304-dependent manner (PubMed:24623306). {ECO:0000269|PubMed:20949621, ECO:0000269|PubMed:22711838, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:24623306, ECO:0000305}. |
Catalytic activity CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000269|PubMed:20949621}; |
Subellular location SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor {ECO:0000269|PubMed:29239724, ECO:0000305|PubMed:23698361}; Cytoplasmic side {ECO:0000305|PubMed:23698361}. Endomembrane system {ECO:0000269|PubMed:29239724}. Cytoplasm, cytosol {ECO:0000269|PubMed:23698361}.; SUBCELLULAR LOCATION: [Isoform 2B]: Cell membrane {ECO:0000269|PubMed:28619714}; Lipid-anchor {ECO:0000305|PubMed:28619714}. |
Structure SUBUNIT: Interacts with PHLPP (By similarity). Interacts (active GTP-bound form preferentially) with RGS14 (By similarity). Interacts (when farnesylated) with PDE6D; this promotes dissociation from the cell membrane (PubMed:23698361). Interacts with SOS1 (PubMed:22431598). Interacts (when farnesylated) with GPR31 (PubMed:28619714). Interacts with RAP1GDS1 (PubMed:20709748, PubMed:24415755). Interacts (active GTP-bound form) with both SHOC2 and PP1c (all isoforms) to form a tertiary complex; SHOC2 and PP1c preferably bind M-Ras/MRAS, but they also bind K-Ras/KRAS, N-Ras/NRAS and H-Ras/HRAS (PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). Interacts (GTP-bound form) with MAPKAP1/SIN1; inhibiting K-Ras/KRAS activity (PubMed:34380736, PubMed:35522713). {ECO:0000250|UniProtKB:P08644, ECO:0000269|PubMed:20709748, ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:24415755, ECO:0000269|PubMed:28619714, ECO:0000269|PubMed:34380736, ECO:0000269|PubMed:35522713, ECO:0000269|PubMed:35768504, ECO:0000269|PubMed:35830882, ECO:0000269|PubMed:35831509, ECO:0000269|PubMed:36175670}.; SUBUNIT: [Isoform 2B]: Interacts with GPR31; in a farnelysation-dependent manner. {ECO:0000269|PubMed:28619714}. |
Post-translational modification PTM: Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs). {ECO:0000269|PubMed:22711838, ECO:0000269|Ref.17}.; PTM: Palmitoylated at Lys-182, Lys-184 and Lys-185 (PubMed:29239724). Palmitoylation on lysine residues is promoted by palmitoylation at Cys-180 (PubMed:29239724). Lysine-depalmitoylation by SIRT2 promotes its localization to endomembranes in endocytic pathways (PubMed:29239724). {ECO:0000269|PubMed:29239724}.; PTM: Ubiquitinated by the BCR(LZTR1) E3 ubiquitin ligase complex at Lys-170 in a non-degradative manner, leading to inhibit Ras signaling by decreasing Ras association with membranes. {ECO:0000305|PubMed:30442762, ECO:0000305|PubMed:30442766}.; PTM: (Microbial infection) Glucosylated at Thr-35 by P.sordellii toxin TcsL. {ECO:0000269|PubMed:19744486}. |
Target Relevance information above includes information from UniProt accession: P01116 |
The UniProt Consortium |
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