CAB39L Human

Calcium Binding Protein 39 Like Human Recombinant
Cat. No.
BT28754
Source
Escherichia Coli.
Synonyms
MO25-BETA, MO2L, MLAA-34, Mo25-like protein.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% 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.
Shipped with Ice Packs
In Stock

Description

CAB39L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 360 amino acids (1-337a.a) and having a molecular mass of 41.5kDa. CAB39L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Calcium-binding protein 39-like (CAB39L) shares similarities with MO25 and is present in the blood of approximately 50% of patients with a blood cancer affecting a specific type of white blood cell. CAB39L is believed to be involved in the development of cancer. Additionally, a protein called LKB1 becomes more active when it binds to a group of proteins that includes CAB39L.
Description
This version of CAB39L is made in bacteria and is a single chain of protein building blocks. It is not modified with sugars and contains 360 building blocks, including a tag for purification. It has a size of 41.5 kDa.
Physical Appearance
A clear and colorless liquid free from bacteria.
Formulation
This CAB39L protein solution is provided at a concentration of 0.5mg/ml in a specific buffer containing Tris-HCl (pH 8.0), NaCl, glycerol, and DTT.
Stability
For short-term storage (up to 4 weeks), keep at 4°C. For longer storage, freeze at -20°C. Adding a carrier protein (HSA or BSA) is recommended for long-term storage. Avoid repeated freezing and thawing.
Purity
More than 95% pure based on SDS-PAGE analysis.
Synonyms
MO25-BETA, MO2L, MLAA-34, Mo25-like protein.
Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MGSMKKMPLF SKSHKNPAEI VKILKDNLAI LEKQDKKTDK ASEEVSKSLQ AMKEILCGTN EKEPPTEAVA QLAQELYSSG LLVTLIADLQ LIDFEGKKDV TQIFNNILRR QIGTRSPTVE YISAHPHILF MLLKGYEAPQ IALRCGIMLR ECIRHEPLAK IILFSNQFRD FFKYVELSTF DIASDAFATF KDLLTRHKVL VADFLEQNYD TIFEDYEKLL QSENYVTKRQ SLKLLGELIL DRHNFAIMTK YISKPENLKL MMNLLRDKSP NIQFEAFHVF KVFVASPHKT QPIVEILLKN QPKLIEFLSS FQKERTDDEQ FADEKNYLIK QIRDLKKTAP.

Product Science Overview

Gene and Protein Structure

The CAB39L gene is located on chromosome 13 and encodes a protein that consists of 341 amino acids with a molecular mass of approximately 42 kDa . The recombinant form of this protein is typically produced in E. coli and includes a 20 amino acid His-Tag at the N-terminus to facilitate purification .

Biological Functions

CAB39L is involved in several key biological pathways:

  • Signal Transduction: It acts as a component of a complex that binds and activates the serine/threonine kinase STK11/LKB1. This complex is essential for stabilizing the interaction between CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta) and STK11/LKB1 .
  • Kinase Activation: CAB39L enables protein serine/threonine kinase activator activity, which is crucial for intracellular signal transduction and the regulation of various cellular processes .
Tissue Distribution and Expression

CAB39L is expressed in various tissues, with significant roles in the innate immune system and endochondral ossification pathways . It is also implicated in diseases such as monocytic leukemia and immunodeficiency 10 .

Clinical Significance

Mutations or dysregulation of the CAB39L gene have been associated with several diseases, including monocytic leukemia and immunodeficiency 10 . As a biomarker, it holds potential for diagnostic and therapeutic applications in these conditions.

Recombinant Protein Production

The recombinant form of CAB39L is produced using E. coli expression systems. The protein is purified using chromatographic techniques to ensure high purity and functionality . This recombinant protein is valuable for research purposes, including studies on protein-protein interactions, kinase activation, and signal transduction pathways.

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