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The recombinant Protein A/G is a genetically engineered protein comprised of 7 IgG-binding domains EDABC-C1C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.

Fatty acid binding protein 9 (FABP9) belongs to the fatty acid-binding proteins (FABPs) which are a family of small, extremely conserved, cytoplasmic proteins to bind long-chain fatty acids and other hydrophobic ligands. FABP9 is found in midpachytene spermatocytes and round spermatids, and comprises part of the perinuclear theca. FABP9 probably links intracellular membranes and signals abnormal sperm formation during spermatogenesis.

Developmentally-regulated GTP-binding protein 1 (DRG1) is a member of the GTP1/OBG family. DRG1 has a role in cell proliferation and differentiation, as well as in apoptosis, proposing a role in tumor formation and metastasis. Expression of the DRG1 was considerably reduced in breast tumor cells, particularly in patients with lymph node or bone metastasis as compared to those with localized breast cancer. The DRG1 protein is expressed at high levels in the heart, kidney and skeletal muscle and at lower levels in the brain, liver, placenta, lung, colon and spleen.

FK506 Binding Protein 5 (FKBP5) belongs to the immunophilin protein family, which has a role in immunoregulation and basic cellular processes involving protein folding and trafficking. FKBP5 is a cis-trans prolyl isomerase, which binds to the immunosuppressants FK506 and rapamycin. FKBP5 is an immunophilin protein with PPIase and co-chaperone activities. FKBP5 is assumed to mediate calcineurin inhibition. FKBP5 is a component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). In addition, FKBP5 interacts functionally with mature hetero-oligomeric progesterone receptor complexes along with the 90 kDa heat shock protein and P23 protein.

Reticulocalbin-2 (RCN2) is a member of the CREC protein family. RCN2 is a calcium-binding protein found in the lumen of the ER. RCN2 contains 6 conserved regions with similarity to a high affinity Ca(+2)-binding motif, the EF-hand.

RAET1E is a member of the MHC class I family. MHC class I family contains main histocompatibility complex (MHC) class I-related genes positioned in a cluster on chromosome 6q24.2-q25.3. RAET1E and RAET1G protein are different from other RAET1 proteins since they have type I membrane-spanning sequences at their C termini instead glycosylphosphatidylinositol anchor sequences.RAET1E acts as a ligand for NKG2D receptor, expressed on the surface of numerous types of immune cells, involves in innate adaptive immune reactions.RAET1E delivers signals to NK cells and advances tumor immune surveillance by inducing the growth of anti-tumor cytotoxic lymphocyte.

S100A3 is part of S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm/nucleus of a broad range of cells, and takes part in the regulation of several cellular processes such as cell cycle progression and differentiation. S100A3 has the largest number of cysteines of all S100 proteins. S100A3 has high affinity for Zinc, and is widely expressed in human hair cuticle.

Alpha & Gamma-Adaptin Binding Protein (AAGAB), which is also known as P34, takes part in membrane traffic and interacts with AP1G1 and AP2A1.AAGAB is highly expressed in skin and keratinocytes, with the highest levels in adrenal gland, rectum and thymus.

Complement Component 4 Binding Protein, Beta (C4BPB) belongs to a superfamily of proteins composed primarily of tandemly arrayed short consensus repeats of approximately 60 amino acids. C4BPB has a regulatory role in the coagulation system also, mediated via the beta-chain binding of protein S, a vitamin K-dependent protein which functions as a cofactor of activated protein C. A single, unique beta-chain of the C4BPB assembles with 7 identical alpha-chains into the principal isoform of C4BPB, which is a multimeric protein that controls activation of the complement cascade via the classical pathway. C4BPB binds as a cofactor to C3b/C4b inactivator (C3bINA), which subsequently hydrolyzes the complement fragment C4b. In addition, C4BPB accelerates the degradation of the C4bC2a complex (C3 convertase) by detaching the complement fragment C2a. Furthermore, C4BPB interacts with anticoagulant protein S and with serum amyloid P component.

