stable

Toxin which activates the particulate form of guanylate cyclase and increases cyclic GMP levels within the host intestinal epithelial cells.

Toxin which activates the particulate form of guanylate cyclase and increases cyclic GMP levels within the host intestinal epithelial cells.

Toxin which activates the particulate form of guanylate cyclase and increases cyclic GMP levels within the host intestinal epithelial cells. Heat-stable enterotoxin ST-2 Protein, E. coli, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 2.0 kDa and the accession number is P01560.

GUCY2C Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-6xHis-Avi tag. The predicted molecular weight is 65-110 KDa and the accession number is P25092.

Human PAP, also known as 28 kDa heat- and acid-stable phosphoprotein, PDGF-associated protein, PDGFA-associated protein 1, PDAP1, HASPP28, is a protein which belongs to the PDAP1 family. The encoded protein in rodents has been shown to bind PDGFA with a low affinity. PDGF-Associated Protein (PAP) is a phosphoprotein that may enhance PDGFA-stimulated cell growth in fibroblasts, but inhibits the mitogenic effect of PDGFB. PDAP1 expression is induced by TNF-alpha, and cells overexpressing PDAP1 show significantly less apoptosis on exposure to TNF-alpha.

A DNA-binding protein implicated in transcriptional repression (silencing). Also involved in bacterial chromosome organization and compaction. H-NS binds tightly to AT-rich dsDNA and inhibits transcription. Binds upstream and downstream of initiating RNA polymerase, trapping it in a loop and preventing transcription. Binds to hundreds of sites, approximately half its binding sites are in non-coding DNA, which only accounts for about 10% of the genome. Many of these loci were horizontally transferred (HTG); this offers the selective advantage of silencing foreign DNA while keeping it in the genome in case of need. Suppresses transcription at many intragenic sites as well as transcription of spurious, non-coding RNAs genome-wide. Repression of HTG by H-NS is thought to allow their DNA to evolve faster than non-H-NS-bound regions, and facilitates integration of HTG into transcriptional regulatory networks. A subset of H-NS/StpA-regulated genes also require Hha (and/or Cnu, ydgT) for repression; Hha and Cnu increase the number of genes DNA bound by H-NS/StpA and may also modulate the oligomerization of the H-NS/StpA-complex. The protein forms 2 clusters in the nucleoid which gather hns-bound loci together, bridging non-contiguous DNA, and causes DNA substantial condensation. Binds DNA better at low temperatures than at 37 degrees Celsius; AT-rich sites nucleate H-NS binding, further DNA-binding is cooperative and this cooperativity decreases with rising temperature. Transcriptional repression can be inhibited by dominant-negative mutants of StpA or itself. May effect transcriptional elongation. Can increase translational efficiency of mRNA with suboptimal Shine-Dalgarno sequences. Plays a role in the thermal control of pili and adhesive curli fimbriae production, by inducing transcription of csgD. Plays a role in flagellar function. Represses the CRISPR-cas promoters, permits only weak transcription of the crRNA precursor; its repression is antagonized by LeuO. Binds preferentially to the upstream region of its own gene recognizing two segments of DNA on both sides of a bend centered around -150. Overexpression suppresses secY24, a temperature-sensitive mutation. Has also been reported to activate transcription of some genes.

GUCY2C Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with C-Fc tag. The predicted molecular weight is 90-120 KDa and the accession number is P25092.

Toxin which activates the particulate form of guanylate cyclase and increases cyclic GMP levels within the host intestinal epithelial cells. Could play an important role in pathogenesis.

Receptor for the E.coli heat-stable enterotoxin (E.coli enterotoxin markedly stimulates the accumulation of cGMP in mammalian cells expressing GC-C). Also activated by the endogenous peptide guanylin. GUCY2C Protein, Rat, Recombinant (His & Myc) is expressed in HEK293 mammalian cells with N-10xHis and C-Myc tag. The predicted molecular weight is 51.4 kDa and the accession number is P23897.

