Other Monoclonal Antibodies

AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.

Proteasomal ubiquitin receptor ADRM1 (ADRM1) functions as a proteasomal ubiquitin receptor. ADRM1 is an integral plasma membrane protein which promotes cell adhesion. ADRM1 is assumed to undergo O-linked glycosylation. ADRM1 gene expression is induced by gamma interferon in some cancer cells. ADRM1 employs the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.

SAR1B is a small GTPase that functions as a homodimer. GTP-Binding Protein SAR1B (SAR1b) is involved in transport from the endoplasmic reticulum to the Golgi apparatus and also in the selection of the protein cargo and the assembly of the COPII coat complex. The SAR1B protein is activated by the guanine nucleotide exchange factor PREB. SAR1B gene defects are a cause of chylomicron retention disease (CMRD), also known as Anderson disease (ANDD).

ACTN1 encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene. Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.

Actin Beta (ACTB) is one of 6 different actin isoforms which have been identified in humans. ACTB is one of the 2 nonmuscle cytoskeletal actins. Actins are highly conserved proteins which are involved in cell motility, structure and integrity. Alpha actins are a key component of the contractile apparatus.

Actin is one of the most highly-conserved proteins, differing by no more than 20% in species as diverse as algae and humans .Actin or ACTA is aprotein localized in the I band of the myofibrils in the muscle, Acting together with myosin.Actin takes part in the contraction and relaxation of muscle. Actin exists as a monomer in low salt concentrations, but filaments form rapidly as salt concentration rises, with the consequent hydrolysis of ATP.Each actin protomer binds one molecule of ATP and has one high affinity site for either calcium or magnesium ions, as well as several low affinity sites. It occurs in globular (G-actin) and fibrous (F-actin) forms. Actin is found in all eukaryotic cells (except for nematode sperm). Its other activitiessuch as cell motility, cell division and cytokinesis, vesicle and organelle movement, cell signaling, and the establishment and maintenance of cell junctions and cell shape.

CtBP was initially known as a cellular protein which cooperates with a C-terminal motif of adenovirus E1A oncoproteins. C-terminal-binding protein is extremely conserved in higher eukaryotes. Vertebrates hold two highly homologous CtBP proteins (CtBP1 and CtBP2) while invertebrates h a single CtBP. CtBP family proteins has a significant sequence homology with D-2-hydroxy acid dehydrogenases. In addition, CtBP proteins cooperates with numerous proteins and functions as a co-repressor of transcription.

Type 1 cystatins are also called stefins which function as intracellular thiol protease inhibitors. Cystatin-B protein is able to form a dimer stabilized by noncovalent forces, inhibiting papain and cathepsins l, h and b. CSTB protein protects proteases leakage from lysosomes. Mutations in Stefin-B gene cause primary defects in patients with progressive myoclonic epilepsy (EPM1), a degenerative disease of the central nervous system. CSTB is overexpressed & elevated in the serum of HCC patients. Cystatin-B in vivo has a polymeric structure which is sensitive to the redox environment. Cystatin-B inhibits bone resorption by down-regulating intracellular cathepsin K activity despite increased osteoclast survival. Protein and mRNA levels of stefin B are significantly lower in atypical benign meningiomas. Stefins-A & Stefin-B which belong to the type-1 Cystatins, are up-regulated in lung tumours and thus able to counteract harmful tumour-associated proteolytic activity. Human stefin-A & Stef

Cystatin-A is the intracellular inhibitor of cysteine proteinase cathepsin B (CatB) and belongs to family 1 of the cystatin superfamily of inhibitor proteins. CSTA is a stefin that functions as a cysteine protease inhibitor, forming tight complexes with papain and the cathepsins B, H, and L. It has been proposed that extracellular CatB together with other classes of proteinases are all subjected to a cascade-like manner of activation. CatB and its inhibitor Cystatin-A are involved in degradation of extracellular matrix proteins during tissue remodeling. CSTA is one of the precursor proteins of cornified cell envelope in keratinocytes and plays a role in epidermal development and maintenance. Cystatin-A has been reported to be found in high concentrations in epithelial cells, polymorphonuclear leukocytes and lymphoid tissue. Stefins may be used as prognostic and diagnostic tools for cancer.

