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PE-Labeled Human Peptide Ready HLA-A*03:01&B2M Tetramer Protein 2220

$1,150.00$4,250.00

Summary

  • Expression: HEK293
  • Functional: Yes (ELISA)
  • Amino Acid Range: Gly25-Thr305(HLA-A*03:01) & Ile21-Met119(B2M)
SKU: 2220parent Categories: , Tag:
Weight 1 lbs
Dimensions 9 × 5 × 2 in
accession

NP_002107.3(HLA-A*03:01)&P61769(B2M)

express system

HEK293

product tag

C-His-Avi

purity

> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC

background

Peptide Ready HLA-A*03:01&B2M Tetramer is absent from peptide, namely peptide-receptive MHC. It can be loaded with antigenic peptides matching HLA-A*03:01. Peptide ready MHC molecules comprising human HLA alleles and B2M, which can be readily tetramerized and loaded with peptides of choice in a high-throughput manner.

molecular weight

0

available size

100 µg, 500 µg

endotoxin

Less than 1EU per μg by the LAL method.

PE-Labeled Human Peptide Ready HLA-A*03:01&B2M Tetramer Protein 2220

protein
Size and concentration
100, 500µg and liquid
Form
Liquid
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 with dry ice.
Purity
> 95% as determined by Tris-Bis PAGE
target relevance
Peptide Ready HLA-A*03:01&B2M Tetramer is absent from peptide, namely peptide-receptive MHC. It can be loaded with antigenic peptides matching HLA-A*03:01. Peptide ready MHC molecules comprising human HLA alleles and B2M, which can be readily tetramerized and loaded with peptides of choice in a high-throughput manner.
Protein names
Protein c-Fos (Cellular oncogene fos) (Fos proto-oncogene, AP-1 transcription factor subunit) (G0/G1 switch regulatory protein 7) (Proto-oncogene c-Fos) (Transcription factor AP-1 subunit c-Fos)
Gene names
FOS,FOS G0S7
Protein family
BZIP family, Fos subfamily
Mass
40695Da
Function
FUNCTION: Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. In the heterodimer, FOS and JUN/AP-1 basic regions each seems to interact with symmetrical DNA half sites. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation. In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum. {ECO:0000269|PubMed:16055710, ECO:0000269|PubMed:17160021, ECO:0000269|PubMed:22105363, ECO:0000269|PubMed:7588633, ECO:0000269|PubMed:9732876}.
Subellular location
SUBCELLULAR LOCATION: Nucleus. Endoplasmic reticulum. Cytoplasm, cytosol. Note=In quiescent cells, present in very small amounts in the cytosol. Following induction of cell growth, first localizes to the endoplasmic reticulum and only later to the nucleus. Localization at the endoplasmic reticulum requires dephosphorylation at Tyr-10 and Tyr-30.
Structure
SUBUNIT: Heterodimer; with JUN (By similarity). Component of the SMAD3/SMAD4/JUN/FOS complex required for synergistic TGF-beta-mediated transcription at the AP1 promoter site (PubMed:9732876). Interacts with SMAD3; the interaction is weak even on TGF-beta activation (PubMed:9732876). Interacts with MAFB (By similarity). Interacts with TSC22D3 (via N-terminus); this interaction inhibits the binding of active AP1 to its target DNA (By similarity). Interacts with CDS1 and PI4K2A (By similarity). Interacts (via bZIP domain and leucine-zipper region) with the multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF) subunits SMARCB1, SMARCC2 and SMARCD1 (By similarity). Interacts (via bZIP domain and leucine-zipper region) with ARID1A (By similarity). {ECO:0000250|UniProtKB:P01101, ECO:0000250|UniProtKB:P12841, ECO:0000269|PubMed:9732876}.
Post-translational modification
PTM: Phosphorylated in the C-terminal upon stimulation by nerve growth factor (NGF) and epidermal growth factor (EGF). Phosphorylated, in vitro, by MAPK and RSK1. Phosphorylation on both Ser-362 and Ser-374 by MAPK1/2 and RSK1/2 leads to protein stabilization with phosphorylation on Ser-374 being the major site for protein stabilization on NGF stimulation. Phosphorylation on Ser-362 and Ser-374 primes further phosphorylations on Thr-325 and Thr-331 through promoting docking of MAPK to the DEF domain. Phosphorylation on Thr-232, induced by HA-RAS, activates the transcriptional activity and antagonizes sumoylation. Phosphorylation on Ser-362 by RSK2 in osteoblasts contributes to osteoblast transformation (By similarity). {ECO:0000250}.; PTM: Constitutively sumoylated with SUMO1, SUMO2 and SUMO3. Desumoylated by SENP2. Sumoylation requires heterodimerization with JUN and is enhanced by mitogen stimulation. Sumoylation inhibits the AP-1 transcriptional activity and is, itself, inhibited by Ras-activated phosphorylation on Thr-232. {ECO:0000269|PubMed:16055710, ECO:0000269|PubMed:17709345}.; PTM: In quiescent cells, the small amount of FOS present is phosphorylated at Tyr-10 and Tyr-30 by SRC. This Tyr-phosphorylated form is cytosolic. In growing cells, dephosphorylated by PTPN2. Dephosphorylation leads to the association with endoplasmic reticulum membranes and activation of phospholipid synthesis. {ECO:0000269|PubMed:17160021, ECO:0000269|PubMed:22105363}.
Target Relevance information above includes information from UniProt accession: P01100
The UniProt Consortium

Data

ELISA with PE-Labeled Human Peptide Ready HLA-A*03:01&B2M Tetramer Prot
Immobilized PE-Labeled Human Peptide Ready HLA-A*03:01&B2M Tetramer, His Tag at 0.5µg/ml (100µl/Well) on the plate. Dose response curve for Anti-HLA class I (W6/32) Antibody, hFc Tag with the EC50 of 6.0ng/ml determined by ELISA.

Publications

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Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.

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