MBL Antibody (285623) [Alexa Fluor® 350]

• Reactivity: Hu
• Applications: B/N
• Clone: 285623
• Clonality: Monoclonal
• Host: Mouse
• Conjugate: Alexa Fluor 350

MBL Antibody (285623) [Alexa Fluor® 350] Summary

• Immunogen: Mouse myeloma cell line NS0-derived recombinant human MBL
  Glu21-Ile248
  Accession # AAH96182
• Specificity: Detects human MBL in direct ELISAs and Western blots. In direct ELISAs and Western blots, no cross-reactivity with recombinant mouse MBL-2 is observed.
• Isotype: IgG2a
• Clonality: Monoclonal
• Host: Mouse
• Purity Statement: Protein A or G purified

Applications/Dilutions

• Dilutions:
  • Blockade of Receptor-ligand Interaction

Packaging, Storage & Formulations

• Storage: Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied
• Buffer: Supplied 0.2mg/ml in 1X PBS with RDF1 and 0.09% Sodium Azide

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for MBL Antibody (285623) [Alexa Fluor® 350]

• COLEC1
• COLEC1collectin-1
• Collectin-1
• HSMBPC
• Mannan-binding protein
• mannose-binding lectin (protein C) 2, soluble (opsonic defect)
• mannose-binding lectin (protein C) 2, soluble
• Mannose-binding lectin
• mannose-binding protein C
• MBL
• MBL2
• MBL2D
• MBLmannan-binding lectin
• MBP
• MBP1
• MBP1mannose-binding lectin 2, soluble (opsonic defect)
• MBP-C
• MGC116832
• MGC116833

Background

Human mannose/mannan-binding lectin (MBL; gene name MBL2; also called MBP-C) is a 25 kDa member of the collectin family of pattern-recognition molecules (1‑3). It 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 (with three cysteines) a 58 aa collagen-like segment and a 111 aa C-type lectin domain that binds to neutral bacterial carbohydrates (3, 4). The molecule is O-glycosylated and contains multiple hydroxylated prolines and lysines (3, 5). Functionally, the molecule operates as a multimer/oligomer. The basic structural unit is a homotrimer. The homotrimer is created by the formation of interchain disulfide bonds among the cysteine-rich regions, plus a helical interaction of the collagen-like domains of each participating polypeptide (5). Mutations in the collagen region are known to interfere with proper trimer and subsequent oligomer formation (6). Once formed, the trimer, as a unit, oligomerizes with other trimers to form high molecular weight complexes. Although the exact nature of these complexes are unclear, it would appear that a three trimer complex (230 kDa) and a four trimer complex (305 kDa) constitute much of the circulating MBL (7). It is within the context of these oligomers that MBL performs its functions. After secretion by hepatocytes, oligomerized MBL will both associate with serine proteases (MASP-1, 2 & 3) and bind to bacterial carbohydrates. If the MBL complex is small, opsonization of bacreria occurs. If the complex is large, the MASPs are engaged and a complement attack complex is generated, destroying bound bacteria (3, 7, 8). Human MBL shares 63%, 61% and 65% aa identity with mouse, porcine and bovine MBL, respectively.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.