Search results

The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.

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.

TRIM21 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The 52 kDa Ro protein is part of the RoSSA ribonucleoprotein, which includes a single polypeptide and one of four small RNA molecules. The RoSSA particle localizes to both the cytoplasm and the nucleus. Ro/SSA interacts with autoantigens in patients with Sjogren syndrome and systemic lupus erythematosus. Ribonucleoprotein particle is composed of a single polypeptide and one of four small RNA molecules. The RoSSA is present in all mammalian cells studied but has no known function. At least 2 isoforms are present in nucleated and red blood cells, and tissue specific differences in Ro/SSA proteins were identified.

Mortality factor 4-like protein 1 (MORF4L1) is a member of the MRG family. MORF4L1 is a component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes mostly by acetylation of nucleosomal histones H4 and H2A. MORF4L1 is a transcription factor expressed in various human tissues, and its orthologs have been found in many other eukaryotes which comprise the MRG protein family. The C-terminal part of MORF4L1 forms a conserved MRG domain that is involved in interactions with the tumor suppressor protein retinoblastoma and a nucleoprotein.

GPN-loop GTPase 1 (GPN1) is a member of the GPN-loop GTPase family. GPN1 is a guanosine triphosphatase enzyme which has a role in DNA repair and may function in activation of transcription. Small GTPases, which share a biochemical mechanism, act as binary molecular switches and function in the cell is nucleocytoplasmic transport of both proteins and RNA. In addition, GPN1 establishs an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, proposing that it is essential to connect RNA polymerase II to regulators of protein complex formation. GPN1 may also be involved in nuclear localization of XPA.

Matrix metalloproteinases are a family of zinc and calcium-dependent endopeptidases that break down extracellular matrix proteins. The MMP9 is secreted as a 92kDa zymogen. Cleavage of ProMMP-9 results in the active enzyme, having a molecular weight of approximately 82kDa. MMP9 is composed of the following domains: a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. MMP9 is produced by the several cell types: monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts and endothelial cells. MMP9 is involved in inflammatory responses, tissue remodeling, wound healing, tumor growth and metastasis. MMP9 may also play an important part in local proteolysis of the extracellular matrix and in leukocyte migration, as well as in bone osteoclastic resorption. MMP9 cleaves type IV and type V collagens into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. MMP9 can also degrade fibronectin but not laminin or Pz-peptide.
MMP9 defects may be a cause of susceptibility to intervertebral disc disease (IDD), also known as lumbar disk herniation (LDH).

ATF1, a cyclic-AMP dependent transcription factor, is expressed in a large selection of cell types and can dimerize with CREB. MSK1 and MSK2 protein kinases are essential for the stress-induced phosphorylation of transcription factors CREB and ATF1 in primary embryonic fibroblasts. Epidermal growth factor induction of c-jun expression needs ATF1 and MEF2 sites in the c-jun promoter.

Tropomyosin beta chain isoform 2 is affiliate to the actin filament binding protein family which primarily expressed in slow, type 1 muscle fibers. Mutations in TPM2 can change the expression of other sarcomeric tropomyosin proteins, and cause cap disease, nemaline myopathy and distal arthrogryposis syndromes.

40S ribosomal protein S5 (RPS5) is a ribosomal protein, which is a member of the ribosomal protein S7P family.Ribosomes, which are the organelles that catalyze protein synthesis, composed of a small subunit and a large subunit that comprise of over 80 distinct ribosomal proteins. RPS5 is a 204 amino acid component of the 40S complex. RPS5 proteins exist as multiple processed pseudogenes which are scattered throughout the genome. RPS5 is expressed at varying amounts in colorectal cancer cells, proposing a possible role in carconigenesis.

HEPACAM2 is necessary during prometaphase for centrosome maturation. Following poly-ADP-ribosylation (PARsylation) by TNKS, HEPACAM2 translocates from the Golgi apparatus to mitotic centrosomes and takes a significant part in the formation of robust microtubules for quick movement of chromosomes.

Phosphoglycerate kinase 1, also referred to PGK1, is an X-linked enzyme whichfunctions in the glycolytic pathway.The gene encoding the erythrocyte enzyme PGK1 & it seems that PGK-1 plays a role as a polymerase alpha cofactor protein (primer recognition protein) as a glyxolytic enzyme role. The PGK1 catalyzes the reversible conversion of 1, 3-diphosphoglycerate to 3-phosphoglycerate during glycolysis, generating one molecule of ATP.

