SELM Protein, Human

SELM protein emerged as a potential thiol-disulfide bond oxidoreductase that plays a key role in the complex disulfide bond formation process. This highlights the importance of SELM proteins in cellular machinery, actively contributing to the delicate coordination of molecular interactions. SELM Protein, Human is the recombinant human-derived SELM protein, expressed by E. coli , with tag free.

SELM Protein takes center stage as a potential thiol-disulfide oxidoreductase, playing a pivotal role in the intricate process of disulfide bond formation. This attribution highlights SELM Protein's significance in cellular mechanisms, actively contributing to the nuanced orchestration of molecular interactions. Such functional insights position SELM Protein as a key molecular actor, revealing its involvement in the complex biochemical pathways that govern the establishment of crucial disulfide linkages within the cellular milieu.

Human

E. coli

Tag Free

Q8WWX9 (A24-L145)

140606  [NCBI]

ATAYRPDWNRLSGLTRARVETCGGSQLNRLKEVKAFVTQDIPFYHNLVMKHLPGADPELVLLGRRYEELERIPLSEMTREEINALVQELGFYRKAAPDAQVPPEYVWAPAKPPEETSDHADL

Approximately 17 kDa.The reducing (R) protein migrate s as 17 kDa in SDS-PAGE may b e due to relative charge.

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized after extensive dialysis against solution in 20 mM Tris-HCl, 0.5 M NaCl, 6% Trehalose, pH 8.0.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.