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Biotinylated Human HLA-G&B2M&Peptide (RIIPRHLQL) Monomer Protein 4336

$310.00$1,250.00

Summary

  • Expression: HEK293
  • Functional: Yes (ELISA)
  • Amino Acid Range: Gly25-Thr305(HLA-G),Ile21-Met119(B2M)and RIIPRHLQL peptide
SKU: 4336parent Categories: , Tag:
Weight1 lbs
Dimensions9 × 5 × 2 in
express system

HEK293

product tag

C-His-Avi

purity

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

background

HLA-G is a molecule that was first known to confer protection to the fetus from destruction by the immune system of its mother, thus critically contributing to fetal-maternal tolerance. The first functional finding constituted the basis for HLA-G research and can be summarized as such: HLA-G, membrane-bound or soluble, strongly binds its inhibitory receptors on immune cells (NK, T, B, monocytes/dendritic cells), inhibits the functions of these effectors, and so induces immune inhibition.

molecular weight

The protein has a predicted MW of 50.5 kDa. Due to glycosylation, the protein migrates to 51-60 kDa based on Tris-Bis PAGE result.

available size

100 µg, 500 µg

endotoxin

Less than 1EU per μg by the LAL method.

Biotinylated Human HLA-G&B2M&Peptide (RIIPRHLQL) Monomer Protein 4336

protein
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
HLA-G is a molecule that was first known to confer protection to the fetus from destruction by the immune system of its mother, thus critically contributing to fetal-maternal tolerance. The first functional finding constituted the basis for HLA-G research and can be summarized as such: HLA-G, membrane-bound or soluble, strongly binds its inhibitory receptors on immune cells (NK, T, B, monocytes/dendritic cells), inhibits the functions of these effectors, and so induces immune inhibition.
Protein names
HLA class I histocompatibility antigen, alpha chain G (HLA G antigen) (MHC class I antigen G) [Cleaved into: Soluble HLA class I histocompatibility antigen, alpha chain G (sHLA-G)]
Gene names
HLA-G,HLA-G HLA-6.0 HLAG
Protein family
MHC class I family
Mass
9606Da
Function
[Isoform 1]: Non-classical major histocompatibility class Ib molecule involved in immune regulatory processes at the maternal-fetal interface (PubMed:19304799, PubMed:23184984, PubMed:29262349). In complex with B2M/beta-2 microglobulin binds a limited repertoire of nonamer self-peptides derived from intracellular proteins including histones and ribosomal proteins (PubMed:7584149, PubMed:8805247). Peptide-bound HLA-G-B2M complex acts as a ligand for inhibitory/activating KIR2DL4, LILRB1 and LILRB2 receptors on uterine immune cells to promote fetal development while maintaining maternal-fetal tolerance (PubMed:16366734, PubMed:19304799, PubMed:20448110, PubMed:23184984, PubMed:27859042, PubMed:29262349). Upon interaction with KIR2DL4 and LILRB1 receptors on decidual NK cells, it triggers NK cell senescence-associated secretory phenotype as a molecular switch to promote vascular remodeling and fetal growth in early pregnancy (PubMed:16366734, PubMed:19304799, PubMed:23184984, PubMed:29262349). Through interaction with KIR2DL4 receptor on decidual macrophages induces pro-inflammatory cytokine production mainly associated with tissue remodeling (PubMed:19304799). Through interaction with LILRB2 receptor triggers differentiation of type 1 regulatory T cells and myeloid-derived suppressor cells, both of which actively maintain maternal-fetal tolerance (PubMed:20448110, PubMed:27859042). May play a role in balancing tolerance and antiviral-immunity at maternal-fetal interface by keeping in check the effector functions of NK, CD8+ T cells and B cells (PubMed:10190900, PubMed:11290782, PubMed:24453251). Reprograms B cells toward an immune suppressive phenotype via LILRB1 (PubMed:24453251). May induce immune activation/suppression via intercellular membrane transfer (trogocytosis), likely enabling interaction with KIR2DL4, which resides mostly in endosomes (PubMed:20179272, PubMed:26460007). Through interaction with the inhibitory receptor CD160 on endothelial cells may control angiogenesis in immune privileged sites (PubMed:16809620).; [Isoform 2]: Likely does not bind B2M and presents peptides. Negatively regulates NK cell- and CD8+ T cell-mediated cytotoxicity (PubMed:11290782).; [Isoform 3]: Likely does not bind B2M and presents peptides. Negatively regulates NK cell- and CD8+ T cell-mediated cytotoxicity (PubMed:11290782).; [Isoform 4]: Likely does not bind B2M and presents peptides. Negatively regulates NK cell- and CD8+ T cell-mediated cytotoxicity (PubMed:11290782).; [Isoform 5]: Non-classical major histocompatibility class Ib molecule involved in immune regulatory processes at the maternal-fetal interface (PubMed:19304799, PubMed:23184984, PubMed:29262349). In complex with B2M/beta-2 microglobulin binds a limited repertoire of nonamer self-peptides derived from