CARHSP1 is a biomarker for diabetic complications. Adenovirus-mediated CARHSP1 overexpression and siRNA-mediated knockdown experiments were performed to characterize the role of CARHSP1 in the regulation of gluconeogenic gene expression. CARHSP1 is regulated by nutrient status in the liver and functions at the transcriptional level to negatively regulate gluconeogenic genes, including the glucose-6-phosphatase catalytic subunit (G6Pc) and phosphoenolpyruvate carboxykinase 1 (PEPCK1). In addition, it is found that CARHSP1 can physically interact with peroxisome proliferator-activated receptor-α (PPARα) and inhibit its transcriptional activity. Both pharmacological and genetic ablations of PPARα attenuate the inhibitory effect of CARHSP1 on gluconeogenic gene expression in hepatocytes.

CLEC12A has recently been identified as an antigen, expressed on leukemic stem cells and leukemic blasts. Given the fact that this expression profile seems stable throughout diagnosis, treatment and relapse on leukemic blasts and leukemic stem cells, CLEC12A can be considered a highly potent and reliable marker for the detection of measurable residual disease and therefore applicable for risk stratification and prognostication in AML. CLEC12A/MICL/CLL-1 Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with N-His tag. The predicted molecular weight is 24.6 kDa and the accession number is A0A2K5WXQ6.

CLEC12A has recently been identified as an antigen, expressed on leukemic stem cells and leukemic blasts. Given the fact that this expression profile seems stable throughout diagnosis, treatment and relapse on leukemic blasts and leukemic stem cells, CLEC12A can be considered a highly potent and reliable marker for the detection of measurable residual disease and therefore applicable for risk stratification and prognostication in AML. CLEC12A/MICL/CLL-1 Protein, Mouse, Recombinant (aa 65-267, His) is expressed in HEK293 mammalian cells with N-His tag. The predicted molecular weight is 24.9 kDa and the accession number is Q504P2-1.

CLEC12A has recently been identified as an antigen, expressed on leukemic stem cells and leukemic blasts. Given the fact that this expression profile seems stable throughout diagnosis, treatment and relapse on leukemic blasts and leukemic stem cells, CLEC12A can be considered a highly potent and reliable marker for the detection of measurable residual disease and therefore applicable for risk stratification and prognostication in AML. CLEC12A/MICL/CLL-1 Protein, Human, Recombinant (His), FITC-Labeled is expressed in HEK293 mammalian cells with N-His tag. The predicted molecular weight is 24.6 kDa and the accession number is Q5QGZ9-2.

Trefoil factors (TFF) are secretory products of mucin producing cells. They play a key role in the maintenance of the surface integrity of oral mucosa and enhance healing of the gastrointestinal mucosa by a process called restitution. TFF comprises the gastric peptides (TFF1), spasmolytic peptide (TFF2), and the intestinal trefoil factor (TFF3). They have an important and necessary role in epithelial restitution within the gastrointestinal tract. Members of the trefoil family are characterized by having at least one copy of the trefoil motif, a 40-amino acid domain that contains three conserved disulfide bonds. They are stable secretory proteins expressed in gastrointestinal mucosa. Trefoil Factor 3(TFF3) is involved in the maintenance and repair of the intestinal mucosa. TFF3 promotes the mobility of epithelial cells in healing processes (motogen).

Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA). Has a role in constitutive stable DNA replication (CsdR) and R-loop formation.

E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD7 to trigger SMAD7-mediated transforming growth factor beta/TGF-beta receptor ubiquitin-dependent degradation, thereby downregulating TGF-beta signaling. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with AIMP1. Also forms a stable complex with TGF-beta receptor-mediated phosphorylated SMAD1, SMAD2 and SMAD3, and targets SMAD1 and SMAD2 for ubiquitination and proteasome-mediated degradation. SMAD2 may recruit substrates, such as SNON, for ubiquitin-dependent degradation. Negatively regulates TGFB1-induced epithelial-mesenchymal transition and myofibroblast differentiation.; (Microbial infection) In case of filoviruses Ebola/EBOV and Marburg/MARV infection, the complex formed by viral matrix protein VP40 and SMURF2 facilitates virus budding.

Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1.; In absence of DNA repair, the XPC complex also acts as a transcription coactivator: XPC interacts with the DNA-binding transcription factor E2F1 at a subset of promoters to recruit KAT2A and histone acetyltransferase complexes (HAT). KAT2A recruitment specifically promotes acetylation of histone variant H2A.Z.1/H2A.Z, but not H2A.Z.2/H2A.V, thereby promoting expression of target genes.

DEP1 / PTPRJ (Receptor-type tyrosine-protein phosphatase eta) is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes, including cell growth, differentiation, mitotic cycle, and oncogenic transformation. DEP1 / PTPRJ possesses an extracellular region containing five fibronectin type III repeats, a single transmembrane region, and a single intracytoplasmic catalytic domain, and thus represents a receptor-type PTP. DEP1 / PTPRJ is present in all hematopoietic lineages, and was shown to negatively regulate T cell receptor signaling possibly through interfering with the phosphorylation of Phospholipase C Gamma 1 and Linker for Activation of T Cells. This protein can also dephosphorylate the PDGF beta receptor, and may be involved in UV-induced signal transduction. In stable MCF-7 cell lines, induction of DEP-1 expression inhibited breast cancer cell growth by 5-10-fold. These data describe PTPs expressed and regulated in breast cancer cell lines during differentiation and identify one PTP, DEP-1, that inhibits the growth of breast cancer cells in vitro.

Dehydrogenase/reductase (SDR family) member 9 (DHRS9) is aberrantly expressed in colorectal cancer (CRC), the decreased expression of DHRS9 correlates with tumor progression and may serve as a potential prognostic biomarker in CRC. The human regulatory macrophage (Mreg) has emerged as a promising cell type for use as a cell-based adjunct immunosuppressive therapy in solid organ transplant recipients. DHRS9 is a specific and stable marker of human Mregs.

Appears to function predominantly as a heterodimeric complex with ILF3. This complex may regulate transcription of the IL2 gene during T-cell activation. It can also promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA. Essential for the efficient reshuttling of ILF3 (isoform 1 and isoform 2) into the nucleus. ILF2 Protein, Human, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 70.1 kDa and the accession number is Q12905.

class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced upon acidification in the endosome.; Stable signal peptide (SSP): cleaved and functions as a signal peptide. In addition, it is also retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of GP1 and GP2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.; interacts with the host receptor.

Complement-activating protein in cobra venom. It is a structural and functional analog of complement component C3b, the activated form of C3. It binds factor B (CFB), which is subsequently cleaved by factor D (CFD) to form the bimolecular complex CVF/Bb. CVF/Bb is a C3/C5 convertase that cleaves both complement components C3 and C5. Structurally, it resembles the C3b degradation product C3c, which is not able to form a C3/C5 convertase. Unlike C3b/Bb, CVF/Bb is a stable complex and completely resistant to the actions of complement regulatory factors H (CFH) and I (CFI). Therefore, CVF continuously activates complement resulting in the depletion of complement activity.

HCV NS3 displays three enzymatic activities: serine protease, NTPase, and RNA helicase. HCV NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A, and NS5A-NS5B. HCV NS3 RNA helicase binds to RNA and unwinds dsRNA in the 3' to 5' direction, and likely RNA stable secondary structure in the template strand (By similarity). Cleaves and inhibits the host antiviral protein MAVS. NS3/NS4A complex also prevents phosphorylation of human IRF3, thus preventing the establishment of dsRNA induced antiviral state. One of the HCV proteases, NS3-4A serine protease, is a non-covalent heterodimer consisting of a catalytic subunit (the N-terminal one-third of NS3 protein) and an activating cofactor (NS4A protein) and is responsible for cleavage at four sites of the HCV polyprotein.

