Human Sialic Acid Binding Ig Like Lectin 7 (SIGLEC7) Protein

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Description
Recombinant Sialic Acid Binding Ig Like Lectin 7 (SIGLEC7) is a recombinant Human protein produced in a Prokaryotic expression system (E. coli).
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Product specifications
Category | Proteins and Peptides |
Immunogen Target | Sialic Acid Binding Ig Like Lectin 7 (SIGLEC7) |
Host | E. coli |
Origin | Human |
Conjugation | Unconjugated |
Observed MW | Molecular Weight: Calculated MW: 15.1 kDa Concentration: Prior to lyophilization: 200 µg/ml Sequence Fragment: Lys381-Lys467 Tag: N-terminal His tag |
Expression | Recombinant |
Purity | > 95% |
Size 1 | 10 µg |
Size 2 | 50 µg |
Size 3 | 100 µg |
Size 4 | 200 µg |
Size 5 | 500 µg |
Form | Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex. |
Tested Applications | WB, SDS-PAGE |
Buffer | Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300. |
Availability | Shipped within 5-12 working days. |
Storage | Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles. |
Dry Ice | No |
UniProt ID | Q9Y286 |
Alias | p75,QA79,AIRM1,CD328,AIRM-1,CDw328,D-siglec,SIGLEC-7,SIGLECP2,SIGLEC19P,p75/AIRM1,Adhesion inhibitory receptor molecule 1 |
Background | Protein SIGLEC7 |
Status | RUO |
Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
SIGLEC7, also known as p75/AIRM1, is an inhibitory receptor expressed on natural killer (NK) cells and some myeloid cells. It binds preferentially to α2-8-linked disialic acids found on both self and microbial surfaces, helping to suppress inappropriate immune activation. SIGLEC7 transmits inhibitory signals via immunoreceptor tyrosine-based inhibitory motifs (ITIMs), reducing NK cell-mediated cytotoxicity. This protein plays a critical role in maintaining self-tolerance and modulating responses to cancer and viral infections. It is frequently studied for its involvement in tumor immune evasion and as a target for immunotherapy.
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anti- SIGLEC7 antibody
Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3-and alpha-2,6-linked sialic acid. Also binds disialogangliosides(disialogalactosyl globoside, disialyl lactotetraosylceramide and disialyl GalNAc lactotetraoslylceramide). The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Mediates inhibition of natural killer cells cytotoxicity. May play a role in hemopoiesis. Inhibits differentiation of CD34+ cell precursors towards myelomonocytic cell lineage and proliferation of leukemic myeloid cells(in vitro).
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Sialic Acid Binding Ig Like Lectin 7 (SIGLEC7) Antibody
SIGLECs are cell surface proteins of the Ig superfamily. Most SIGLECs have 1 or more cytoplasmic immune receptor tyrosine-based inhibitory motifs, or ITIMs. A large subgroup of SIGLECs share high homology with SIGLEC3 (CD33) and are localized to 19q13.4. The cDNA for the SLG gene encodes 2 variants, SLG-long (SLGL) and SLG-short (SLGS). The 595-amino acid SLGL protein contains a signal peptide and 2 V-set N-terminal Ig-like domains. The 477-amino acid SLGS protein has a weak signal sequence and, like most SIGLEC3-like SIGLECs, has only 1 V-set N-terminal Ig-like domain. Both variants contain 2 C2-set N-terminal Ig-like domains, a transmembrane domain, and a cytoplasmic tail with a putative ITIM and a putative SLAM-like tyrosine-based motif. The conserved arginine residue thought to be essential for sialic acid binding in other SIGLECs is replaced by a glutamine in SLGS and by a cysteine in SLGL. RT-PCR analysis detected high expression of both variants in spleen and small intestine, and SLGS was highly expressed in adrenal gland and SLGL was highly expressed in bone marrow.
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Sialic Acid Binding Ig Like Lectin 7 (SIGLEC7) Antibody
SIGLECs are cell surface proteins of the Ig superfamily. Most SIGLECs have 1 or more cytoplasmic immune receptor tyrosine-based inhibitory motifs, or ITIMs. A large subgroup of SIGLECs share high homology with SIGLEC3 (CD33) and are localized to 19q13.4. The cDNA for the SLG gene encodes 2 variants, SLG-long (SLGL) and SLG-short (SLGS). The 595-amino acid SLGL protein contains a signal peptide and 2 V-set N-terminal Ig-like domains. The 477-amino acid SLGS protein has a weak signal sequence and, like most SIGLEC3-like SIGLECs, has only 1 V-set N-terminal Ig-like domain. Both variants contain 2 C2-set N-terminal Ig-like domains, a transmembrane domain, and a cytoplasmic tail with a putative ITIM and a putative SLAM-like tyrosine-based motif. The conserved arginine residue thought to be essential for sialic acid binding in other SIGLECs is replaced by a glutamine in SLGS and by a cysteine in SLGL. RT-PCR analysis detected high expression of both variants in spleen and small intestine, and SLGS was highly expressed in adrenal gland and SLGL was highly expressed in bone marrow.
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