RHBDD1 Rabbit Polyclonal Antibody
CNY 1,999.00
CNY 3,280.00
货期*
2周
规格
经常一起买 (1)
beta Actin Mouse Monoclonal Antibody, Clone OTI1, Loading Control
CNY 300.00
CNY 1,430.00
Specifications
Product Data | |
Applications | ICC/IF, WB |
Recommend Dilution | WB,1:500 - 1:2000 IF,1:50 - 1:100 |
Reactivity | Human, Mouse, Rat |
Modifications | Unmodified |
Host | Rabbit |
Clonality | Polyclonal |
Immunogen | Recombinant fusion protein containing a sequence corresponding to amino acids 206-315 of human RHBDD1 (NP_115652.2). |
Formulation | Buffer: PBS with 0.02% sodium azide,50% glycerol,pH7.3. |
Concentration | lot specific |
Purification | Affinity purification |
Conjugation | Unconjugated |
Storage Condition | Store at -20℃. Avoid freeze / thaw cycles. |
Predicted Protein Size | 12kDa/35kDa |
Gene Name | rhomboid domain containing 1 |
Database Link | |
Background | Intramembrane-cleaving serine protease that cleaves single transmembrane or multi-pass membrane proteins in the hydrophobic plane of the membrane, luminal loops and juxtamembrane regions. Involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors. Functional component of endoplasmic reticulum-associated degradation (ERAD for misfolded membrane proteins. Required for the degradation process of some specific misfolded endoplasmic reticulum (ER luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Functions in BIK, MPZ, PKD1, PTCRA, RHO, STEAP3 and TRAC processing. Involved in the regulation of exosomal secretion; inhibits the TSAP6-mediated secretion pathway. Involved in the regulation of apoptosis; modulates BIK-mediated apoptotic activity. Also plays a role in the regulation of spermatogenesis; inhibits apoptotic activity in spermatogonia. |
Synonyms | DKFZp547E052; MGC117258 |
Reference Data |
Documents
Product Manuals |
FAQs |
SDS |
Resources
抗体相关资料 |
Customer
Reviews
Loading...