Sialic Acid Binding Ig-Like Lectin 12 (SIGLEC12) Peptide
SIGLEC12
Reactivity: Human
Host: Synthetic
BP, WB
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- Target See all SIGLEC12 products
- SIGLEC12 (Sialic Acid Binding Ig-Like Lectin 12 (SIGLEC12))
- Origin
- Human
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Source
- Synthetic
- Application
- Blocking Peptide (BP), Western Blotting (WB)
- Characteristics
- This is a synthetic peptide designed for use in combination with anti-SIGLEC12 antibody (Catalog #: ARP50183_P050). It may block above mentioned antibody from binding to its target protein in western blot and/or immunohistochecmistry under proper experimental settings. There is no guarantee for its use in other applications.
- Purification
- Purified
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- Application Notes
- Each Investigator should determine their own optimal working dilution for specific applications.
- Restrictions
- For Research Use only
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- Format
- Lyophilized
- Reconstitution
- Add 100 μL of sterile PBS. Final peptide concentration is 1 mg/mL in PBS.
- Concentration
- 1 mg/mL
- Buffer
- Final peptide concentration is 1 mg/mL in PBS.
- Handling Advice
- Avoid repeated freeze-thaw cycles.
- Storage
- -20 °C
- Storage Comment
- For longer periods of storage, store at -20°C. Avoid repeat freeze-thaw cycles.
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- Target
- SIGLEC12 (Sialic Acid Binding Ig-Like Lectin 12 (SIGLEC12))
- Background
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Sialic acid-binding immunoglobulin-like lectins (SIGLECs) are a family of cell surface proteins belonging to the immunoglobulin superfamily. They mediate protein-carbohydrate interactions by selectively binding to different sialic acid moieties present on glycolipids and glycoproteins. SIGLEC12 is a member of the SIGLEC3-like subfamily of SIGLECs. SIGLEC12, upon tyrosine phosphorylation, has been shown to recruit the Src homology 2 domain-containing protein-tyrosine phosphatases SHP1 and SHP2. It has been suggested that the protein is involved in the negative regulation of macrophage signaling by functioning as an inhibitory receptor.Western blots using four different antibodies against four unique regions of this protein target confirm the same apparent molecular weight in our tests.Sialic acid-binding immunoglobulin-like lectins (SIGLECs) are a family of cell surface proteins belonging to the immunoglobulin superfamily. They mediate protein-carbohydrate interactions by selectively binding to different sialic acid moieties present on glycolipids and glycoproteins. This gene encodes a member of the SIGLEC3-like subfamily of SIGLECs. Members of this subfamily are characterized by an extracellular V-set immunoglobulin-like domain followed by two C2-set immunoglobulin-like domains, and the cytoplasmic tyrosine-based motifs ITIM and SLAM-like. The encoded protein, upon tyrosine phosphorylation, has been shown to recruit the Src homology 2 domain-containing protein-tyrosine phosphatases SHP1 and SHP2. It has been suggested that the protein is involved in the negative regulation of macrophage signaling by functioning as an inhibitory receptor. This gene is located in a cluster with other SIGLEC3-like genes on 19q13.4. Alternatively spliced transcript variants encoding distinct isoforms have been described for this gene.
Alias Symbols: FLJ38600, S2V, SIGLECL1, SLG, Siglec-12, Siglec-L1, Siglec-XII
Protein Interaction Partner: CMAS,PTPN11,PTPN6
Protein Size: 595 - Molecular Weight
- 63 kDa
- Gene ID
- 89858
- NCBI Accession
- NM_053003, NP_443729
- UniProt
- Q96PQ1
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