MBL1 recombinant protein

Recombinant Mouse MBL1 Protein (His tag)

Cat. Num. AAA2547240

• Gene Names: Mbl1; MBL-A; MBP-A; S-MBP
• Purity: > 92 % as determined by SDS-PAGE
• Synonyms: MBL1; Recombinant Mouse MBL1 Protein (His tag); MBL-A; MBP-A; S-MBP; Mbl1; MBL1 recombinant protein

• Host: Human Cells
• Purity/Purification: > 92 % as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH 7.4
• Sequence Length: 239

• Application Notes: The secreted recombinant mouse MBL consists of 238 amino acids and has a calculated molecular mass of 25.8 kDa. As a result of glycosylation, the recombinant protein migrates as an approximately 32 kDa protein in SDS-PAGE under reducing conditions.
• Predicted N Terminal: His
• Endotoxin: < 1.0 EU per mug of the protein as determined by the LAL method
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -70 degree C

SDS-PAGE

Related Product Information for MBL1 recombinant protein

Background: Mannose-binding lectin (MBL), also named mannose or mannan-binding protein (MBP), is a C-type lectin which participates in the innate immune system as an activator of the complement system and as opsonin after binding to certain carbohydrate structures on microorganisms and pathogens. Its function appears to be pattern recognition in the first line of defense in the pre-immune host. MBL recognizes carbohydrate patterns found on the surface of a large number of pathogenic micro-organisms including bacteria, viruses, protozoa and fungi. Binding of MBL to a micro-organism results in activation of the lectin pathway of the complement system. Two forms of MBL, MBL-A and MBL-C, were characterized in rodents, rabbits, bovine and rhesus monkeys, whereas only one form was identified in humans, chimpanzees and chickens. The two forms are encoded by two distinct genes named MBL1 and MBL2, which have been identified in many species including the pig. The MBL1 and MBL2 genes encode mannan-binding lectins (MBL) A and C, respectively, that are collagenous lectins (collectins) produced mainly by the liver. The MBL1 gene encodes MBL-A, which has bacteria-binding properties in pigs and rodents but is mutated to a pseudogene in humans and chimpanzees. Deficiency of MBL is probably the most common human immunodeficiency and is associated with an increased risk of mucosally acquired infections including meningococcal disease. MBL could modify disease susceptibility by modulating macrophage interactions with mucosal organisms at the site of initial acquisition.

Description: A DNA sequence encoding the mature form of mouse MBL (NP_034905.1) (Ser 18-Ala 239) was expressed with a N-terminal polyhistidine tag.

NCBI and Uniprot Product Information

• NCBI GI #: 6754654
• NCBI GeneID: 17194
• NCBI Accession #: NP_034905.1
• NCBI GenBank Nucleotide #: NM_010775.2
• UniProt Accession #: P39039; Q0P6H1
• Molecular Weight: 15,600 Da
• NCBI Official Full Name: mannose-binding protein A
• NCBI Official Synonym Full Names: mannose-binding lectin (protein A) 1
• NCBI Official Symbol: Mbl1
• NCBI Official Synonym Symbols: MBL-A; MBP-A; S-MBP
• NCBI Protein Information: mannose-binding protein A
• UniProt Protein Name: Mannose-binding protein A
• Protein Family: Mannose-binding protein
• UniProt Gene Name: Mbl1
• UniProt Synonym Gene Names: MBP-A; RaRF p28B

Uniprot Description

Mbl1: Calcium-dependent lectin involved in innate immune defense. Binds mannose, fucose and N-acetylglucosamine on different microorganisms and activates the lectin complement pathway. Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating their uptake by macrophages. 2 isoforms of the human protein are produced by alternative splicing.

Chromosomal Location of Human Ortholog: 14 B|14 22.36 cM

Cellular Component: extracellular space

Molecular Function: calcium ion binding; calcium-dependent protein binding; mannose binding; polysaccharide binding; protease binding; protein homodimerization activity

Biological Process: complement activation, lectin pathway; defense response to Gram-positive bacterium; killing by host of symbiont cells; positive regulation of phagocytosis; protein homotetramerization