S100A4 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 belongs to the family of calcium binding proteins such as calmodulin and troponin C. S100A is composed of an alpha and beta chain whereas S100B is composed of two beta chains. S100 protein is also expressed in the antigen presenting cells such as the Langerhans cells in skin and interdigitating reticulum cells in the paracortex of lymph nodes. 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. S100A4 may function in motility, invasion, and tubulin polymerization. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. Chromosomal rearrangements and altered expression of the S100A4 gene have been implicated in tumor metastasis.

S100A11 is a member of the S100 family of proteins which contains two EF-hand calcium-binding motifs and is thought to be involved in the regulation of a number of cellular processes including cell cycle progression and differentiation. S100A11 may function in motility, invasion and tubulin polymerisation. 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. Chromosomal rearrangements and altered expression of S100A11 have been implicated in tumor metastasis.

MHC Class II is consists of 2 membrane spanning proteins. Each of these proteins is roughly 30 kDa, and has of two Globular domains, Alpha-1, Alpha-2, Beta-1 and Beta-2. The two regions farthest away from the membrane are alpha-1 and beta-1. The two proteins link without Covalent Bonds. The MHC Class II protein mainly presents peptides, which have been digested from external sources. MHC Class II is normally only expressed by Antigen Presenting Cells (APC) which digest foreign protein. Within the RER the alpha and beta proteins of the molecule, associate with each other, while a third protein called the "invariant chain," is necessary for stabilizing the complex, without it, they will not associate. The MHC-invariant complex is then passed from the RER, into and out of, the Golgi body. It fuses with an Endocytic compartment, where an external protein has been sampled and degraded.

HC Class II is consists of 2 membrane spanning proteins. Each of these proteins is roughly 30 kDa, and has of two Globular domains, Alpha-1, Alpha-2, Beta-1 and Beta-2. The two regions farthest away from the membrane are alpha-1 and beta-1. The two proteins link without Covalent Bonds. The MHC Class II protein mainly presents peptides, which have been digested from external sources. MHC Class II is normally only expressed by Antigen Presenting Cells (APC) which digest foreign protein. Within the RER the alpha and beta proteins of the molecule, associate with each other, while a third protein called the "invariant chain," is necessary for stabilizing the complex, without it, they will not associate. The MHC-invariant complex is then passed from the RER, into and out of, the Golgi body. It fuses with an Endocytic compartment, where an external protein has been sampled and degraded.

MHC Class II is consists of 2 membrane spanning proteins. Each of these proteins is roughly 30 kDa, and has of two Globular domains, Alpha-1, Alpha-2, Beta-1 and Beta-2. The two regions farthest away from the membrane are alpha-1 and beta-1. The two proteins link without Covalent Bonds. The MHC Class II protein mainly presents peptides, which have been digested from external sources. MHC Class II is normally only expressed by Antigen Presenting Cells (APC) which digest foreign protein. Within the RER the alpha and beta proteins of the molecule, associate with each other, while a third protein called the "invariant chain," is necessary for stabilizing the complex, without it, they will not associate. The MHC-invariant complex is then passed from the RER, into and out of, the Golgi body. It fuses with an Endocytic compartment, where an external protein has been sampled and degraded.

MHC Class II is consists of 2 membrane spanning proteins. Each of these proteins is roughly 30 kDa, and has of two Globular domains, Alpha-1, Alpha-2, Beta-1 and Beta-2. The two regions farthest away from the membrane are alpha-1 and beta-1. The two proteins link without Covalent Bonds. The MHC Class II protein mainly presents peptides, which have been digested from external sources. MHC Class II is normally only expressed by Antigen Presenting Cells (APC) which digest foreign protein. Within the RER the alpha and beta proteins of the molecule, associate with each other, while a third protein called the "invariant chain," is necessary for stabilizing the complex, without it, they will not associate. The MHC-invariant complex is then passed from the RER, into and out of, the Golgi body. It fuses with an Endocytic compartment, where an external protein has been sampled and degraded.