AHSP, also known as ERAF, is a conserved mammalian erythroid protein which belongs to the AHSP family. It is expressed in blood and bone marrow. AHSP facilitates the production of Hemoglobin A by stabilizing free α-globin. It rapidly binds to ferrous α with association (k'(AHSP)) and dissociation (k(AHSP)) rate constants of ≈1 μm(-1) s(-1) and .2 s(-1), respectively, at pH 7.4 at 22 ℃. A small slow phase was observed when AHSP binds to excess ferrous αCO. This slow phase appears to be due to cis to trans prolyl isomerization of the Asp(29)-Pro(3) peptide bond in wild-type AHSP because it was absent when αCO was mixed with P3A and P3W AHSP, which are fixed in the trans conformation. This slow phase was also absent when met(Fe(3+))-α reacted with wild-type AHSP, suggesting that met-α is capable of rapidly binding to either Pro(3) conformer. Both wild-type and Pro(3)-substituted AHSPs drive the formation of a met-α hemichrome conformation following binding to either met- or oxy(Fe(2+))-α. The dissociation rate of the met-α·AHSP complex (k(AHSP) ≈ .2 s(-1)) is ～1-fold slower than that for ferrous α·AHSP complexes, resulting in a much higher affinity of AHSP for met-α. Thus, in vivo, AHSP acts as a molecular chaperone by rapidly binding and stabilizing met-α hemichrome folding intermediates. The low rate of met-α dissociation also allows AHSP to have a quality control function by kinetically trapping ferric α and preventing its incorporation into less stable mixed valence Hemoglobin A tetramers. Reduction of AHSP-bound met-α allows more rapid release to β subunits to form stable fully, reduced hemoglobin dimers and tetramers.

NOTCH2 (Notch Receptor 2) is a Protein Coding gene. This gene encodes a member of the Notch family. Members of this Type 1 transmembrane protein family share structural characteristics and play a role in a variety of developmental processes by controlling cell fate decisions. Hajdu Cheney Syndrome (HCS) is a rare disease associated with mutations of NOTCH2 that lead to the translation of a truncated, presumably stable, NOTCH2 protein. NOTCH2 is down-regulated in colon cancer, and reduced expression is associated with a less differentiated, more aggressive phenotype, and reduced overall survival. NOTCH2 has also been shown to have pro-apoptotic and growth-suppressive effects in thyroid carcinoma, and carcinoid tumors. NOTCH2 acts as an oncogene that promotes bladder cancer growth and metastasis through EMT, cell-cycle progression, and maintenance of stemness.

Desmin is a cytoplasmic protein and belongs to the intermediate filament family. interacts with DST and MTM1. Desmin is only expressed in vertebrates, however homologous proteins are found in many organisms. Desmin is the main intermediate filament in mature skeletal, cardiac and smooth-muscle cells. DES founctions as homopolymers to form a stable intracytoplasmic filamentous network connecting myofibrils to each other and to the plasma membrane. .Defects in DES are cause of the myopathy myofibrillar type 1, cardiomyopathy dilated type 1I, and neurogenic scapuloperoneal syndrome Kaeser type.

Activin Receptor Type-2A is a protein that in humans is encoded by the ACVR2A gene. ACVR2A is an activin type 2 receptor. This gene encodes activin A type II receptor. Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I (I and IB) and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding extracellular domain with cysteine-rich region, a transmembrane domain, and a cytoplasmic domain with predicted serine/threonine specificity. Type I receptors are essential for signaling; and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a stable complex after ligand binding, resulting in phosphorylation of type I receptors by type II receptors. Type II receptors are considered to be constitutively active kinases.

U6 snRNA-associated Sm-like protein LSm4 (LSM4) is a member of the snRNP Sm proteins family. Sm-like proteins contain the Sm sequence motif and are thought to form a stable heteromer present in tri-snRNP particles, which are important for pre-mRNA splicing. LSM4 forms a heteromer with a donut shape. The complexes are involved in various steps of RNA metabolism. LSM4 binds specifically to the 3-terminal U-tract of U6 snRNA. LSM4 contributes RNA protein interactions and structural changes which are essential during ribosomal subunit assembly.

CLEC12A has recently been identified as an antigen, expressed on leukemic stem cells and leukemic blasts. Given the fact that this expression profile seems stable throughout diagnosis, treatment and relapse on leukemic blasts and leukemic stem cells, CLEC12A can be considered a highly potent and reliable marker for the detection of measurable residual disease and therefore applicable for risk stratification and prognostication in AML. CLEC12A/MICL/CLL-1 Protein, Human, Recombinant (hFc & Avi), Biotinylated is expressed in HEK293 mammalian cells with N-hFc-Avi tag. The predicted molecular weight is 51.7 kDa and the accession number is Q5QGZ9-2.

