MBL2 / MBL / COLEC1 Protein (Native)

22.05.2013

Sino Biological Inc. liefert MBL2 / MBL / COLEC1 Protein (Native) mit höherer Qualität und günstiger Kosten im Vergleich mit anderen globalen Lieferanten.

Weitere Informationen über MBL2 / MBL / COLEC1 Protein (Native) lesen Sie bitte: http://www.sinobiological.com/MBL-2-Protein-a-637.html

Produkt-Information von MBL2 / MBL / COLEC1 Protein

Synonym	MBL, COLEC1, HSMBPC, MBP, MBP1
Protein Construction	A DNA sequence encoding the human MBL (NP_000233.1) (Met1-Ile 248) was expressed.
Source	Human
Expression Host	CHO Stable Cells

QC Testing von MBL2 / MBL / COLEC1 Protein

Purity	> 95 % as determined by SDS-PAGE	SDS-PAGE: MBL2 protein
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Stability	Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N terminal	Glu 21
Molecular Mass	The recombinant human MBL consists of 228 amino acids and predicts a molecular mass of 24 KDa. It migrates as an approximately 31 KDa band in SDS-PAGE under reducing conditions.
Formulation	Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. Please contact us for any concerns or special requirements.

Usage Guide von MBL2 / MBL / COLEC1 Protein

Storage	Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution	A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

Beschreiung von MBL2 / MBL / COLEC1 Protein

Mannose/mannan-binding lectin (MBL) found in serum belongs to the class of collectins in the C-type lectin superfamily, and is involved in first-line host defense as a key component of innate immunity. MBL monomeric polypeptide consists of a short N-terminal cysteine-rich domain, a collagen-like domain of 18-20 repeats of Gly-Xaa-Yaa with an interruption (Gly-Gln-Gly) and a C-terminal carbohydrate recognition, or lectin, domain. MBL recognizes carbohydrate patterns, such as mannose and N-acetylglucosamine, found on the surface of a large number of pathogenic microorganisms including bacteria, viruses, protozoa and fungi. MBL subunits are comprised of three identical 32kDa polypeptides, followed by formation of the disulfide cross-linked higher order MBL oligomers (400-700 kDa). Although MBL can form several oligomeric forms, there are indications that dimers and trimers are not biologically active and at least a tetramer form is needed for activation of complement. Active MBL forms complex with another protein MASP-2 (MBL-associated serine protease 2) and binds to the microorganisms, and thus leads to the activation of the lectin pathway of the complement system. MBL defects have been associated with susceptibility to autoimmune and infectious diseases.

References

Super M. et al., 1992, Nat Genet. 2: 50-5.
Wong NK. et al., 1999, Mol Immunol. 36: 853-61.
Butler GS. et al., 2002, J Biol Chem. 277: 17511-9.
Ji X. et al., 2005, Mol Immunol. 42: 145-52.
Bouwman LH. et al., 2006, Hum Immunol. 67: 247-56.