Lysosomal-Associated Membrane Protein 3, also known as LAMP3 is part of the lysosome-associated membrane protein family. LAMP3 and CD68 share an extremely similar predicted structure. LAMP3 performs in dendritic cell function and in adaptive immunity as well. Furthermore, LAMP3 overexpression is actively involved in tumor invasion via increased migration into lymph-vascular spaces.

Ribosomal Protein 4X (RPS4X) is ribosomal protein S4, a component of the 40S subunit which is a part from the S4E family of ribosomal proteins. Ribosomal protein S4 is the only ribosomal protein known to be encoded by more than one gene, that is RPS4X and ribosomal protein S4, Y-linked (RPS4Y). Both isoforms encoded by these genes are not the same, but are functionally alike.

AP-3 complex subunit sigma-1 (AP3S1) belongs to the AP-3 complex, an adapter-related complex which is not clathrin-associated. AP3S1 is linkd with the Golgi region in addition to more peripheral structures. AP3S1 facilitates the budding of vesicles from the Golgi membrane and involved in trafficking to lysosomes.

DR1 is a phosphoprotein that inhibits both basal and activated levels of transcription. DR1 is phosphorylated in vivo which affects its interaction with TBP. DR1 has a histone fold motif at the amino terminus, a TBP-binding domain, and a glutamine- and alanine-rich region. By selectively repressing polymerases II and III, DR1 alters the physiological balance of transcriptional output in favor of polymerase I.

NSL1 holds two coiled-coil domains.NSL1 proteins, localized to kinetochores - chromosome associated structures which attach to microtubules and mediate chromosome movements throughout cell division. NSL1 is a fragment of a conserved protein complex that hold two chromodomain-containing proteins and a component of the outer plate of the kinetochore. NSL1 connect centromeric heterochromatin with the outer kinetochore structure. Several transcript variants are known to encod different isoforms for this gene.

U6 snRNA-associated Sm-like protein LSm1 (LSM1) has a role in replication-dependent histone mRNA degradation and binds specifically to the 3''-terminal U-tract of U6 snRNA. Sm-like proteins include the Sm sequence motif, which consists of two regions separated by a linker of variable length that folds as a loop. The LSM1 protein facilitates RNA protein interactions and structural modifications which are required during ribosomal subunit assembly. The Sm-like proteins are believed to form a stable heteromer present in tri-snRNP particles, which are vital for pre-mRNA splicing. LSM1 is overexpressed in pancreatic cancer as well as in several breast cancer cell lines.

C3 is central to the activation of all 3 pathways of complement activation. Initiation of each pathway generates proteolytic enzyme complexes which binds the target surface. These enzymes cleave a peptide bond in C3 releasing the anaphylatoxin C3a and activating C3b. Most of the C3 activated during complement activation never attaches to the surface due to its thioester reaction with water forming fluid phase C3b which is rapidly inactivated by factors H and I forming iC3b. Surface-bound C3b is necessary in all 3 pathways for efficient activation of C5 and formation of C5b-9 complexes that lyse the target cell membrane.

The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are stable secretory proteins expressed in the gastrointestinal tract (gastric mucosa), and are involved in intestinal mucosal defense and repair. TFF1 is an essential protein for normal differentiation of the antral and pyloric gastric mucosa and functions as a gastric-specific tumor suppressor gene. TFF1 is a stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. TFF1 protects the mucosa from isults, stabilizes the mucus layer, & affects healing of the epithelium. TFF1 is commonly expressed in tumors. TFF1 is related with the cell membrane of MCF-7 cells. High levels of TFF1 and TFF2 are found in serum from inflammatory bowel disease.

SPIN1 is a member of the SPIN/STSY family. SPIN1 is localized to nucleus, and expressed in several tissues and cells. SPIN1 takes part in cell-cycle regulation in the course of the transition from gamete to embryo.

ARL6 is a member of the ARF family of GTP-binding proteins. ARL6 has a vital part in modulating membrane trafficking and cytoskeletal functions. Mutation in ARL6 is the source of Bardet-Biedl syndrome (BBS3) which is a pleiotropic genetic disorder that causes obesity, photoreceptor degeneration, polydactyly, hypogenitalism, renal abnor-malities and developmental delay.

PRKAG1 is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer comprised of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is a vital energy-sensing enzyme which supervises cellular energy status. PRKAG1 is one of the gamma regulatory subunits of AMPK. Alternatively spliced transcript variants encoding dissimilar isoforms were found.