CLEC12A has recently been identified as an antigen, expressed on leukemic stem cells and leukemic blasts. Given the fact that this expression profile seems stable throughout diagnosis, treatment and relapse on leukemic blasts and leukemic stem cells, CLEC12A can be considered a highly potent and reliable marker for the detection of measurable residual disease and therefore applicable for risk stratification and prognostication in AML. CLEC12A/MICL/CLL-1 Protein, Human, Recombinant (aa 65-265, His) is expressed in HEK293 mammalian cells with N-His tag. The predicted molecular weight is 24.6 kDa and the accession number is Q5QGZ9-2.

Ca2+-regulated heat-stable protein of 24 kDa (CRHSP-24) is a serine phosphoprotein originally identified as a physiological substrate for the Ca2+-calmodulin regulated protein phosphatase calcineurin (PP2B). CRHSP-24 is a paralog of the brain-specific mRNA-binding protein PIPPin and was recently shown to interact with the STYX/dead phosphatase protein in developing spermatids.

NGF is the first member discovered in the Neurotrophin family, which includes brain-derived neurotrophic factor (BDNF), neurotrophin-3 (NT-3), and neurotrophin-4 (NT-4). These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. Mouse beta -NGF is a homodimer of two 120 amino acid polypeptides. It shares approximately 90% homology at the amino acid level with human beta -NGF and 95.8% with rat beta -NGF. NGF signaling has been shown to play an important role in neuroprotection and repair. β-NGF acts as a growth and differentiation factor for B lymphocytes, and enhances B-cell survival. It is a potent neurotrophic factor that signals through its receptor β-NGFR, and plays a crucial role in the development and preservation of the sensory and sympathetic nervous systems.

p53, also known as Tp53, is a DNA-binding protein which belongs to the p53 family. It contains transcription activation, DNA-binding, and oligomerization domains. p53 protein is expressed at low level in normal cells and at a high level in a variety of transformed cell lines, where it's believed to contribute to transformation and malignancy. p53 (TP53) is a transcription factor whose protein levels and post-translational modification state alter in response to cellular stress (such as DNA damage, hypoxia, spindle damage). Activation of p53 begins through a number of mechanisms including phosphorylation by ATM, ATR, Chk1 and MAPKs. MDM2 is a ubiquitin ligase that binds p53 and targets p53 for proteasomal degradation. Phosphorylation, p14ARF and USP7 prevent MDM2-p53 interactions, leading to an increase in stable p53 tetramers in the cytoplasm. Further modifications such as methylation and acetylation lead to an increase in Tp53 binding to gene specific response elements. Tp53 regulates a large number of genes (>100 genes) that control a number of key tumor suppressing functions such as cell cycle arrest, DNA repair, senescence and apoptosis. Whilst the activation of p53 often leads to apoptosis, p53 inactivation facilitates tumor progression. It is postulated to bind to a p53-binding site and activate expression of downstream genes that inhibit growth and/or invasion, and thus function as a tumor suppressor. Mutants of p53 that frequently occur in a number of different human cancers fail to bind the consensus DNA binding site, and hence cause the loss of tumor suppressor activity. Defects in TP53 are a cause of esophageal cancer, Li-Fraumeni syndrome, lung cancer and adrenocortical carcinoma.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy

LSM1 is an Sm-like protein. Sm-like proteins can be detected in a variety of organisms based on sequence homology with the Sm protein family. 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 Sm-like proteins are thought to form a stable heteromer present in tri-snRNP particles, which are important for pre-mRNA splicing. LSM1 has a role in replication-dependent histone mRNA degradation and binds specifically to the 3''-terminal U-tract of U6 snRNA. LSM1 also facilitates RNA protein interactions and structural modifications which are required during ribosomal subunit assembly.

