CCDC90B Human
Coiled-Coil Domain Containing 90B Human Recombinant
Cat. No.
BT11791
Source
E.coli.
Synonyms
MDS011, MDS025, CUA003, Coiled-coil domain-containing protein 90B mitochondrial, CCDC90B.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
CCDC90B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (43-230 a.a) and having a molecular mass of 24.1kDa.
CCDC90B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
CCDC90B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Introduction
Belonging to the CCDC90 family, Coiled-Coil Domain Containing 90B (CCDC90B) is characterized by the presence of a DUF1640 domain. This domain, whose function remains unknown, spans the majority of the protein, excluding the initial 23 amino acids. These initial residues constitute a mitochondrial targeting site, suggesting that CCDC90B, upon cleavage, functions as a mitochondrial protein. Notably, CCDC90B is not predicted to possess any transmembrane spans or segments. Analyses suggest that CCDC90B contains at least three distinct phosphorylation sites.
Description
Recombinantly produced in E. coli, CCDC90B Human Recombinant is a single, non-glycosylated polypeptide chain. It comprises 211 amino acids (specifically, residues 43 to 230) and exhibits a molecular weight of 24.1 kDa. A 23 amino acid His-tag is fused to the N-terminus of CCDC90B. Purification is achieved using proprietary chromatographic methods.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The provided CCDC90B protein solution (at a concentration of 0.25 mg/ml) is formulated in a buffer consisting of 20mM Tris-HCl (pH 8.0), 0.15M NaCl, 10% glycerol, and 1mM DTT.
Stability
For optimal storage, the product should be kept at 4°C if the entire vial is expected to be used within 2-4 weeks. For prolonged storage, freezing at -20°C is recommended. To further enhance stability during long-term storage, the addition of a carrier protein (either HSA or BSA) to a final concentration of 0.1% is advisable. Repeated cycles of freezing and thawing should be avoided.
Purity
Purity exceeds 90%, as assessed by SDS-PAGE analysis.
Synonyms
MDS011, MDS025, CUA003, Coiled-coil domain-containing protein 90B mitochondrial, CCDC90B.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSGYDRRPV DITPLEQRKL TFDTHALVQD LETHGFDKTQ AETIVSALTA LSNVSLDTIY KEMVTQAQQE ITVQQLMAHL DAIRKDMVIL EKSEFANLRA ENEKMKIELD QVKQQLMHET SRIRADNKLD INLERSRVTD MFTDQEKQLM ETTTEFTKKD TQTKSIISET SNKIDAEIAS LKTLMESNKL E.
Product Science Overview
Gene and Protein Structure
The CCDC90B gene is located on chromosome 11q14.1 . The protein encoded by this gene consists of 254 amino acids and features several distinct domains:
- N-terminal mitochondrial targeting signal sequence: This sequence directs the protein to the mitochondria.
- Disordered region: Following the targeting signal, this region lacks a fixed structure.
- Head domain: This domain is involved in protein-protein interactions.
- Stalk domain: This domain contains the coiled-coil structure, which is characteristic of the protein.
- C-terminal transmembrane helix: This helix anchors the protein to the mitochondrial membrane .
Functional Role
CCDC90B is a membrane-anchored coiled-coil protein that interacts with other components of the MCU complex, including MCU and MCUR1 . Despite its interaction with these components, knockdown studies have shown that CCDC90B does not significantly alter mitochondrial calcium uptake, suggesting it has a nominal role in MCU activity .
Biochemical Features
Recombinant fragments of human CCDC90B have been studied to understand its structure and function. For instance, a purified fragment comprising residues 43 to 125, which includes the head-neck segment and part of the coiled-coil stalk, has been shown to form stable trimers in solution. Structural studies revealed that this fragment adopts an alpha-helical structure and forms an extended helical trimer .
Clinical Relevance
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