FKBP4 is part of the immunophilin protein family, which takes part in immunoregulation and necessary cellular processes concerning protein folding and trafficking. FKBP4 is a cis-trans prolyl isomerase that connects to the immunosuppressants FK506 and rapamycin. FKBP4 has high structural and functional similarity to FKBP1A, though, FKBP4 does not have immunosuppressant activity when complexed with FK506. FKBP4 is known to connect with phytanoyl-CoA alpha-hydroxylase. FKBP4 associates with HSP90 & HSP70 thus takes part in the intracellular trafficking of hetero-oligomeric forms of the steroid hormone receptors. FKBP4 highly associates with adeno-associated virus type 2 vectors (AAV) resulting in a considerable increase in AAV-mediated transgene expression in human cell lines. FKBP4 is involved in the optimal use of AAV vectors in human gene therapy.

Mannose-binding protein C (MBL2),belongs to the collectin family of patternrecognition molecules and is an important component in the innate immune system. MBL2 is a secreted glycoprotein which recognizes mannose and N-acetylglucosamine on various microorganisms, and is capable of activating the classical complement pathway. Lacking MBL2 has been associated with susceptibility to autoimmune and infectious diseases.

S100G (calbindin D9K) is a vitamin D-dependent calcium-binding protein. S100G, which is a cytosolic protein, is a member of a family of calcium-binding proteins that includes calmodulin, parvalbumin, troponin C, and S100 protein. In the intestine, S100G is vitamin D-dependent and its expression correlates with calcium transport activity. S100G may increase Ca2+ absorption by buffering Ca2+ in the cytoplasm and increase ATP-dependent Ca2+ transport in duodenal basolateral membrane vesicles.

Bestrophin 1 (BEST1) is a part of the bestrophin gene family and is also forms calcium-activated chloride-ion channels in epithelial. This small gene family is characterized by proteins with a highly conserved N-terminus with 4-6 transmembrane domains. BEST1 is extremely permeable to bicarbonate.

IGFBP6 plays a role in lipoprotein assembly and dietary cholesterol absorption. in addition to its acyltransferase activity, it may act as a ligase. may provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa.

S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

IGFBP5 is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein forms a ternary complex with insulin-like growth factor acid-labile subunit (IGFALS) and either insulin-like growth factor (IGF) I or II. In this form, it circulates in the plasma, prolonging the half-life of IGFs and altering their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

S100A1 is a member of the S100 family of calcium binding proteins with EF-hand type Ca+2 binding motive. S100A1 (Calcium Binding Protein A1) is involved in the activation of sarcoplasmatic calcium release and the regulation of intermediate filament polymerization. S100A1 may function in stimulation of Ca2+-induced Ca2+ release, inhibition of microtubule assembly, and inhibition of protein kinase C-mediated phosphorylation. Reduced expression of S100A1 has been implicated in cardiomyopathies.
S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21.

RNA Binding Motif Protein 11 (RBM11) which contains 1 RNA recognition motif is a part of the RBM family. The RBM gene family encodes proteins with an RNA binding motif which participate in the modulation of apoptosis. RBM11 is expressed in testis, kidney, spleen, brain, spinal cord and mammary gland and can be found as 2 isoforms produced by alternative splicing.

Guanine Nucleotide Binding Protein Gamma 11 (GNG11) which belongs to the guanine nucleotide-binding protein (G protein) gamma family encodes a lipid-anchored, cell membrane protein. G proteins act as a modulator or transducer in various transmembrane signaling systems. GNG11 is also subject to carboxyl-terminal processing.

S100A6 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21.
S100A6 may function in stimulation prolactin secretion, and exocytosis. Chromosomal rearrangements and altered expression of the S100A6 gene are implicated in melanoma.

Nuclear receptor binding factor 2 (NRBF2) which works as transcriptional activator, modulates transcriptional activation by target nuclear receptors.

Reticulocalbin 3 (RCN3) belongs to the CREC (cab45/reticulocalbin/ ERC45/calumenin) family. RCN3 contains 5 Arg-Xaa-Xaa-Arg motifs, which function as target sequences of SPCs (subtilisin-like proprotein convertases), which is a family of serine endoproteases that proteolytically activate proproteins. The synthesis of PACE4 is induced by association and coexpression with RCN3.

RLBP1 is a 36-kD water-soluble protein that transports 11-cis-retinal or 11-cis-retinaldehyde as physiologic ligands. RLBP1 is a functional element of the visual cycle. RLBP1 gene mutations cause retinitis punctata albescens, severe rod-cone dystrophy and Bothnia dystrophy (nonsyndromic autosomal recessive retinitis pigmentosa).