Afamin is an 87 kDa glycoprotein with five predicted N-glycosylation sites. Afamin's glycan abundance contributes to conformational and chemical inhomogeneity presenting great challenges for molecular structure determination. Afamin, a human plasma glycoprotein and putative transporter of hydrophobic molecules, has been shown to act as extracellular chaperone for poorly soluble, acylated Wnt proteins, forming a stable, soluble complex with functioning Wnt proteins. The 2.1-Å crystal structure of glycosylated human afamin reveals an almost exclusively hydrophobic binding cleft capable of harboring large hydrophobic moieties. Afamin plays a role in anti-apoptotic cellular processes related to oxidative stress and is associated with insulin resistance and other features of metabolic syndrome. Afamin may serve as a new early biomarker for pathological glucose metabolism during pregnancy. And first trimester screening for pre-eclampsia could be provided by a combination of afamin and placental bed vascularization. Moreover, the combination of first trimester serum afamin levels with BMI could provide a possible screening for gestational diabetes mellitus.

Ca2+/calmodulin-dependent protein kinase2A (CAMK2A) belongs to the serine/threonine protein kinase family and, together with other 28 different isoforms, belongs to the Ca2+/ calmodulin-dependent protein kinase subfamily. CaM kinase Ⅱ is thought to be an important mediator of learning and memory and is also necessary for Ca2+homeostasis and reuptake in cardiomyocytes chloride transport in epithelia, positive T-cell selection, and CD8 T-cell activation. CAMKIIA is one of the major forms of CAMKII. It has been found to play a critical role in sustaining activation of CAMKII at the postsynaptic density. Studies have found that knockout mice without CAMKIIA demonstrate a low frequency of LTP. Additionally, these mice do not form persistent, stable place cells in the hippocampus.

MST4, also known as mammalian STE2-like protein kinase 4, is a novel member of the germinal center kinase subfamily of human Ste2-like kinases and is closely related to MST3. The 416 amino acid full-length MST4 contains a C-terminal regulatory domain and an N-terminal kinase domain, both of which are required for full activation of the kinase. MST4 is highly expressed in the placenta, thymus, and peripheral blood leukocytes. MST4 specifically activates ERK but not JNK or p38 MAPK in transiently transfected cells or stable cell lines, and thus is biologically active in the activation of the MEK/ERK pathway mediating cell growth and transformation. Further, MST4 kinase activity is stimulated significantly by epidermal growth factor receptor (EGFR) ligands, which are known to promote the growth of certain cancer cells. Accordingly, MST4 has a potential role in signal transduction pathways involved in cancer progression. Three alternatively spliced isoforms of MST4 have been isolated, and isoform 3 lacks an exon encoding kinase domain and may function as a dominant-negative regulator of the MST4 kinase.

C-type lectin domain family 3 member A (CLEC3A) is a poorly characterized protein belonging to the superfamily of C-type lectins. Elevated CLEC3A expression may correlate with breast IDC metastatic potential and indicated a poor prognosis in breast IDC. CLEC3A knockdown inhibited BC cell growth and metastasis might be through suppressing PI3K/AKT signaling activity. That CLEC3A is a promising therapeutic target for BC in the future. Matrilysin (MMP-7) plays important roles in tumor progression. Previous studies have suggested that MMP-7 binds to tumor cell surface and promotes their metastatic potential. C-type lectin domain family 3 member A (CLEC3A) as a membrane-bound substrate of MMP-7. CLEC3A binds to heparan sulfate proteoglycans on cell surface, leading to the enhancement of cell adhesion to integrin ligands on ECM. It can be speculated that the cleavage of CLEC3A by MMP-7 weakens the stable adhesion of tumor cells to the matrix and promotes their migration in tumor microenvironments.

CLEC12A has recently been identified as an antigen, expressed on leukemic stem cells and leukemic blasts. Given the fact that this expression profile seems stable throughout diagnosis, treatment and relapse on leukemic blasts and leukemic stem cells, CLEC12A can be considered a highly potent and reliable marker for the detection of measurable residual disease and therefore applicable for risk stratification and prognostication in AML. CLEC12A/MICL/CLL-1 Protein, Human, Recombinant (His, Avi), Biotinylated is expressed in HEK293 mammalian cells with N-His and C-Avi tag. The predicted molecular weight is 26.4 kDa and the accession number is Q5QGZ9-2.

