Recombinant Proteins

p53
LBP
CEA
HLA
TCL
TTC
NPM
MAF
Bax
BID

C1QTNF3 Human

Complement C1q Tumor Necrosis Factor-Related Protein 3 Human Recombinant

C1QTNF3 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 234 amino acids and having a molecular mass of 25.4 kDa. The protein contains an extra 10 aa His tag at N-terminus. The C1QTNF3 amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q9BXJ4 amino acids 23–246. The C1QTNF3 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14421
Source
Escherichia Coli.
Appearance

C1QTNF4 Human

Complement C1q Tumor Necrosis Factor-Related Protein 4 Human Recombinant

C1QTNF4 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Leu17-Leu329) containing a total of 319 amino acids, having a calculated molecular mass of 34.5kDa and fused to a 6 aa His tag at C-Terminus.
Shipped with Ice Packs
Cat. No.
BT14474
Source
Escherichia Coli.
Appearance
Filtered colorless solution.

C1QTNF5 Human

Complement C1q Tumor Necrosis Factor-Related Protein 5 Human Recombinant

C1QTNF5 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 253 amino acids (16-243.a.a) and having a molecular mass of 26.4kDa. C1QTNF5 Human is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT14530
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

C1QTNF6 Human

Complement C1q Tumor Necrosis Factor-Related Protein 6 Human Recombinant

C1QTNF6 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 242 amino acids and having a molecular mass of 27 kDa. The protein contains an extra His tag at N-terminus. The C1QTNF6 amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q9BXI9 amino acids 29–259.
The C1QTNF6 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14639
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

C1QTNF7 Human

Complement C1q Tumor Necrosis Factor-Related Protein 7 Human Recombinant

C1QTNF7 Human Recombinant produced in E.Coli is a signle, non-glycosylated, Polypeptide chain containing 283 amino acids and having a molecular mass of 30.22 kDa. The protein contains an extra 10 amino acid His tag at N-terminus. The C1QTNF7 amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q9BXJ2 amino acids 17–289.
The C1QTNF7 is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT14690
Source
Escherichia Coli.
Appearance

Filtered White lyophilized (freeze-dried) powder.

C1QTNF8 Human

Complement C1q Tumor Necrosis Factor-Related Protein 8 Human Recombinant

C1QTNF8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 255 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 28.4kDa (calculated).
Shipped with Ice Packs
Cat. No.
BT15009
Source
Escherichia Coli.
Appearance
Filtered colorless solution.

C1QTNF9 Human

Complement C1q Tumor Necrosis Factor-Related Protein 9 Human Recombinant

C1QTNF9 Protein is a 33.7 kDa protein containing 324 aa fused to a 10 aa N-Terminal His-tag.
Shipped with Ice Packs
Cat. No.
BT15083
Source
E. coli
Appearance

C1R Human

Complement C1r Human

Human Complement C1r produced in Human plasma having a molecular mass of 92 kDa.

Shipped with Ice Packs
Cat. No.
BT15161
Source

Human Plasma.

Appearance

Sterile Filtered solution.

C1S Human

Complement C1s Human

Human Complement C1s produced in Human plasma having a molecular mass of 86 kDa.

Shipped with Ice Packs
Cat. No.
BT15232
Source

Human Plasma.

Appearance

Sterile Filtered solution.

C2 Human

Complement C2 Human

Human Complement C2 produced in Human plasma having a molecular mass of 93 kDa.

Shipped with Ice Packs
Cat. No.
BT15327
Source

Human Plasma.

Appearance

Sterile Filtered solution.

Definition and Classification

The complement system is a crucial part of the immune system, consisting of over 20 proteins that circulate in the blood and tissue fluids. These proteins are typically inactive but become sequentially activated in response to the recognition of molecular components of microorganisms . The complement system can be classified into three main pathways: the classical pathway, the alternative pathway, and the lectin pathway .

Biological Properties

Complement components are serum proteins that cooperate with both the innate and adaptive immune systems to eliminate pathogens . They are primarily synthesized by liver cells, but also by macrophages and other cell types . These proteins are heat-labile and glycosylated . They are distributed in various tissues and are present in the sera of all mammals, including humans, birds, amphibians, and fishes .

Biological Functions

The primary functions of complement components include opsonization, chemotaxis, and lysis of pathogens . They play a significant role in immune responses by enhancing the ability of antibodies and phagocytic cells to clear microbes and damaged cells . Complement components also promote inflammation and attack the pathogen’s cell membrane .

Modes of Action

Complement activation occurs through three pathways: the classical pathway, the lectin pathway, and the alternative pathway . Each pathway involves a series of proteolytic cleavages that activate complement proteins, leading to the formation of enzyme complexes such as C3 and C5 convertases . These complexes facilitate the binding of complement proteins to pathogens, promoting their opsonization and lysis . The membrane attack complex (MAC) is formed, which creates pores in the pathogen’s membrane, leading to cell lysis .

Regulatory Mechanisms

The complement system is tightly regulated to prevent damage to host tissues . Regulatory proteins, such as complement control proteins, interact with complement components to distinguish between self and non-self cells . These regulatory mechanisms include transcriptional regulation and post-translational modifications that control the expression and activity of complement proteins .

Applications

Complement components have various applications in biomedical research, diagnostic tools, and therapeutic strategies . They are used to study immune responses and develop treatments for autoimmune diseases and infections . Complement proteins are also utilized in diagnostic assays to detect immune deficiencies and monitor disease progression .

Role in the Life Cycle

Throughout the life cycle, complement components play a vital role in maintaining immune homeostasis . They are involved in the clearance of apoptotic cells and immune complexes, which is essential for preventing autoimmune diseases . Complement activity is crucial from development to aging, as it helps protect against infections and supports tissue repair .

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