癌症的基本特征包括细胞增殖、血管生成、迁移、凋亡逃避机制和细胞永生等。找到癌症发生过程中这些通路的关键标记物和对应的抗体用于检测至关重要。
为您推荐一个泛素化位点预测神器——泛素化分析工具，可以为您的蛋白的泛素化位点作出预测和评分。
细胞自噬受体图形绘图工具为你的蛋白的细胞受体结合位点作出预测和评分，识别结合到自噬通路中的蛋白是非常重要的，便于让我们理解自噬在正常生理、病理过程中的作用，如发育、细胞分化、神经退化性疾病、压力条件下、感染和癌症。
SIGLEC7 (D-siglec) Antibody (N-term)
Purified Rabbit Polyclonal Antibody (Pab)
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- 实验流程
- 背景知识
Application 
| WB, IHC-P, E |
|---|---|
| Primary Accession | Q9Y286 |
| Other Accession | Q9NZQ1 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 51143 Da |
| Antigen Region | 1-30 aa |
| Gene ID | 27036 |
|---|---|
| Other Names | Sialic acid-binding Ig-like lectin 7, Siglec-7, Adhesion inhibitory receptor molecule 1, AIRM-1, CDw328, D-siglec, QA79 membrane protein, p75, CD328, SIGLEC7, AIRM1 |
| Target/Specificity | This SIGLEC7 (D-siglec) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human SIGLEC7 (D-siglec). |
| Dilution | WB~~1:1000 IHC-P~~1:100~500 E~~Use at an assay dependent concentration. |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | SIGLEC7 (D-siglec) Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | SIGLEC7 |
|---|---|
| Synonyms | AIRM1 |
| Function | 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). |
| Cellular Location | Membrane; Single-pass type I membrane protein. |
| Tissue Location | Predominantly expressed by resting and activated natural killer cells and at lower levels by granulocytes and monocytes High expression found in placenta, liver, lung, spleen, and peripheral blood leukocytes |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
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.
REFERENCES
Nicoll, G., et al., Eur. J. Immunol. 33(6):1642-1648 (2003).
Alphey, M.S., et al., J. Biol. Chem. 278(5):3372-3377 (2003).
Angata, T., et al., Glycobiology 10(4):431-438 (2000).
Falco, M., et al., J. Exp. Med. 190(6):793-802 (1999).
Nicoll, G., et al., J. Biol. Chem. 274(48):34089-34095 (1999).
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