SCGB1A1 Human
Uteroglobin Human Recombinant
Cat. No.
BT29768
Source
Escherichia Coli.
Synonyms
Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs 
In Stock 
Description
Uteroglobin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of 15.8kDa.
The SCGB1A1 is purified by proprietary chromatographic techniques.
The SCGB1A1 is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Uteroglobin (SCGB1A1), a member of the Secretoglobin (SCGBs) family, is a versatile protein with anti-inflammatory and anti-tumorigenic properties. It achieves this by binding to small hydrophobic molecules like phospholipids and prostaglandins. Uteroglobin plays a crucial role in various biological processes, including inflammation reduction, phospholipase A2 inhibition, and the sequestration of hydrophobic ligands. Primarily produced by Clara cells (non-ciliated, non-mucous secretory cells abundant in lung bronchioles) and other epithelia interacting with the external environment, SCGB1A1 not only sequesters pro-inflammatory mediators and carcinogens but also participates in inhibiting cell migration and invasion, platelet aggregation, and T cell differentiation. Notably, defects in the SCGB1A1 gene are linked to an increased susceptibility to asthma.
Description
Recombinant Human Uteroglobin, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 70 amino acids. With a molecular weight of 15.8 kDa, SCGB1A1 undergoes purification using proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The Uteroglobin protein was lyophilized from a 0.2µm filtered solution concentrated in PBS with a pH of 7.4.
Solubility
For reconstitution of lyophilized SCGB1A1, sterile 18M-cm H₂O at a concentration of at least 100µg/ml is recommended. This solution can be further diluted with other aqueous solutions.
Stability
Lyophilized Uteroglobin remains stable at room temperature for up to 3 weeks; however, storage in desiccated conditions below -18°C is recommended. After reconstitution, SCGB1A1 should be stored at 4°C for 2-7 days. For long-term storage, adding a carrier protein (0.1% HSA or BSA) is advisable. It is important to avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 98.0% as determined by: (a) Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) analysis and (b) Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis.
Biological Activity
The ED₅₀, determined by the immobilized protein's ability to support the adhesion of A549 human lung carcinoma cells, is less than 5.0µg/ml. This corresponds to a specific activity exceeding 200 IU/mg.
Synonyms
Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.
Source
Escherichia Coli.
Amino Acid Sequence
EICPSFQRVI ETLLMDTPSS YEAAMELFSP DQDMREAGAQ LKKLVDTLPQ KPRESIIKLM EKIAQSSLCN.
Product Science Overview
Structure and Expression
Uteroglobin is a small, non-glycosylated protein that forms a homodimeric structure with a molecular weight of approximately 16.1 kDa . It consists of 142 amino acid residues and is produced and secreted by non-ciliated, non-mucous Clara cells, which are predominant in the epithelial surfaces of pulmonary airways . These cells are also found in other non-ciliated epithelia .
Biological Functions
Uteroglobin has several important biological functions:
- Anti-inflammatory Effects: By binding to phospholipids and prostaglandins, Uteroglobin can sequester pro-inflammatory mediators, thereby reducing inflammation .
- Anti-tumorigenic Effects: It has been shown to inhibit cell migration and invasion, which are critical processes in cancer metastasis .
- Immune Modulation: Uteroglobin can influence immune responses by affecting T cell differentiation and platelet aggregation .
Recombinant Production
Recombinant Human Uteroglobin is produced using Escherichia coli (E. coli) expression systems . The recombinant protein is purified to a high degree, with a purity of ≥ 98% as determined by SDS-PAGE gel and HPLC analyses . The endotoxin level is maintained at less than 0.1 ng/µg of protein, ensuring its suitability for research applications .
Applications in Research
Due to its multifunctional properties, Uteroglobin is of significant interest in various fields of research, including:
- Cancer Research: Its anti-tumorigenic effects make it a valuable tool for studying cancer cell behavior and potential therapeutic interventions .
- Inflammation Studies: Researchers utilize Uteroglobin to investigate mechanisms of inflammation and develop anti-inflammatory therapies .
- Immune System Research: Its role in modulating immune responses is crucial for understanding immune-related diseases and developing immunotherapies .
Quick Inquiry
Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