CLEC12A has recently been identified as an antigen, expressed on leukemic stem cells and leukemic blasts. Given the fact that this expression profile seems stable throughout diagnosis, treatment and relapse on leukemic blasts and leukemic stem cells, CLEC12A can be considered a highly potent and reliable marker for the detection of measurable residual disease and therefore applicable for risk stratification and prognostication in AML. CLEC12A/MICL/CLL-1 Protein, Human, Recombinant (aa 65-265, hFc) is expressed in HEK293 mammalian cells with N-hFc tag. The predicted molecular weight is 50.9 kDa and the accession number is Q5QGZ9-2.

Endogenous activator of intestinal guanylate cyclase. It stimulates this enzyme through the same receptor binding region as the heat-stable enterotoxins. May be a potent physiological regulator of intestinal fluid and electrolyte transport. May be an autocrine/paracrine regulator of intestinal salt and water transport. GUCA2B Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with N-6xHis tag. The predicted molecular weight is 13.5 kDa and the accession number is Q16661.

LSM3 (LSM3 Homolog, U6 Small Nuclear RNA And MRNA Degradation Associated) is a Protein Coding gene. LSM3 is a member of the snRNP Sm proteins family. It plays role in pre-mRNA splicing as a component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as a component of the pre-catalytic spliceosome (spliceosome B complex). Sm-like proteins can be detected in a variety of organisms. They all have the Sm sequence motif, which consists of 2 regions separated by a linker of variable length that folds as a loop. The Sm-like proteins are thought to form a stable heteromer present in tri-snRNP particles, which are important for pre-mRNA splicing. Diseases associated with LSM3 include Spondylolysis.

Statherin, also known as STATH, belongs to the histatin/statherin family. Statherin may play an important role in the maintenance of oral health. It prevents calcium phospate precipitation in saliva, so maintaining a high calcium level in saliva and preventing teeth from dissolving. Statherin also inhibits spontaneous precipitation of calcium phosphate salts. Thus, statherin and PRPs may prevent build-up of harmful deposits in the salivary glands and on the tooth surfaces. Statherin is a highly stable salivary protein of low molecular mass (5,380).

Acyl-coenzyme A: cholesterol acyltransferase (ACAT) is an intracellular enzyme that produces cholesteryl esters in various tissues. In mammals, two ACAT genes (ACAT1 and ACAT2) have been identified. Together, these two enzymes are involved in storing cholesteryl esters as lipid droplets, in macrophage foam-cell formation, in absorbing dietary cholesterol, and in supplying cholesteryl esters as part of the core lipid for lipoprotein synthesis and assembly. The key difference in tissue distribution of ACAT1 and ACAT2 between humans, mice and monkeys is that, in adult human liver (including hepatocytes and bile duct cells), the major enzyme is ACAT1, rather than ACAT2. There is compelling evidence implicating a role for ACAT1 in macrophage foam-cell formation, and for ACAT2 in intestinal cholesterol absorption.Ubiquitin linkage to cysteine is an unconventional modification targeting protein for degradation. However, the physiological regulation of cysteine ubiquitylation is still mysterious. Here we found that ACAT2, a cellular enzyme converting cholesterol and fatty acid to cholesteryl esters, was ubiquitylated on Cys277 for degradation when the lipid level was low. gp78-Insigs catalysed Lys48-linked polyubiquitylation on this Cys277. A high concentration of cholesterol and fatty acid, however, induced cellular reactive oxygen species (ROS) that oxidized Cys277, resulting in ACAT2 stabilization and subsequently elevated cholesteryl esters. Furthermore, ACAT2 knockout mice were more susceptible to high-fat diet-associated insulin resistance. By contrast, expression of a constitutively stable form of ACAT2 (C277A) resulted in higher insulin sensitivity. ACAT2 is an appealing target for therapy to reduce coronary heart disease.

Activin proteins that belong to the transforming growth factor-beta (TGF-β) superfamily, exert their biological actions by binding to heteromeric receptor complexes of type I and type II serine/threonine kinase receptors. On ligand binding, type I and II receptors form a stable complex, resulting in phosphorylation of type I receptors by type II receptors with constitutive kinase activity, and subsequently initiates the activation of downstream molecules including the endogenous Smads. ActRIIB, also known as ActRIIB, is a type II receptor containing an extracellular domain (ECD), a transmembrane segment, and a cytoplasmic region that includes the kinase domain. ActRIIB is a receptor for activin A, activin B and inhibin A. Multiple ActRIIB isoforms can also be generated, which bind activin isoforms with different affinities.

