Recombinant Human Complement Component C9 (C9) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-07024P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Complement Component C9 (C9) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-07024P
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Product Overview

Description Recombinant Human Complement Component C9 (C9) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P02748
Target Symbol C9
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His&C-Myc
Target Protein Sequence QYTTSYDPELTESSGSASHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRCTDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLRCNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGYGINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWNVASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAAISLKFTPTETNKAEQCCEETASSISLH
Expression Range 22-265aa
Protein Length Partial
Mol. Weight 35.3 kDa
Research Area Immunology
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 Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C9 is the pore-forming subunit of the MAC.
Subcellular Location Secreted. Target cell membrane; Multi-pass membrane protein.
Protein Families Complement C6/C7/C8/C9 family
Database References
Associated Diseases Complement component 9 deficiency (C9D); Macular degeneration, age-related, 15 (ARMD15)
Tissue Specificity Plasma (at protein level).

Gene Functions References

  1. The data supports the assumption that C9 gene expression may stimulate the expression of inflammatory (NLRP3) and angiogenic growth factors (VEGF) in retinal pigment epithelial cells. PMID: 30090015
  2. Serum-expressed apolipoprotein B-100 protein, C9 Complement, and gelsolin can be used for differential diagnosis of Barrertts esophagus and adenocarcinoma of esophagus. PMID: 26404905
  3. Data indicate that complement C9 binds to the ATPase domain of mortalin. PMID: 24719326
  4. Liver biopsy specimens from chronically hepatitis C virus-infected patients exhibited a lower level of C9 mRNA expression than liver biopsy specimens from unrelated disease or healthy control human liver RNA. PMID: 23487461
  5. the haploinsufficiency of C9, a terminal complement complex component, engenders reduced intraocular secretion of VEGF and decreased risk for CNV development. PMID: 22190594
  6. C9 and fucosylated form could serve as a useful marker for SQLC. PMID: 21840429
  7. It was concluded that variations in the complement component 9 gene are unlikely to influence clearance of chronic hepatitis B virus infection and hepatocellular carcinoma occurrence. PMID: 21380615
  8. Mapping the intermedilysin-human CD59 receptor interface reveals a deep correspondence with the binding site on CD59 for complement binding proteins C8alpha and C9. PMID: 21507937
  9. These results suggested that the lack of membrane attack complex because of an Arg95Stop mutation of the complement component 9 gene predisposed patients to pathognomonic glomerulonephritis. PMID: 21057849
  10. provided evidence for the recognition of membrane-bound C9 on complement-lysed ghosts by an antibody specific for the helix-turn-helix fold. PMID: 20153530
  11. Data show that mortalin supports cancer cell resistance to complement-dependent cytotoxicity and suggest consideration of mortalin as a novel target for cancer adjuvant immunotherapy. PMID: 19739077
  12. The human complement C9 gene: structural analysis of the 5' gene region and genetic polymorphism studies. PMID: 11881818
  13. C9 binding is dependent on the N-terminal modules (thrombospondin type 1 and low-density lipoprotein receptor class A) of C8 alpha together with the C8 alpha membrane attack complex/perforin domain. PMID: 12463754
  14. Founder effect was demonstrated for the R95X mutation of the C9 gene in Japanese PMID: 12596049
  15. results indicate that the principal binding site for C9 lies within the MACPF domain of C8alpha PMID: 16618117
  16. analysis of the CD59-C9 binding interaction PMID: 16844690

FAQs

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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.

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