Analytical Data
-
Gene name
IAP
- Application
-
Alternative Names
IAP;API3;BIRC4;IAP3;E3 ubiquitin-Protein ligase XIAP
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9UMX0
-
Expression Region
2-589aa
-
AA Sequence
AESGESGGPPGSQDSAAGAEGAGAPAAAASAEPKIMKVTVKTPKEKEEFAVPENSSVQQFKEEISKRFKSHTDQLVLIFAGKILKDQDTLSQHGIHDGLTVHLVIKTQNRPQDHSAQQTNTAGSNVTTSSTPNSNSTSGSATSNPFGLGGLGGLAGLSSLGLNTTNFSELQSQMQRQLLSNPEMMVQIMENPFVQSMLSNPDLMRQLIMANPQMQQLIQRNPEISHMLNNPDIMRQTLELARNPAMMQEMMRNQDRALSNLESIPGGYNALRRMYTDIQEPMLSAAQEQFGGNPFASLVSNTSSGEGSQPSRTENRDPLPNPWAPQTSQSSSASSGTASTVGGTTGSTASGTSGQSTTAPNLVPGVGASMFNTPGMQSLLQQITENPQLMQNMLSAPYMRSMMQSLSQNPDLAAQMMLNNPLFAGNPQLQEQMRQQLPTFLQQMQNPDTLSAMSNPRAMQALLQIQQGLQTLATEAPGLIPGFTPGLGALGSTGGSSGTNGSNATPSENTSPTAGTTEPGHQQFIQQMLQALAGVNPQLQNPEVRFQQQLEQLSAMGFLNREANLQALIATGGDINAAIERLLGSQPS
-
Molecular Weight
69.8 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Research on immunoglobulin-binding proteins (IAPs) has gained significant attention due to their pivotal role in modulating immune responses. These proteins, which include a diverse range of molecules, bind to immunoglobulins and can influence not only the stability and half-life of antibodies but also their interaction with other components of the immune system. The importance of IAPs extends to various fields, including therapeutic antibody development, infection biology, and vaccine design. Understanding how IAPs function can provide critical insights into immune evasion strategies employed by pathogens, as many microbes express IAP-like proteins to subvert host defenses. Furthermore, researchers are exploring the potential of IAPs as targets for novel therapies and diagnostics, given their unique properties and the ability to tailor engineered IAPs for specific applications. The advancement of recombinant DNA technology has facilitated the production of recombinant IAP proteins, allowing for more detailed studies of their mechanisms and interactions. Overall, the investigation of IAPs holds promise for enhancing our understanding of immune regulation and developing innovative strategies to harness the immune system for therapeutic purposes.











