anti-Vitamin D Binding Protein, mAb (2B12)

CHF 322.00
In stock
YIF-LF-MA0147100 µlCHF 322.00
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Product Details
Synonyms GC; VDB; DBP; Gc-Globulin; Group-specific Component; Vitamin D-binding Protein
Product Type Monoclonal Antibody
Properties
Clone 2B12
Isotype Mouse IgG2b κ
Immunogen/Antigen Protein purified from human plasma.
Application

Western Blot (1:2,000)
IHC-P

Crossreactivity Human
Purity Detail Ammonium sulfate precipitation.
Formulation Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol.
Other Product Data

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Our product description may differ slightly from the original manufacturers product datasheet.

Declaration Manufactured by AbFrontier
Shipping and Handling
Shipping BLUE ICE
Short Term Storage +4°C
Long Term Storage -20°C
Use/Stability Stable for at least 1 year after receipt when stored at -20°C.
Documents
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Product Specification Sheet
Datasheet Download PDF

Vitamin D-binding protein (DBP, VDBP), also called group-specific component (Gc) and macrophage-activating factor (GcMAF/DBP-MAF), is 52 to 58kDa plasma glycoprotein with many functions, such as transport of vitamin D metabolites, control of bone development, binding of fatty acids, sequestration of actin, and modulating immune and inflammatory responses. DBP is synthesized predominantly by hepatic parenchymal cells and detected in plasma, cerebrospinal fluid, seminal fluid, saliva and breast milk. The exploitation of the unique properties of DBP could enable the development of important therapeutic agents such as vitamin D-associated conditions, actin sequestering in trauma and inflammation, chronic obstructive pulmonary disease, osteopetrosis, cancer therapy and immune modulation by macrophage activation. The DBP molecule is therefore an ideal candidate molecule for further investigation by biotechnology-based companies seeking a platform from which to pursue new therapeutic options. Transferrins are iron binding transport proteins which can bind two Fe3+ ions in association with the binding of an anion, usually bicarbonate. Lactotransferrin has antimicrobial activity which depends on the extracellular cation concentration. Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for κ-receptors than for mu-receptors. The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity.

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