Recombinant Human Syndecan-1 Fc Chimera Avi-tag Protein, CF
Recombinant Human Syndecan-1 Fc Chimera Avi-tag Protein, CF Summary
Learn more about Avi-tag Biotinylated ProteinsProduct Specifications
Human Syndecan-1 (Gln18-Gln251) Accession # AAH08765.1 | IEGRMD | Human IgG1 Fc (Pro100-Lys330) | Avi-tag |
N-terminus | C-terminus | ||
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
AVI10913
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution | Reconstitute at 500 μg/mL in PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
In a functional ELISA, Biotinylated Recombinant Human Syndecan-1/CD138 Fc Chimera Avi-tag (Catalog # AVI10913) binds to Human Syndecan-1/CD138 Antibody (Catalog # MAB2780) with an ED50 of 0.400-5.00 ng/mL.
2 μg/lane of Biotinylated Recombinant Human Syndecan‑1/CD138 Fc Chimera Avi-tag Protein (Catalog # AVI10913) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 81-105 kDa and 160-210 kDa, respectively.
Reconstitution Calculator
Background: Syndecan-1/CD138
Syndecan-1, designated CD138, is a dimeric type I transmembrane (TM) protein that belongs to the syndecan family of Type 1 transmembrane proteins (1, 2). The four syndecan family members are major carriers of heparan sulfate (HS) and chondroitin sulfate glycosaminoglycans (GAGs) that have different expression patterns and extracellular sequences. Syndecan-1 forms weak non-covalent homodimers, or heterodimers with Syndecan-2 or -3, through interactions of the transmembrane domain (3). It is synthesized as a 310 amino acid (aa) precursor with a 17 aa signal sequence, a 234 aa extracellular domain (ECD) that includes three closely-spaced consensus Ser-Gly HS attachment sites near the N-terminus, a 25 aa TM segment, and a 34 aa cytoplasmic region that includes a PDZ binding motif with a tyrosine phosphorylation site. The ECD is variably modified by GAGs, producing molecular weights of 120-200 kDa for native Syndecan-1. Soluble forms are shed via proteolytic cleavage. Human Syndecan-1 ECD shares 65-71% aa identity with the ECD of rat, mouse, canine, equine and bovine Syndecan-1. Syndecan-1 shows highest expression on epithelial cells such as keratinocytes, and terminally differentiated B cells such as plasma cells (4, 5). It aids wound healing in skin, cornea, and heart following myocardial infarction by promoting re-epithelialization, migration, and collagen deposition (4-8). It binds chemokines, creating chemotactic gradients when shed, but also binds and modulates integrins to control the influx of leukocytes (5, 7, 9). The net effect is to allow, but limit, inflammation. In myeloma and other cancers, shedding of Syndecan-1 can facilitate growth, angiogenesis and metastasis (10-12). Growth factors, such as FGFs and HGF, bind GAG chains and use Syndecan-1 as a coreceptor (12, 13). The GAG chains may also be used by a variety of viruses and bacteria for cell adhesion and uptake (4). Our Avi-tag Biotinylated human Syndecan-1/CD138 features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
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