Antibodies, Proteins, Kits and Reagents for Life Science

Key features and details

Suitable for: Blocking

Product name

Human Mannan Binding Lectin/MBL peptide (237-248) (Carboxyterminal end)
See all Mannan Binding Lectin/MBL proteins and peptides
Animal free

No
Nature

Synthetic
- Species
  
  Human
- Sequence
  
  STSHLAVCEFPI
- Amino acids
  
  237 to 248
Description

Human Mannan Binding Lectin/MBL peptide

Alternative names
- COLEC 1
- COLEC1
- Collectin-1
- HSMBPC
- Lectin, mannose-binding, soluble, 2
- Mannan binding lectin
- Mannan binding protein
- Mannan-binding protein
- Mannose binding lectin
- Mannose binding lectin (protein C) 2 soluble
- Mannose binding lectin (protein C) 2, soluble
- Mannose binding lectin (protein C) 2, soluble (opsonic defect)
- Mannose binding lectin 2 soluble
- Mannose binding lectin 2, soluble (opsonic defect)
- Mannose binding lectin protein C2 soluble opsonic defect
- Mannose binding protein
- Mannose binding protein C
- Mannose binding protein C precursor
- Mannose binding protein, serum
- Mannose-binding lectin
- Mannose-binding protein C
- MBL
- MBL 2
- MBL2
- MBL2_HUMAN
- MBL2D
- MBP
- MBP 1
- MBP C
- MBP-C
- MBP1
- MBPB
- MBPC
- MBPD
- MGC116832
- MGC116833
- Opsonic defect
- protein C
- Soluble mannose binding lectin
see all
Function

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. May bind DNA.
Tissue specificity

Plasma protein produced mainly in the liver.
Involvement in disease

Note=There is an association between low levels of MBL2 and a defect of opsonization which results in susceptibility to frequent and chronic infections.
Sequence similarities

Contains 1 C-type lectin domain.
Contains 1 collagen-like domain.
Cellular localization

Secreted.
Target information above from: UniProt accession P11226 The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010) .

Information by UniProt

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