Recombinant Human Mannose-Binding Protein C/MBL-2/MBP- C(C-6His) #abs04339

abs04339-10ug

1-2 Weeks

123

abs04339-50ug

1-2 Weeks

337

abs04339-500ug

1-2 Weeks

2353

abs04339-1mg

1-2 Weeks

3201

Description

Our Mammalian expression system has successfully produced Recombinant Human Mannose Binding Lectin 2. This protein is encoded by a target gene that expresses Glu21-Ile248 with a 6His tag at the C-terminus. We take pride in the quality of our product and ensure that it closely mimics the original protein structure.

Other names

MBP-C, also known as Collectin-1, Mannan-Binding Protein, or Mannose-Binding Lectin, is a protein encoded by the MBL2 gene (also named COLEC1) that plays a vital role in the innate immune system. It is a pattern recognition molecule that binds to a range of microorganisms through carbohydrate binding, which initiates the complement system and activates the immune response to eliminate pathogens.
Mannose-Binding Protein C is a multifunctional protein that is produced mainly in the liver and secreted into the bloodstream. It is a member of the collectin family, a group of innate immune proteins that have collagen-like domains and calcium-dependent carbohydrate recognition domains. Collectins are involved in the clearance of apoptotic cells, as well as the recognition and clearance of microorganisms.
MBP1 has been found to be crucial in the defense against infections, including viral, bacterial, and fungal infections. Research has also shown that MBP-C plays a role in inflammation, tissue repair, and autoimmune diseases. Some studies have suggested that low levels of MBP-C may be linked to an increased risk of bacterial infections in individuals with compromised immune systems, while high levels of MBP-C may be associated with increased susceptibility to autoimmune diseases.
Overall, the function of Mannose-Binding Protein C is vitally important in the innate immune system, helping to defend the host against infection and foreign invaders. Future research may help us better understand the role of this critical protein in human health and disease.

Source

Human Cells

Format

pH 7.2, 5% Trehalose, 150mM NaCl, and 20mM PB were lyophilized from a solution filtered through a 0.2 μm filter. Let me provide you with some additional information on the process.

Properties

aa_sequence

PAGKPSPGKGQKGDPGKGEKGEPGQGLPGQGLRGLQGPPGKLGPPGNPGPSGSPGPDGDSSLAASERKALQTEMARIKKWLTFSLGNKFFLTNGEIMTFEKEVKALCVKFQASVATPRNAAENGAIQNGEAGSDEDCVLLLKNGQWNDSLAFTSHPIVCEFPPVTDENLTYTNWNEGEPNNAGQKFPGKDFPGKDGRDGTKETVTCEDAQKTCPAVIACSSPGINGFPGKDGVFVDLTGNTTEGQEDKTE.

Concentration

Through SDS-PAGE reduction, the analysis revealed that the protein has a similarity rate of more than 95%. In order to communicate the information in a different manner, this statement could be rephrased as follows: The protein's comparison rate was evaluated using SDS-PAGE reduction techniques, and the outcome demonstrated that the similarity score was greater than 95%.

Endotoxin_level

The LAL test has determined the presence of less than 0.1 ng/μg (1 IEU/μg). A highly similar content can be generated by rearranging the information provided above.

Reconstitution

It is advisable to always spin the tubes in a centrifuge prior to opening them. Avoid using vortex or pipetting to mix the contents. Reconstituting the protein to a concentration below 100 μg/ml is not recommended. To dissolve the lyophilized protein, kindly use ddH2O. To prevent damage from freeze-thaw cycles, kindly divide the reconstituted solution into smaller portions.

Target

Background

Mannose-Binding Protein C (MBP-C) belongs to the Collectin family of innate immune defense proteins. MBL binds to an array of carbohydrate patterns on pathogen surfaces. Collectin family members share common structural features: a cysteine rich amino-terminal domain, a collagen-like region, an α-helical coiled-coil neck domain and a carboxy terminal C-type Lectin or carbohydrate recognition domain (CRD). MBL homotrimerizes to form a structural unit joined by N-terminal disulfide bridges. These homotrimers further associates into oligomeric structures of up to 6 units. Whereas two forms of MBL proteins exist in rodents and other animals. Human MBL-2 is 25 kDa. Human MBL-2 is a secreted glycoprotein that is synthesized as a 248 amino acid (aa) precursor that contains a 20 aa signal sequence, a 21 aa cysteine-rich region, a 58 aa collagen-like segment and a 111 aa C-type lectin domain that binds to neutral bacterial carbohydrates.

Accession

P11226