Human MIC-A protein (Recombinant) (C-His) (STJP000947)

SPECIFICATIONS
HostHEK293 cells
ConjugationUnconjugated
ImmunogenRecombinant Human MIC-A Protein is produced by HEK293 cells expression system. The target protein is expressed with sequence (Met1-Gln308) of human MICA (Accession #NP_000238.1) fused with a 6×His tag at the C-terminus.
STJP000947
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General Information

Short DescriptionRecombinant-Human MIC-A-C-His protein was developed in hek293 cells using the region Met1-Gln308. For use in research applications.
HostHEK293 cells
NoteSTRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.

Product Properties

ConjugationUnconjugated
FormulationLyophilised from a 0.22 Mu m filtered solution of PBS, pH 7.4.
Storage InstructionStore at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles.
ImmunoreactivityMeasured by its binding ability in a functional ELISA. Immobilized Human MICA Protein at 2 Mu g/mL (100 Mu L/well) can bind NKG2D with a linear range of 0.61-14.3 ng/mL.
Determination Method< 0.1 EU/Mu g of the protein by LAL method.

Target Information

Gene SymbolMICA
Gene ID100507436
Uniprot IDMICA_HUMAN
ImmunogenRecombinant Human MIC-A Protein is produced by HEK293 cells expression system. The target protein is expressed with sequence (Met1-Gln308) of human MICA (Accession #NP_000238.1) fused with a 6×His tag at the C-terminus.
Immunogen RegionMet1-Gln308
Immunogen SequenceMGLGPVFLLLAGIFPFAPPG AAAEPHSLRYNLTVLSWDGS VQSGFLTEVHLDGQPFLRCD RQKCRAKPQGQWAEDVLGNK TWDRETRDLTGNGKDLRMTL AHIKDQKEGLHSLQEIRVCE IHEDNSTRSSQHFYYDGELF LSQNLETKEWTMPQSSRAQT LAMNVRNFLKEDAMKTKTHY HAMHADCLQELRRYLKSGVV LRRTVPPMVNVTRSEASEGN ITVTCRASGFYPWNITLSW

Additional Info

Tissue Specificity Widely expressed with the exception of the central nervous system where it is absent. Expressed predominantly in gastric epithelium and also in monocytes, keratinocytes, endothelial cells, fibroblasts and in the outer layer of Hassal's corpuscles within the medulla of normal thymus. In skin, expressed mainly in the keratin layers, basal cells, ducts and follicles. Also expressed in many, but not all, epithelial tumors of lung, breast, kidney, ovary, prostate and colon. In thyomas, overexpressed in cortical and medullar epithelial cells. Tumors expressing MICA display increased levels of gamma delta T-cells.
Post Translational Modifications N-glycosylated. Glycosylation is not essential for interaction with KLRK1/NKG2D but enhances complex formation. Proteolytically cleaved and released from the cell surface of tumor cells which impairs KLRK1/NKG2D expression and T-cell activation. Palmitoylated on cysteine residues in the cytoplasmic tail leading to its association with membrane microdomains enriched in cholesterol. N-glycosylation is necessary for cell surface expression. (Microbial infection) Ubiquitinated by human herpesvirus 8 protein K5, leading to degradation.
Function Widely expressed membrane-bound protein which acts as a ligand to stimulate an activating receptor KLRK1/NKG2D, expressed on the surface of essentially all human natural killer (NK), gammadelta T and CD8 alphabeta T-cells. Up-regulated in stressed conditions, such as viral and bacterial infections or DNA damage response, serves as signal of cellular stress, and engagement of KLRK1/NKG2D by MICA triggers NK-cells resulting in a range of immune effector functions, such as cytotoxicity and cytokine production.
Protein Name Mhc Class I Polypeptide-Related Sequence A
Mic-A
Database Links Reactome: R-HSA-198933
Cellular Localisation Cell Membrane
Single-Pass Type I Membrane Protein
Cytoplasm
Expressed On The Cell Surface In Gastric Epithelium
Endothelial Cells And Fibroblasts And In The Cytoplasm In Keratinocytes And Monocytes
Infection With Human Adenovirus 5 Suppresses Cell Surface Expression Due To The Adenoviral E3-19k Protein Which Causes Retention In The Endoplasmic Reticulum
Alternative Protein Names Mhc Class I Polypeptide-Related Sequence A protein
Mic-A protein
MICA protein
PERB11.1 protein

Information sourced from Uniprot.org

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