Human Factor XII (FXII) Matched Antibody Pair

Name: Human Factor XII (FXII) Matched Antibody Pair
SKU: ABPR-L015
Rating: 5 (1 reviews)

Regulatory status: For research use only, not for use in diagnostic procedures.

COA

SDS

Datasheet

Summary

Sample

Plasma

Species Reactivity

Human

Detection Method

Sandwich ELISA

Intended Use

This antibody pair set comes with matched antibody pair to detect and quantify protein level of Human Factor XII

Contents of Kit

1. Capture Antibody (yellow): 0.5 ml of polyclonal affinity purified anti-FXII antibody for coating plates.
2. Detecting Antibody (red): 0.5 ml of peroxidase conjugated polyclonal anti-FXII antibody for detection of captured FXII.
Note: Reagents are sufficient for at least 5×96 well plates using recommended protocols. Antibodies are supplied in a 50% (v/v) glycerol solution for storage at –10 to -20°C. Keep vials tightly capped. Do not store in frost-free freezers

Storage

-10 to -20°C

General Description

Factor XII (F.XII, Hageman factor) is a 76 kDa, single chain glycoprotein produced in the liver. In plasma, F.XII circulates as a protease zymogen at a concentration of approximately 30 μg/ml (400 nM). Upon vascular injury F.XII binds to negatively charged extravascular surfaces such as cartilage and skin, which facilitate activation of the zymogen to the active serine protease. Cleavage of F.XII by kallikrein after residue Arg353 produces the enzyme α F.XIIa, consisting of a 28 kDa light chain containing the protease domain, and a 52 kDa heavy chain containing the anionic surface-binding domain. Substrates for surface bound F.XIIa include the zymogens prekallikrein (PK) and factor XI (F.XI) as well as the procofactor high-molecular weight kininogen (HK). The activation of these substrates results in positive feedback activation of F.XII. Further cleavage of αF.XIIa by kallikrein produces the 28 kDa fragment β F.XIIa (Hageman factor fragment). βF.XIIa has reduced procoagulant activity as it lacks the anionic surface-binding domain, but is capable of fluid-phase activation of PK, factor VII and complement C1. The activity of F.XIIa in plasma is regulated predominantly by C1-Inhibitor, with relatively minor contributions by α2 Antiplasmin, α2 macroglobulin and antithrombin, even in the presence of therapeutic levels of heparin.

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Documents

pdf COA

pdf SDS

pdf Datasheet

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Customer Reviews

References

Genes lost during the transition from land to water in cetaceans highlight genomic changes associated with aquatic adaptations

SCIENCE ADVANCES

Authors: Huelsmann, Matthias; Hecker, Nikolai; Springer, Mark S.; Gatesy, John; Sharma, Virag; Hiller, Michael

Abstract

The transition from land to water in whales and dolphins ( cetaceans) was accompanied by remarkable adaptations. To reveal genomic changes that occurred during this transition, we screened for protein- coding genes that were inactivated in the ancestral cetacean lineage. We found 85 gene losses. Some of these were likely beneficial for cetaceans, for example, by reducing the risk of thrombus formation during diving (F12 and KLKB1), erroneous DNA damage repair (POLM), and oxidative stress- induced lung inflammation (MAP3K19). Additional gene losses may reflect other diving-related adaptations, such as enhanced vasoconstriction during the diving response (mediated by SLC6A18) and altered pulmonary surfactant composition (SEC14L3), while loss of SLC4A9 relates to a reduced need for saliva. Last, loss of melatonin synthesis and receptor genes (AANAT, ASMT, and MTNR1A/B) may have been a precondition for adopting unihemispheric sleep. Our findings suggest that some genes lost in ancestral cetaceans were likely involved in adapting to a fully aquatic lifestyle.

Optimization of culture media to enhance the growth of tissue engineered cartilage

BIOTECHNOLOGY PROGRESS

Authors: Bajic, Andjela; Tarantino, Roberto; Chiu, Loraine L. Y.; Duever, Thomas; Waldman, Stephen D.

Abstract

Tissue engineering is a promising option for cartilage repair. However, several hurdles still need to be overcome to develop functional tissue constructs suitable for implantation. One of the most common challenges is the general low capacity of chondrocytes to synthesize cartilage-specific extracellular matrix (ECM). While different approaches have been explored to improve the biosynthetic response of chondrocytes, several studies have demonstrated that the nutritional environment (e.g., glucose concentration and media volume) can have a profound effect on ECM synthesis. Thus, the purpose of this study was to optimize the formulation of cell culture media to upregulate the accumulation of cartilaginous ECM constituents (i.e., proteoglycans and collagen) by chondrocytes in 3D culture. Using response surface methodology, four different media factors (basal media, media volume, glucose, and glutamine) were first screened to determine optimal media formulations. Constructs were then cultured under candidate optimal media formulations for 4 weeks and analyzed for their biochemical and structural properties. Interestingly, the maximal accumulation of proteoglycans and collagen appeared to be elicited by different media formulations. Most notably, proteoglycan accumulation was favored by high volume, low glucose-containing DMEM/F12 (1:1) media whereas collagen accumulation was favored by high volume, high glucose-containing F12 media. While high glutamine-containing media elicited increased DNA content, glutamine concentration had no apparent effect on ECM accumulation. Therefore, optimizing the nutritional environment during chondrocyte culture appears to be a promising, straight-forward approach to improve cartilaginous tissue formation. Future work will investigate the combined effects of the nutritional environment and external stimuli.