intracellular proteins including histones and ribosomal proteins (PubMed:7584149, PubMed:8805247). Peptide-bound HLA-G-B2M complex acts as a ligand for inhibitory/activating KIR2DL4, LILRB1 and LILRB2 receptors on uterine immune cells to promote fetal development while maintaining maternal-fetal tolerance (PubMed:16366734, PubMed:19304799, PubMed:20448110, PubMed:23184984, PubMed:29262349). Upon interaction with KIR2DL4 and LILRB1 receptors on decidual NK cells, it triggers NK cell senescence-associated secretory phenotype as a molecular switch to promote vascular remodeling and fetal growth in early pregnancy (PubMed:16366734, PubMed:19304799, PubMed:23184984, PubMed:29262349). Through interaction with KIR2DL4 receptor on decidual macrophages induces pro-inflammatory cytokine production mainly associated with tissue remodeling (PubMed:19304799). Through interaction with LILRB2 receptor triggers differentiation of type 1 regulatory T cells and myeloid-derived suppressor cells, both of which actively maintain maternal-fetal tolerance (PubMed:20448110). Reprograms B cells toward an immune suppressive phenotype via LILRB1 (PubMed:24453251).; [Isoform 6]: Likely does not bind B2M and presents peptides.; [Isoform 7]: Likely does not bind B2M and presents peptides.
Subellular location
[Isoform 1]: Cell membrane ; Single-pass type I membrane protein. Endoplasmic reticulum membrane. Early endosome membrane .; [Soluble HLA class I histocompatibility antigen, alpha chain G]: Secreted .; [Isoform 2]: Cell membrane ; Single-pass type I membrane protein .; [Isoform 3]: Cell membrane ; Single-pass type I membrane protein .; [Isoform 4]: Cell membrane ; Single-pass type I membrane protein .; [Isoform 5]: Secreted. Early endosome .; [Isoform 6]: Secreted .; [Isoform 7]: Secreted .; Cell projection, filopodium membrane. Note=HLA-G trogocytosis from extravillous trophoblast's filopodia occurs in the majority of decidual NK cells.
Tissues
Expressed in adult eye (PubMed:1570318). Expressed in immune cell subsets including monocytes, myeloid and plasmacytoid dendritic cells and regulatory T cells (Tr1)(at protein level) (PubMed:20448110). Secreted by follicular dendritic cell and follicular helper T cells (PubMed:24453251).; [Isoform 5]: Detected in physiological fluids including amniotic fluid and serum.; [Isoform 7]: Expressed in placenta, amniotic membrane, skin, cord blood and peripheral blood mononuclear cells.
Structure
Forms a heterotrimer with B2M and a self-peptide (peptide-bound HLA-G-B2M) (PubMed:7584149, PubMed:8805247). HLA-G-B2M complex interacts with components of the antigen processing machinery TAPBP and TAP1-TAP2 complex; this interaction is required for loading of high affinity peptides and heterotrimer translocation to the cell surface (PubMed:7584149). Interacts with CALCR; this interaction is required for appropriate folding (PubMed:9640257). Interacts with COPB1; this interaction mediates the endoplasmic reticulum (ER) retrieval of HLA-G-B2M complexes that bind low affinity peptides (PubMed:11520457, PubMed:12582157). On the cell surface, peptide-bound HLA-G-B2M molecules (referred to as monomers) can form disulfide-linked homomultimers, homodimers and homotrimers (PubMed:12454284, PubMed:12874224, PubMed:16455647). Interacts with KIR2DL4; this interaction is direct (PubMed:10190900, PubMed:16366734). Interacts with LILRB1 and LILRB2 receptors; this interaction is direct (PubMed:12853576, PubMed:16366734, PubMed:16455647, PubMed:17056715). Interacts with CD160; this interactions is direct (PubMed:16809620). Interacts with CD8A homodimer; this interaction is direct and might down-regulate T cell receptor signaling (PubMed:12853576). Isoform 2: Forms a non-disulfide-linked homodimer and interacts with LILRB2 (PubMed:28348268).
Post-translational modification
N-glycosylated.; [Soluble HLA class I histocompatibility antigen, alpha chain G]: Produced by proteolytic cleavage at the cell surface (shedding) by matrix metalloproteinase MMP2.
Domain
Th
Target Relevance information above includes information from UniProt accession: P17693
The UniProt Consortium

Data

ELISA with Biotinylated Human HLA-G&B2M&Peptide (RIIPRHLQL) Monomer Pro
Immobilized Biotinylated Human HLA-G&B2M&Peptide (RIIPRHLQL) Monomer, His-Avi Tag at 1µg/ml (100µl/Well) on the streptavidin precoated plate (5µg/ml). Dose response curve for Anti-HLA-G Antibody, hFc Tag with the EC50 of 5.4ng/ml determined by ELISA.
HPLC of Biotinylated Human HLA-G&B2M&Peptide (RIIPRHLQL) Monomer Protei
The purity of Biotinylated Human HLA-G&B2M&Peptide (RIIPRHLQL) Monomer is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Biotinylated Human HLA-G&B2M&Peptide (RIIPRHLQL) Monome
Biotinylated Human HLA-G&B2M&Peptide (RIIPRHLQL) Monomer on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

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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