Name :
Recombinant Human CD8 alpha Protein (ECD, His & AVI Tag), Biotinylated, HPLC-verified

Biological Activity :

Background :
T-cell surface glycoprotein CD8 alpha chain, also known as CD8a, is a single-pass type I membrane protein. The CD8 glycoprotein is expressed by thymocytes, mature T cells and natural killer (NK) cells and has been implicated in the recognition of monomorphic determinants on major histocompatibility complex (MHC) Class I antigens, and in signal transduction during the course of T-cell activation. Both human and rodent CD8 antigens are comprised of two distinct polypeptide chains, alpha and beta. The Ig domains of CD8 alpha are involved in controlling the ability of CD8 to be expressed. Mutation of B- and F-strand cysteine residues in CD8 alpha reduced the ability of the protein to fold properly and, therefore, to be expressed. Defects in CD8a are a cause of familial CD8 deficiency. Familial CD8 deficiency is a novel autosomal recessive immunologic defect characterized by absence of CD8+ cells, leading to recurrent bacterial infections.

Biological Activity :
Testing in progress

Expression Host :
Human

Source :
HEK293 Cells

Tag :

Protein Accession No. :
NP_001759.3

NCBI Gene ID :

Synonyms :

Synonyms :
CD8a molecule

Amino Acid Sequence :

Molecular Weight :
The recombinant Human CD8a consists of 187 amino acids and predicts a molecular mass of 20.87 kDa. It migrates as an approximately 29.7 kDa band in SDS-PAGE under reducing conditions.

Purity :
≥ 95 % as determined by SDS-PAGE. ≥ 95 % as determined by SEC-HPLC.

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 protein as determined by the LAL method.

Protein Construction :
A DNA sequence encoding the Human CD8a (NP_001759.3)(Met1-Asp182) was expressed with a C-terminal polyhistidine tag followed by an AVI tag. The expressed protein was biotinylated in vivo by the Biotin-Protein ligase (BirA enzyme) which is co-expressed.

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 :
CD8 Protein, Human; CD8 alpha Protein, Human; Leu-2 Protein, Human; Leu2 Protein, Human; MAL Protein, Human; p32 Protein, Human; p32 186910 Protein, Human CD8 alpha 背景信息 T-cell surface glycoprotein CD8 alpha chain, also known as CD8a, is a single-pass type I membrane protein. The CD8 glycoprotein is expressed by thymocytes, mature T cells and natural killer (NK) cells and has been implicated in the recognition of monomorphic determinants on major histocompatibility complex (MHC) Class I antigens, and in signal transduction during the course of T-cell activation. Both human and rodent CD8 antigens are comprised of two distinct polypeptide chains, alpha and beta. The Ig domains of CD8 alpha are involved in controlling the ability of CD8 to be expressed. Mutation of B- and F-strand cysteine residues in CD8 alpha reduced the ability of the protein to fold properly and, therefore, to be expressed. Defects in CD8a are a cause of familial CD8 deficiency. Familial CD8 deficiency is a novel autosomal recessive immunologic defect characterized by absence of CD8+ cells, leading to recurrent bacterial infections.

References & Citations :
References Devine, L. et al., 2000, J Immunol. 164 (2): 833-8. Arcaro, A. et al., 2000, J Immunol. 165 (4): 2068-76. Saha, K. et al., 2001, Nat Med. 7 (1): 65-72. Romero, P. et al., 2005, Eur J Immunol. 35 (11): 3092-4.

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