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TSPAN5 Rabbit pAb
- 产品详情
- 实验流程
Application 
| WB, IHC-P, IHC-F, IF |
|---|---|
| Primary Accession | P62079 |
| Other Accession | P62079 |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 30337 Da |
| Physical State | Liquid |
| Immunogen | KLH conjugated synthetic peptide derived from human TSPAN5 |
| Epitope Specificity | 21-130/268 |
| Isotype | IgG |
| Purity | affinity purified by Protein A |
| Buffer | 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol. |
| SIMILARITY | Belongs to the tetraspanin (TM4SF) family. |
| SUBUNIT | Monomer. Under normal conditions, interacts with HSP90AA1in the HSP90 multichaperone complex; the interaction preventstrimerization and activation of HSF1. On activation by heat-stressor by other factors such as metal ions, HSF1 is released from thecomplex, homotrimerizes, is hyperphosphorylated and translocated tothe nucleus where, subsequently, it can activate transcription.Binds the complex through the regulatory domain. Interacts withSYMPK and CSTF2 in heat-stressed cells. Interacts with FKBP4 in theHSP90 multichaperone complex; the interaction is independent of thephosphorylation state of HSF1. Interacts with MAPKAPK2. |
| Post-translational modifications | Phosphorylated on multiple serine residues, a subset of whichare involved in stress-related regulation of transcriptionactivation. Constitutive phosphorylation represses transcriptionalactivity at normal temperatures. Levels increase on specificresidues heat-shock and enhance HSF1 transactivation activity.Phosphorylation on Ser-307 derepresses activation on heat-stressand in combination with Ser-303 phosphorylation appears to beinvolved in recovery after heat-stress. Phosphorylated on Ser-230by CAMK2, in vitro. Cadmium also enhances phosphorylation at thissite. Phosphorylation on Ser-303 is a prerequisite for HSF1sumoylation. Phosphorylation on Ser-121 inhibits transactivationand promotes HSP90 binding. Phosphorylation on Thr-142 alsomediates transcriptional activity induced by heat.Sumoylated with SUMO1 and SUMO2 on heat-shock. Heat-induciblesumoylation occurs after 15 min of heat-shock, after which levelsdecrease and at 4 hours, levels return to control levels.Sumoylation has no effect on HSE binding nor on transcriptionalactivity. Phosphorylation on Ser-303 is a prerequisite forsumoylation. |
| Important Note | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
| Background Descriptions | TSPAN5 is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. |
| Gene ID | 10098 |
|---|---|
| Other Names | NET-4; NET4; TM4SF9; TSPAN-5; 2810455A09Rik; 4930505M03Rik; TSN5_BOVIN; TSPAN5; TSN5_HUMAN; Tetraspan NET-4; Transmembrane 4 superfamily member 9; TSN5_MOUSE; TSN5_RAT; tetraspanin 5 |
| Dilution | WB=1:500-2000,IHC-P=1:100-500,IHC-F=1:100-500,IF=1:100-500 |
| Storage | Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | TSPAN5 (HGNC:17753) |
|---|---|
| Synonyms | TM4SF9 |
| Function | Part of TspanC8 subgroup, composed of 6 members that interact with the transmembrane metalloprotease ADAM10. This interaction is required for ADAM10 exit from the endoplasmic reticulum and for enzymatic maturation and trafficking to the cell surface as well as substrate specificity. Different TspanC8/ADAM10 complexes have distinct substrates (PubMed:26686862, PubMed:28600292, PubMed:37516108). Promotes ADAM10-mediated cleavage of CD44 (PubMed:26686862). Seems to regulate VE-cadherin expression in endothelial cells probably through interaction with ADAM10, promoting leukocyte transmigration (PubMed:28600292). |
| Cellular Location | Cell membrane; Multi-pass membrane protein |
Research Areas
Application Protocols
Provided below are standard protocols that you may find useful for product applications.
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