Involved in biofilm formation. Self-polymerizes and forms a layer on the surface of biofilms that confers hydrophobicity to the biofilm. The layer is stable and capable of resistance to high mechanical force compression. Required for complex colony architecture. May function synergistically with exopolysaccharides and TasA amyloid fibers to facilitate the assembly of the biofilm matrix. YuaB Protein, Bacillus subtilis, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 35.3 kDa and the accession number is P71014.

This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of the final effector complex. The ATPase activity of MutL is stimulated by DNA. MutL Protein, E. coli, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 71.9 kDa and the accession number is P23367.

Histone-lysine N-methyltransferase SUV42H2, also known as Suppressor of variegation 4-2 homolog 2, Su(var)4-2 homolog 2, Lysine N-methyltransferase 5C, SUV42H2 and KMT5C, is nucleus protein that belongs to the histone-lysine methyltransferase family and Suvar4-2 subfamily. SUV42H2 is a histone methyltransferase that specifically trimethylates 'Lys-2' of histone H4. H4 'Lys-2' trimethylation represents a specific tag for epigenetic transcriptional repression. SUV42H2 mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV42H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2). FRAP experiments reveal that SUV42H2 is strongly associated with pericentric heterochromatin. The fraction of SUV42H2 captured and characterized by TAP/MS is a soluble fraction which may be in a stable association with HP1. SUV42H2 may be recruited to heterochromatin in association with HP1, and stably maintained at its heterochromatin sites in an HP1-independent fashion.

Calmodulin-like protein 5, also known as Calmodulin-like skin protein, CALML5 and CLSP, is a protein which contains fourEF-hand domains. CALML5 / CLSP is particularly abundant in the epidermis where its expression is directly related to keratinocyte differentiation.The expression is very low in lung. CALML5 / CLSP binds calcium. It may be involved in terminal differentiation of keratinocytes. Coxsackievirus and adenovirus receptor (CAR) is a member of the immunoglobulin (Ig) superfamily and a component of epithelial tight junction. CAR functions as a primary receptor for coxsackievirus B and adenovirus (Ad) infection. CALML5 / CLSP is closely related to CAR. The structure and dynamics of human calmodulin-like skin protein CALML5 / CLSP have been characterized by NMR spectroscopy. The mobility of CALML5 / CLSP has been found to be different for the N-terminal and C-terminal domains. The N-terminal domain is characterized by four stable helices, which experience large fluctuations. This is shown to be due to mutations in the hydrophobic core. The overall N-terminal domain behavior is similar both in the full-length protein and in the isolated domain.

acidic leucine-rich nuclear phosphoprotein 32 family member A, also known as acidic nuclear phosphoprotein pp32, Leucine-rich acidic nuclear protein, Mapmodulin, Potent heat-stable protein phosphatase 2A inhibitor I1PP2A, Putative HLA-DR-associated protein I, PHAPI and ANP32A, is a nucleus, cytoplasm and endoplasmic reticulum. ANP32A / LANP is expressed in all tissues tested. It is highly expressed in kidney and skeletal muscle, moderate levels of expression is in brain, placenta and pancreas. ANP32A / LANP is weakly expressed in lung. It is found in all regions of the brain examined (amygdala, caudate nucleus, corpus callosum, hippocampus and thalamus), with highest levels in amygdala. ANP32A / LANP is a component of the SET complex, which also contains SET, APEX1, HMGB2 and NME1. It directly interacts with SET. ANP32A / LANP also interacts with ATXN1/SCA1. ANP32A / LANP is implicated in a number of cellular processes, including proliferation, differentiation, caspase-dependent and caspase-independent apoptosis, suppression of transformation (tumor suppressor), inhibition of protein phosphatase 2A, regulation of mRNA trafficking and stability in association with ELAVL1, and inhibition of acetyltransferases as part of the INHAT (inhibitor of histone acetyltransferases) complex. ANP32A / LANP plays a role in E4F1-mediated transcriptional repression.