cytoskeleton

High-affinity epithelial cell surface receptor for APF.; Mediates the anchoring of the endoplasmic reticulum to microtubules. CKAP4 Protein, Mouse, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 57.6 kDa and the accession number is Q8BMK4.

Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin-proteasome system (UPS), autophagy and endoplasmic reticulum-associated protein degradation (ERAD) pathway. Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome. Plays a role in the ERAD pathway via its interaction with ER-localized proteins UBXN4, VCP and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome. Isoform 1, isoform 2 and isoform 3 play a role in unfolded protein response (UPR) by attenuating the induction of UPR-inducible genes, DDTI3/CHOP, HSPA5 and PDIA2 during ER stress. Involved in the regulation of macroautophagy and autophagosome formation; required for maturation of autophagy-related protein LC3 from the cytosolic form LC3-I to the membrane-bound form LC3-II and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion. Negatively regulates the TICAM1/TRIF-dependent toll-like receptor signaling pathway by decreasing the abundance of TICAM1 via the autophagic pathway. Isoform 1 and isoform 3 play a key role in the regulation of the levels of PSEN1 by targeting its accumulation to aggresomes which may then be removed from cells by autophagocytosis. Promotes the ubiquitination and lysosomal degradation of ORAI1, consequently downregulating the ORAI1-mediated Ca2+ mobilization. Suppresses the maturation and proteasomal degradation of amyloid beta A4 protein (A4) by stimulating the lysine 63 (K63)-linked polyubiquitination. Delays the maturation of A4 by sequestering it in the Golgi apparatus and preventing its transport to the cell surface for subsequent processing.

High-affinity epithelial cell surface receptor for APF.; Mediates the anchoring of the endoplasmic reticulum to microtubules. CKAP4 Protein, Mouse, Recombinant (His & MBP) is expressed in Baculovirus insect cells with N-MBP and C-6xHis tag. The predicted molecular weight is 96.6 kDa and the accession number is Q8BMK4.

Actins are ubiquitous globular and highly conserved proteins that are involved in various types of cell motility, structure, and integrity. Three main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins co-exist in most cell types as components of the cytoskeleton, and as mediators of internal cell motility. ACTB is a major constituent of the contractile apparatus and one of the two nonmuscle cytoskeletal actins. Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others.

Testin belongs to the prickle/espinas/testin family. Testin contains three LIM zinc-binding domains and one PET domain, TES as a scaffold protein that may have a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. In addition, TES can also as a tumor suppressor, inhibits tumor cell growth, regulate the cell proliferation.TES interacts with many cytoskeletal proteins, such as Zyxin, Mena, Actin, Talin and VASP. The ability of TES to associate with alpha-actin, Zyxin and paxillin is dependent on the conformational state of the molecule.

Protein Kinase C and Casein Kinase Substrate in Neurons Protein 2 (PACSIN2) is a member of the PACSIN family. PACSIN2 is localized to the plasma membrane via its coiled-coil domain. PACSIN2 is widely expressed and contains one FCH domain and one SH3 domain. PACSIN2 forms homo- and hetero-aggregates with other PACSINs. PACSIN2 may play a role in vesicle formation and transport. In addition, PACSIN2 is involved in linking the actin cytoskeleton with vesicle formation by regulating tubulin polymerization.

Cytoskeleton-associated protein 4 (CKAP4) is located in the rough endoplasmic reticulum (ER) and plays an important role in stabilizing the structure of ER. Meanwhile, CKAP4 is also found to act as an activated receptor at the cell surface. CKAP4 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-His tag. The predicted molecular weight is 53.66 kDa and the accession number is Q07065.

Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Mediates docking of the dynein/dynactin motor complex to vesicle cargos for retrograde axonal transport through its interaction with TMEM108 and DCTN1.; plays a structural role in the assembly of hemidesmosomes of epithelial cells; anchors keratin-containing intermediate filaments to the inner plaque of hemidesmosomes. Required for the regulation of keratinocyte polarity and motility; mediates integrin ITGB4 regulation of RAC1 activity.; required for bundling actin filaments around the nucleus.; regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport.

Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Mediates docking of the dynein/dynactin motor complex to vesicle cargos for retrograde axonal transport through its interaction with TMEM108 and DCTN1.; plays a structural role in the assembly of hemidesmosomes of epithelial cells; anchors keratin-containing intermediate filaments to the inner plaque of hemidesmosomes. Required for the regulation of keratinocyte polarity and motility; mediates integrin ITGB4 regulation of RAC1 activity.; required for bundling actin filaments around the nucleus.; regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport.

Plays a role in mitotic bipolar spindle formation. Binds mRNA. May function in nucleocytoplasmic transport and in directly or indirectly attaching cytoplasmic mRNPs to the cytoskeleton. RAE1 Protein, Human, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 68.0 kDa and the accession number is P78406.

Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1. May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12. Isoform 6 increases water and sodium absorption in the intestine and gall-bladder. SORBS2 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 33.1 kDa and the accession number is O94875.

Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.

Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Profilin 2 Protein, Phleum pratense, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 21.5 kDa and the accession number is O24650.

LSP1 (Lymphocyte Specific Protein 1) is a Protein Coding gene. This gene encodes an intracellular F-actin binding protein. The protein is expressed in lymphocytes, neutrophils, macrophages, and endothelium and may regulate neutrophil motility, adhesion to fibrinogen matrix proteins, and transendothelial migration. LSP1 is a lymphocyte-specific intracellular Ca2(+)-binding protein. LSP1 localizes to nascent phagocytic cups during Fcgamma receptor-mediated phagocytosis, where it displays the same spatial and temporal distribution as the actin cytoskeleton. Down-regulation of LSP1 severely reduces the phagocytic activity of macrophages, clearly demonstrating a crucial role for this protein in Fcgamma receptor-mediated phagocytosis. LSP1, expressed in endothelial cells, plays a pivotal role in regulating subsequent recruitment steps following leukocyte adhesion.

ANTXR1 contains 1 VWFA domain and belongs to the ATR family. ATR (Ataxia telangiectasia and Rad3 related) and ATM (Ataxia telangiectasia mutated) are closely related kinases that are activated by DNA damage. They are serine-threonine protein kinases and belongs to the phosphatidylinositol 3' kinase-like kinase (PIKK) family. Upon recruitment by the DNA damage binding proteins/complexes (ATRIP for ATR; MRN for ATM), ATM/ATR initiate the DNA damage checkpoint by phosphorylating a number of key proteins. ANTXR1 interacts with extracellular matrix proteins and with the actin cytoskeleton. It functions in cell attachment and migration. ANTXR1 also mediates adhesion of cells to type 1 collagen and gelatin, reorganization of the actin cytoskeleton and promotes cell spreading. It plays a role in the angiogenic response of cultured umbilical vein endothelial cells.

MAPRE3 (Microtubule Associated Protein RP/EB Family Member 3, also known as EB3) is a Protein Coding gene. 2 alternatively spliced human isoforms have been reported. MAPRE3 is a member of the RP/EB family. It localizes to the cytoplasmic microtubule network and binds APCL. MAPRE3 regulates the dynamics of the microtubule cytoskeleton and promotes microtubule growth. It may be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. MAPRE3 may also play a role in cell migration. MAPRE3 is broadly expressed in the brain, testis, and other tissues. Diseases associated with MAPRE3 include Neuronopathy, Distal Hereditary Motor, Type Viib, and Distal Hereditary Motor Neuronopathy Type 7.

c-Abl belongs to the class of tyrosine kinases and is the prototype of a subfamily which includes two members, c-Abl and Arg (Abl-related gene). Both proteins are localized at the cell membrane, actin cytoskeleton and cytosol, and c-Abl is present in the nucleus as well. c-Abl is a non-receptor tyrosine kinase that participates in multiple signaling pathways linking the cell surface, cytoskeleton, and the nucleus. Recent in vitro studies have also linked c-Abl to amyloid-beta-induced toxicity and tau phosphorylation. c-Abl has been implicated in many cellular processes including differentiation, division, adhesion, death, and stress response. c-Abl is a latent tyrosine kinase that becomes activated in response to numerous extra- and intra-cellular stimuli. The c-Abl protein is a ubiquitously expressed nonreceptor tyrosine kinase involved in the development and function of many mammalian organ systems, including the immune system and bone. It regulates the cellular response to TAM through functional interaction with the estrogen receptor, which suggests c-Abl as a therapeutic target and a prognostic tumor marker for breast cancer. c-Abl also plays a key role in signaling chemokine-induced T-cell migration. In addition, c-Abl contains NLSs (nuclear localization signals) and DNA-binding sequences important for nuclear functions. c-Abl has become an important therapeutic target in human chronic myeloid leukaemia.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy

ATG5 is an E2 ubiquitin ligase which is necessary for autophagy. Its expression is a relatively late event in the apoptotic process, occurring downstream of caspase activity, dramatically highly expressed in apoptotic cells. It is activated by ATG7, conjugates to ATG12 and associates with isolation membrane to form cup-shaped isolation membrane and autophagosome. The conjugate complex detaches from the membrane immediately before or after autophagosome formation is completed. ATG5 plays an important role in the apoptotic process, possibly within the modified cytoskeleton.

Cytoskeleton-associated protein 4 (CKAP4) is located in the rough endoplasmic reticulum (ER) and plays an important role in stabilizing the structure of ER. Meanwhile, CKAP4 is also found to act as an activated receptor at the cell surface. CKAP4 Protein (Primary Amine Labeling), Human, Recombinant (His), Biotinylated is expressed in E. coli expression system with N-His tag. The predicted molecular weight is 53.66 kDa and the accession number is Q07065.

