Recombinant Human Serum Amyloid P-Component (APCS) Protein (His)

Name: Recombinant Human Serum Amyloid P-Component (APCS) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07918P
Price: 549.6 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Serum Amyloid P-Component (APCS) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P02743
Target Symbol	APCS
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	HTDLSGKVFVFPRESVTDHVNLITPLEKPLQNFTLCFRAYSDLSRAYSLFSYNTQGRDNELLVYKERVGEYSLYIGRHKVTSKVIEKFPAPVHICVSWESSSGIAEFWINGTPLVKKGLRQGYFVEAQPKIVLGQEQDSYGGKFDRSQSFVGEIGDLYMWDSVLPPENILSAYQGTPLPANILDWQALNYEIRGYVIIKPLVWV
Expression Range	20-223aa
Protein Length	Full Length of Mature Protein
Mol. Weight	27.3 kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin.
Subcellular Location	Secreted.
Protein Families	Pentraxin family
Database References	HGNC: 584 OMIM: 104770 KEGG: hsa:325 STRING: 9606.ENSP00000255040 UniGene: Hs.507080
Associated Diseases	SAP is a precursor of amyloid component P which is found in basement membrane and associated with amyloid deposits.
Tissue Specificity	Found in serum and urine.

Gene Functions References

The findings suggest that the F57I mutation affects the aggregation process of lysozyme resulting in the formation of cytotoxic species and that SAP is able to prevent cell death in the F57I flies by preventing accumulation of toxic F57I structures. PMID: 27428539
Data suggest that SAP (serum amyloid P-component) interacts with at least 33 proteins/ligands in plasma containing physiological calcium levels; these ligands can be categorized to include apolipoproteins, complement system proteins, coagulation proteins, and components that regulate proteolysis. PMID: 28098450
Data suggest that serum haptoglobin, fetuin-A, platelet factor-4, hs-CRP (high sensitive-C-reactive protein), SAP (serum amyloid P), AGP (alpha1-acid glycoprotein) levels of adolescents with metabolic syndrome are significantly higher than those of controls subjects. PMID: 27754964
SNPs in APCS were associated with late age at onset in familial amyloid polyneuropathy. PMID: 26286643
Data suggest that serum amyloid P (SAP) activates CD209 DC-SIGN to regulate the innate immune system differently from C-reactive protein (CRP), and that DC-SIGN is a target for antifibrotics. PMID: 26106150
Here, it is reported that X-ray analysis of the SAP complex with CPHPC and cadmium ions provides higher resolution detail of the interaction than is observed with calcium ions. PMID: 25084341
Compared to wildtype C57BL/6 mice, we find that in Apcs-/- "SAP knock-out" mice, bleomycin induces a more persistent inflammatory response and increased fibrosis. PMID: 24695531
The effects of SAP and Xiapex (Collagenase Clostridium histolyticum) on fibrocytes derived from Dupuytren's disease, was evaluated. PMID: 24933153
plasma protein serum amyloid P binds to FcgammaRI on monocytes to inhibit fibrocyte differentiation, and binds to FcgammaRIIa on neutrophils to reduce neutrophil adhesion. PMID: 25024390
In the late phase post-myocardial infarct there is a coordinated decrease in immune response-inflammation proteins, except for SAP which showed an increase related to the specific activation of the classical complement pathway. PMID: 23992930
9 different proteins (haptoglobin, transthyretin, apolipoprotein A-1, serum amyloid P component, apolipoprotein E, complement factor H, fibrinogen gamma, thrombin, complement C3) were identified as a potential diagnostic pattern of Parkinson's disease. PMID: 23385359
Human SAP binds phosphoethanolamine, while rabbits seem to have low levels of SAP that bind to a lesser extent. PMID: 23600950
These results indicate that SAP functions as a host defense factor, similar to other peptidoglycan recognition proteins and nucleotide-binding oligomerization domain-like receptors. PMID: 23966633
SAP may act as an effective receptor mimic to limit influenza A virus infection of airway epithelial cells. PMID: 23544079
Persons who develop non-affective psychoses have lower levels of certain acute phase proteins, including SAP, at the time of birth. PMID: 23423137
[review] On the basis of structure, serum amyloid P component is a prototype of the short pentraxin family. PMID: 23527487
SAP has a new role in reducing the toxicity of early amyloidogenic aggregates in transthyretin amiloidosis. PMID: 23390551
observations suggest that serum amyloid P, at least in part, uses FcgammaRI and FcRgamma to inhibit fibrocyte differentiation PMID: 22493081
Low levels of serum amyloid P mark the brains of individuals who escape dementia despite the presence of beta amyloid plaques and tangles in Alzheimer's disease neuropathology. PMID: 22205573
Studies indicate that pharmaceutical grade serum amyloid P component and C-reactive protein were isolated and purified. PMID: 22867744
The START domain in GPBP is important for this interaction. SAP and GPBP form complexes in blood and partly colocalize in amyloid plaques from Alzheimer disease patients. PMID: 22396542
