Recombinant Human Serum Amyloid P/SAP protein is a Human Full Length protein, in the 20 to 223 aa range, expressed in Mammalian, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
>95% SDS-PAGE
< 1 EU/µg
Mammalian
His tag C-Terminus
SDS-PAGE, HPLC
No
H T D L S G K V F V F P R E S V T D H V N L I T P L E K P L Q N F T L C F R A Y S D L S R A Y S L F S Y N T Q G R D N E L L V Y K E R V G E Y S L Y I G R H K V T S K V I E K F P A P V H I C V S W E S S S G I A E F W I N G T P L V K K G L R Q G Y F V E A Q P K I V L G Q E Q D S Y G G K F D R S Q S F V G E I G D L Y M W D S V L P P E N I L S A Y Q G T P L P A N I L D W Q A L N Y E I R G Y V I I K P L V W V D H H H H H H
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application HPLC | Reactivity Reacts | Dilution info - | Notes - |
Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin.
Serum amyloid P-component, SAP, 9.5S alpha-1-glycoprotein, APCS, PTX2
Recombinant Human Serum Amyloid P/SAP protein is a Human Full Length protein, in the 20 to 223 aa range, expressed in Mammalian, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
Serum amyloid P-component, SAP, 9.5S alpha-1-glycoprotein, APCS, PTX2
>95% SDS-PAGE
< 1 EU/µg
Mammalian
His tag C-Terminus
SDS-PAGE, HPLC
No
No
Human
Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100 µg/ml. Dissolve the lyophilized protein in 1X PBS.
pH: 7.2
Constituents: 99% Phosphate Buffer, 0.88% Sodium chloride
H T D L S G K V F V F P R E S V T D H V N L I T P L E K P L Q N F T L C F R A Y S D L S R A Y S L F S Y N T Q G R D N E L L V Y K E R V G E Y S L Y I G R H K V T S K V I E K F P A P V H I C V S W E S S S G I A E F W I N G T P L V K K G L R Q G Y F V E A Q P K I V L G Q E Q D S Y G G K F D R S Q S F V G E I G D L Y M W D S V L P P E N I L S A Y Q G T P L P A N I L D W Q A L N Y E I R G Y V I I K P L V W V D H H H H H H
Full Length
23.2 kDa
20 to 223
Recombinant
His tag C-Terminus
Lyophilized
Greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE.
Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin.
Belongs to the pentraxin family.
N-glycosylated with a complex biantennary oligosaccharide chain with a sialic acid at the end (disialo-SAP). Monosialo-SAP as well as asioalo-SAP are also detected (PubMed:15174148).
Blue Ice
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
ab151645 was produced by transfected Human cells.Previously labelled as Serum Amyloid P.
Serum Amyloid P component also known as SAP P-SAP or APCS protein is a pentraxin family member. It has a molecular mass of approximately 25 kDa. SAP expresses mainly in the liver and circulates in blood plasma. The protein consists of five identical subunits which form a homopentameric structure. This structure enables SAP to bind to amyloid fibrils a defining mechanical action of this protein.
SAP plays a role in the immune system by recognizing damaged cells and pathogens. It acts as an opsonin marking these cellular targets for phagocytosis. As part of a complex SAP stabilizes extracellular matrix and amyloid deposits. It binds specifically to amyloid fibrils found in various tissues potentially facilitating their removal by immune cells. The protein's binding actions are important for its role in maintaining tissue and fluid homeostasis.
SAP is actively involved in the innate immune response and amyloidogenic pathways. It interacts with the complement system to enhance the clearance of cell debris and amyloid fibrils. The complement system is an important component of innate immunity where SAP can engage with complement proteins like C1q. This interaction suggests that SAP plays roles in modulating both inflammation and tissue repair processes.
SAP has significant connections. SAP is related to systemic amyloidosis where it binds to amyloid deposits affecting multiple organs. Moreover SAP has been implicated in Alzheimer's disease due to its interaction with beta-amyloid protein plaques. In these disorders the involvement of SAP aids researchers in understanding the pathological mechanisms and could open avenues for targeted therapies aimed at modulating SAP functions.
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