MHC Class II is consists of 2 membrane spanning proteins. Each of these proteins is roughly 30 kDa, and has of two Globular domains, Alpha-1, Alpha-2, Beta-1 and Beta-2. The two regions farthest away from the membrane are alpha-1 and beta-1. The two proteins link without Covalent Bonds. The MHC Class II protein mainly presents peptides, which have been digested from external sources. MHC Class II is normally only expressed by Antigen Presenting Cells (APC) which digest foreign protein. Within the RER the alpha and beta proteins of the molecule, associate with each other, while a third protein called the "invariant chain," is necessary for stabilizing the complex, without it, they will not associate. The MHC-invariant complex is then passed from the RER, into and out of, the Golgi body. It fuses with an Endocytic compartment, where an external protein has been sampled and degraded.

MHC Class II is consists of 2 membrane spanning proteins. Each of these proteins is roughly 30 kDa, and has of two Globular domains, Alpha-1, Alpha-2, Beta-1 and Beta-2. The two regions farthest away from the membrane are alpha-1 and beta-1. The two proteins link without Covalent Bonds. The MHC Class II protein mainly presents peptides, which have been digested from external sources. MHC Class II is normally only expressed by Antigen Presenting Cells (APC) which digest foreign protein. Within the RER the alpha and beta proteins of the molecule, associate with each other, while a third protein called the "invariant chain," is necessary for stabilizing the complex, without it, they will not associate. The MHC-invariant complex is then passed from the RER, into and out of, the Golgi body. It fuses with an Endocytic compartment, where an external protein has been sampled and degraded.

MHC Class II is consists of 2 membrane spanning proteins. Each of these proteins is roughly 30 kDa, and has of two Globular domains, Alpha-1, Alpha-2, Beta-1 and Beta-2. The two regions farthest away from the membrane are alpha-1 and beta-1. The two proteins link without Covalent Bonds. The MHC Class II protein mainly presents peptides, which have been digested from external sources. MHC Class II is normally only expressed by Antigen Presenting Cells (APC) which digest foreign protein. Within the RER the alpha and beta proteins of the molecule, associate with each other, while a third protein called the "invariant chain," is necessary for stabilizing the complex, without it, they will not associate. The MHC-invariant complex is then passed from the RER, into and out of, the Golgi body. It fuses with an Endocytic compartment, where an external protein has been sampled and degraded.

MHC Class I is a membrane spanning molecule consisting of 2 proteins. MHC Class I is just about 350 amino acids in length, with roughly 75 amino acids at the carboxylic end comprising the transmembrane and cytoplasmic portions. The remaining 270 amino acids, are divided into three globular domains labeled Alpha-1, Alpha-2 and Alpha-3 prime, with Alpha-1 being closest to the amino terminus and Alpha-3 closest to the membrane. The second portion of the molecule is a small globular protein called Beta-2 Microglobulin. It links primarily with the Alpha-3 prime domain and is essential for MHC stability.
The MHC ability to show a vast range of antigenic peptides for T cell recognition needs a compromise between broad specificity and high affinity. Both MHC class I and MHC class II show an exceptional structure while the peptide main chain is tightly bound and peptide side chains show less restrictive interactions. It is primarily the peptide side-chain contacts and conformational variability that ensures that the peptide-MHC complex presents an antigenically unique surface to T cell receptors.

MHC Class I is a membrane spanning molecule consisting of 2 proteins. MHC Class I is just about 350 amino acids in length, with roughly 75 amino acids at the carboxylic end comprising the transmembrane and cytoplasmic portions. The remaining 270 amino acids, are divided into three globular domains labeled Alpha-1, Alpha-2 and Alpha-3 prime, with Alpha-1 being closest to the amino terminus and Alpha-3 closest to the membrane. The second portion of the molecule is a small globular protein called Beta-2 Microglobulin. It links primarily with the Alpha-3 prime domain and is essential for MHC stability.
The MHC ability to show a vast range of antigenic peptides for T cell recognition needs a compromise between broad specificity and high affinity. Both MHC class I and MHC class II show an exceptional structure while the peptide main chain is tightly bound and peptide side chains show less restrictive interactions. It is primarily the peptide side-chain contacts and conformational variability that ensures that the peptide-MHC complex presents an antigenically unique surface to T cell receptors.