Serum amyloid P level increased by approximately 5-fold in Parkinson's disease samples;a potential feasibility of plasma amyloid P as a marker to approach Parkinson's disease PMID: 21223953
Under physiological conditions, phosphoethanolamine is bound with higher affinity by human SAP than by human CRP. PMID: 21360619
TGF-beta driven lung fibrosis is macrophage dependent and blocked by Serum amyloid P. PMID: 21044893
these data suggest that local production of serum amyloid P and c-reactive protein in the alzheimer disease brain does not substantially contribute to the CSF levels. PMID: 20930309
Human SAP inhibits DNA-mediated innate immune activation in vitro and may limit innate and adaptive immune responses after DNA vaccination of transgenic mice. PMID: 21278351
serum SAP levels may be an easy detected predictor for the healing of burn wounds PMID: 20932823
Interaction between MBL and PTX3 led to communication between the lectin and classical complement pathways via recruitment of C1q, whereas SAP-enhanced complement activation occurs via a hitherto unknown mechanism PMID: 21106539
SAP has an effect on macrophages in fibrotic lung disease PMID: 20300636
Functional analysis demonstrated that SAP associated with HDL promotes SR-BI-dependent cholesterol efflux and lipid-free SAP enhances ABCA1-dependent cholesterol efflux PMID: 20189569
A possible role of SAP in either host resistance or viral virulence was investigated during influenza infection in vivo. Influenza virus infection is not affected by serum amyloid P component.Human SAP binds much more avidly than mouse SAP to the virus. PMID: 11984001
Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis. PMID: 12015594
serum amyloid P component does not circulate in complex with C4-binding protein, fibronectin or any other major protein ligand PMID: 12100475
structures of crystalline complexes of human serum amyloid P component with its carbohydrate ligand, the cyclic pyruvate acetal of galactose PMID: 12126626
Serum amyloid p component binds to late apoptotic cells and is involved in the phagocytosis of these cells by human monocyte-derived macrophages. PMID: 12528126
Serum amyloid P component binding to Shiga toxin 2 requires both a subunit and B pentamer. PMID: 14500533
Purified SAP inhibits fibrocyte differentiation at levels similar to those found in plasma, while depleting SAP reduces the ability of plasma to inhibit fibrocyte differentiation. PMID: 14607961
This protein, a non-fibrillar component, causes soluble fibrils to condense into localized fibrillar aggregates with a greatly enhanced local density of fibril entanglements. PMID: 15031287
Genetic variation in APCS is associated with amyloid polyneuropathy PMID: 15649951
Amyloid-associated SAP significantly increases fibrillar prion protein-related peptide-induced release of interleukin-6 and TNF-alpha from human microglia. PMID: 15837583
Review discusses clinical significance of different levels of SAP, its role in induction or protection from autoimmunity, and the presence of specific SAP autoantibodies in different autoimmune diseases. PMID: 16380821
the shared specificity as well as their shared capability to activate complement, suggest that IgM and the pentraxins CRP and SAP exert similar functions in the removal of apoptotic cells PMID: 16643876
Monocytes bound biotinylated serum amyloid P component with avidity in a dose-dependent and saturable manner; speculated that binding of SAP by monocytes could be of physiological relevance at extravascular sites by influencing complement regulation PMID: 16784490
Serum amyloid P (SAP) and C-reactive protein (CRP) may represent different facets of inflammation. The association of SAP with cardiovascular disease in these older adults further supports the role of innate immunity in atherosclerosis. PMID: 17138933
No reduced circulating concentrations of serum amyloid P component (SAP) in patients with systemic sclerosis, nor any evidence of an association between SAP levels and the extent or severity of fibrosis were observed. PMID: 17530641
SAP may modulate the inflammatory response to amyloid fibrils in atherosclerosis PMID: 17630380
SAP was quantitated using PVDF affinity probes and MALDI-MS. PMID: 17676666
The complex structure between human SAP and FcgammaRIIa reveals a diagonally bound receptor on each SAP pentamer with both D1 and D2 domains of the receptor contacting the ridge helices from two SAP subunits. PMID: 19011614
Our data suggest that measurement of cerebrospinal fluid SAP levels can aid in the identification of incipient Alzheimer's disease among mild cognitive impairment patients PMID: 19052452
Serum amyloid P binds to cells in the early stage of apoptosis, presumably via phosphatidylethanolamine exposed in flip-flopped membranes, suggesting a role for serum amyloid P in the clearance of these cells in vivo. PMID: 11441067

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.