CRYM Human
Description
CRYM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 334 amino acids (1-314) and having a molecular mass of 35.9kDa. CRYM is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
Recombinant human CRYM, expressed in E. coli bacteria, is a single polypeptide chain devoid of any glycosylation modifications. It comprises 334 amino acids, with the first 314 representing the CRYM protein and an additional 20 amino acids forming a His-Tag at the N-terminus. The protein has a molecular weight of 35.9 kDa and is purified using proprietary chromatographic methods.
The CYRM solution has a concentration of 1mg/ml and is prepared in a buffer containing 20mM Tris-HCl (pH 8.0), 1mM DTT, and 10% glycerol.
While CRYM remains stable for up to one week at 4°C, it is recommended to store it below -18°C for optimal long-term preservation. Adding a carrier protein like HSA or BSA (0.1%) is advisable for prolonged storage. Repeated freezing and thawing should be avoided.
MGSSHHHHHH SSGLVPRGSH MSRVPAFLSA AEVEEHLRSS SLLIPPLETA LANFSSGPEG GVMQPVRTVV PVTKHRGYLG VMPAYSAAED ALTTKLVTFY EDRGITSVVP SHQATVLLFE PSNGTLLAVM DGNVITAKRT AAVSAIATKF LKPPSSEVLC ILGAGVQAYS HYEIFTEQFS FKEVRIWNRT KENAEKFADT VQGEVRVCSS VQEAVAGADV IITVTLATEP ILFGEWVKPG AHINAVGASR PDWRELDDEL MKEAVLYVDS QEAALKESGD VLLSGAEIFA ELGEVIKGVK PAHCEKTTVF KSLGMAVEDT VAAKLIYDSW SSGK
Product Science Overview
Crystallins are divided into two main classes: taxon-specific and ubiquitous. Crystallin, Mu falls under the taxon-specific category. The gene encoding Crystallin, Mu is known as CRYM and is located on chromosome 16p13.11 in humans . This gene encodes a protein that is expressed in various tissues, including neural tissue, muscle, and kidney .
The recombinant form of Crystallin, Mu is typically produced in Escherichia coli (E. coli) and includes an N-terminal His-tag for purification purposes . The protein consists of 314 amino acids and has a molecular weight of approximately 35.9 kDa . The high purity of the recombinant protein (>95%) is confirmed through SDS-PAGE analysis .
Crystallin, Mu is also known as ketimine reductase or NADP-regulated thyroid-hormone-binding protein (THBP) . It plays a crucial role in the reduction of imine bonds in brain substrates, which may include cystathionine ketimine (CysK) and lanthionine ketimine (LK) . Additionally, it binds thyroid hormone, which acts as a strong reversible inhibitor . This binding is presumed to regulate the free intracellular concentration of triiodothyronine and its access to nuclear receptors .