MHC Class I is a membrane spanning molecule consisting of 2 proteins. MHC Class I is just about 350 amino acids in length, with roughly 75 amino acids at the carboxylic end comprising the transmembrane and cytoplasmic portions. The remaining 270 amino acids, are divided into three globular domains labeled Alpha-1, Alpha-2 and Alpha-3 prime, with Alpha-1 being closest to the amino terminus and Alpha-3 closest to the membrane. The second portion of the molecule is a small globular protein called Beta-2 Microglobulin It links primarily with the Alpha-3 prime domain and is essential for MHC stability.
The MHC ability to show a vast range of antigenic peptides for T cell recognition needs a compromise between broad specificity and high affinity. Both MHC class I and MHC class II show an exceptional structure while the peptide main chain is tightly bound and peptide side chains show less restrictive interactions. It is primarily the peptide side-chain contacts and conformational variability that ensures that the peptide-MHC complex presents an antigenically unique surface to T cell receptors.

Acetoacetyl-CoA thiolase (ACAT1) is an enzyme member of the membrane-bound acyltransferase family and Sterol o-acyltransferase subfamily. The ACAT1 enzyme catalyzes the reversible formation of acetoacetyl-CoA from 2 molecules of acetyl-CoA. ACAT1 plays a part in lipoprotein compilation and dietary cholesterol absorption. Added to its acyltransferase activity, ACAT1 acts as a ligase.

RUVBL1 is part of NuA4 histone acetyltransferase complex which participates in transcriptional activation of specific genes mainly by acetylation of nucleosomal histone H4 and H2A. This complex is essential for the activation of transcriptional programs associated with oncogene and proto oncogene mediated growth induction, tumor suppressor mediated growth arrest.

Microfibrillar-associated protein 4 (MFAP4) is a member of Fibrinogen protein family and contains 1 fibrinogen C-terminal domain. The MFAP4 protein has similarity to a bovine microfibril-associated protein. MFAP4 has binding specificities for both collagen and carbohydrate. MFAP4 is believed to be an extracellular matrix protein that is involved in cell adhesion or intercellular interactions. MFAP4 deletion was found in 30 of 31 Smith-Magenis syndrome (SMS) patients.

Human chorionic gonadotropin (hCG) is a peptide hormoneproduced in pregnancy, that is made by the embryosoon after conceptionand later by the syncytiotrophoblast(part of the placenta). Its role is to prevent the disintegration of the corpus luteumof the ovaryand thereby maintain progesteroneproduction that is critical for a pregnancyin humans. hCG may have additional functions, for instance it is thought that it affects the immune tolerance of the pregnancy. Early pregnancy testinggenerally is based on the detection or measurement of hCG.

CRP is an acute phase protein that correlates with inflammatory disease and is synthesized by hepatocytes during the acute phase response by certain cytokines (IL-1 and TNF Alpha and Beta). CRP levels increase dramatically (up to 1,000 fold) and serve as a useful marker of inflammation in such conditions as bacterial infection, rheumatoid arthritis, viral infections, transplantation rejection, meningitis, myocardial infarction, septicemia, osteomyelitis and others. CRP is also highly correlated to Serum Amyloid A levels.

Mediator of ErbB2-driven cell motility 1 (MEMO1) is a member of the UPF0103 family. MEMO1 regulates cell migration by transmitting extracellular chemotactic signals to the microtubule cytoskeleton. Furthermore, MEMO1 controls the localization of APC and CLASP2 to the cell membrane, using the regulation of GSK3B activity. MEMO1 is essential for breast carcinoma cell migration, suggesting a key role in tumorigenesis. MEMO1 is also a mediator of ERBB2 signaling.