Name :
Recombinant Human MICB Protein (His & hFc Tag)
Biological Activity :
Background :
MHC class I polypeptide-related sequence B, also known as MICB, is a heavily glycosylated protein serving as a ligand for the type II receptor NKG2D. MICB shares 85% amino acid identity with MICA, a closely related protein, both of which contain three extracellular immunoglobulin-like domains, but without the capacity to bind peptide or interact with beta-2-microglobulin. acting as a stress-induced self-antigen, binding of MICB to the NKG2D receptor activates the cytolytic response of natural killer (NK) cells, CD8+αβ T cells, and γδ T cells on which the receptor is expressed. MICA/B is minimally expressed on normal cells, but are frequently expressed on epithelial tumors and can be induced by bacterial and viral infections. MICA/B recognition thus is involved in tumor surveillance, viral infections, and autoimmune diseases.
Biological Activity :
Immobilized human His-NKG2D (78-216) (Cat:10575-H07B) at 10 μg/ml (100 μl/well) can bind human MICB-Fch, The EC50 of human MICB-Fch is 15.9-37.1 ng/ml.
Expression Host :
Human
Source :
HEK293 Cells
Tag :
Protein Accession No. :
NP_005922.2
NCBI Gene ID :
Synonyms :
Synonyms :
MHC class I polypeptide-related sequence B
Amino Acid Sequence :
Molecular Weight :
The recombinant human MICB/Fc is a disulfide-linked homodimer. The reduced monomer consists of 524 amino acids and has a predicted molecular mass of 59.5 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rh MICB/Fc monomer is approximately 80-90 kDa due to glycosylation.
Purity :
> 98 % as determined by SDS-PAGE
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
< 1.0 EU per μg of the protein as determined by the LAL method
Protein Construction :
A DNA sequence encoding the extracellular domain of human MICB (NP_005922.2) (Met 1-Gly 298) was fused with the C-terminal polyhistidine-tagged Fc region of human IgG1 at the C-terminus.
Buffer Solution :
Lyophilized from sterile PBS, pH 7.4.Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
PERB11.2 Protein, Human MICB 背景信息 MHC class I polypeptide-related sequence B, also known as MICB, is a heavily glycosylated protein serving as a ligand for the type II receptor NKG2D. MICB shares 85% amino acid identity with MICA, a closely related protein, both of which contain three extracellular immunoglobulin-like domains, but without the capacity to bind peptide or interact with beta-2-microglobulin. acting as a stress-induced self-antigen, binding of MICB to the NKG2D receptor activates the cytolytic response of natural killer (NK) cells, CD8+αβ T cells, and γδ T cells on which the receptor is expressed. MICA/B is minimally expressed on normal cells, but are frequently expressed on epithelial tumors and can be induced by bacterial and viral infections. MICA/B recognition thus is involved in tumor surveillance, viral infections, and autoimmune diseases.
References & Citations :
Bauer, S. et al., 1999, Science. 285:727-729. Braud, V.M. et al., 1999, Curr. Opin. Immunol. 11: 100-108. Groh, V. et al., 2001, Nature Immunol. 2: 255-260. Stephens, H., 2001, Trends Immunol. 22: 378-385. Borrego, F. et al., 2002, Mol. Immunol. 38: 637–660. Groh, V. et al., 2002, Nature. 419:734-738.
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