S100A8 and S100A9 (also known as MRP8 and MRP14, respectively) are Ca2 binding proteins belonging to the S100 family. They often exist in the form of heterodimer, while homodimer exists very little because of the stability. S100A8/A9 is constitutively expressed in neutrophils and monocytes as a Ca2 sensor, participating in cytoskeleton rearrangement and arachidonic acid metabolism. S100A9 Protein, Cynomolgus, Recombinant (His) is expressed in E. coli expression system with N-His tag. The predicted molecular weight is 14.70 kDa and the accession number is A0A2K5VRV3.

Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance. During the axon guidance process, acts downstream of SEMA3A to promote FLNA dissociation from F-actin which results in the rearrangement of the actin cytoskeleton and the collapse of the growth cone. Involved in invasive growth and cell migration. May participate in cytokinesis. CRMP1 Protein, Human, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 62.2 kDa and the accession number is Q14194.

Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. May play a role in endocytosis.

Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration.

The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization.; Extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains. Receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells. Also acts as a receptor for laminin LAMA5.; Transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton. Acts as a cell adhesion receptor in both muscle and non-muscle tissues. Receptor for both DMD and UTRN and, through these interactions, scaffolds axin to the cytoskeleton. Also functions in cell adhesion-mediated signaling and implicated in cell polarity.; (Microbial infection) Acts as a receptor for lassa virus and lymphocytic choriomeningitis virus glycoprotein and class C new-world arenaviruses. Acts as a Schwann cell receptor for Mycobacterium leprae, the causative organism of leprosy, but only in the presence of the G-domain of LAMA2.

Receptor for SEMA4D. Plays a role in GABAergic synapse development. Mediates SEMA4A- and SEMA4D-dependent inhibitory synapse development. Plays a role in RHOA activation and subsequent changes of the actin cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Plexin-B1 Protein, Human, Recombinant (mFc) is expressed in HEK293 mammalian cells with N-mFc tag. The predicted molecular weight is 83.2 kDa and the accession number is O43157.

Plays a role in cell attachment and migration. Interacts with extracellular matrix proteins and with the actin cytoskeleton. Mediates adhesion of cells to type 1 collagen and gelatin, reorganization of the actin cytoskeleton and promotes cell spreading. Plays a role in the angiogenic response of cultured umbilical vein endothelial cells.

Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in AUM-cytoskeleton interaction in terminally differentiated urothelial cells. It also contributes to the formation of urothelial glycocalyx which may play an important role in preventing bacterial adherence. UPK3A Protein, Mouse, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 25.5 kDa and the accession number is Q9JKX8.

Component of the cytoskeleton-like structure which stabilizes the shape of the wall-less mycoplasma. This cytoskeleton-like network of accessory proteins containing HMW proteins 1 to 5 allows the proper anchoring of cytadhesin proteins in the mycoplasmal membrane at the attachment organelle. Essential for successful surface parasitism. HMW3 Protein, Mycoplasma pneumoniae, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 27.1 kDa and the accession number is Q50360.

Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin-associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function in stabilizing the sarcolemma. Also implicated in signaling events and synaptic transmission. Dystrophin Protein, Rat, Recombinant (His) is expressed in yeast with C-6xHis tag. The predicted molecular weight is 29.1 kDa and the accession number is P11530.

Actopaxin, also known as alpha-parvin, belongs to the parvin family. It is widely expressed, with highest levels in heart, skeletal muscle, kidney and liver. Actopaxin contains 2 CH (calponin-homology) domains and probably plays a role in the regulation of cell adhesion and cytoskeleton organization. It interacts with integrin-linked protein kinase and probably with actin and the LD1 and LD4 motifs of PXN. Actopaxin binds directly to both F-actin and paxillin LD1 and LD4 motifs. Actopaxin also exhibits robust focal adhesion localization in several cultured cell types but is not found along the length of the associated actin-rich stress fibers. It is absent from actin-rich cell-cell adherens junctions.

Integrin alpha V beta 8 is a receptor for fibronectin. It recognizes the sequence R-G-D in its ligands. ITGAVB8 does not appear to assume different activation states; and the cytoplasmic tail does not connect to the cytoskeleton. It binds ligands containing an RGD motif; including vitronectin; fibrin and the latency associated peptide (LAP) of the latent TGF-beta complex. High affinity binding of alpha V beta 8 to LAP allows proteolytic cleavage by MT1-MMP; which releases active TGF-beta. This mechanism differs from that of alpha V beta 6; the other alpha V integrin which can activate TGF-beta from latency through non-proteolytic mechanisms.

The ADAMs (a disintegrin and metalloprotease) comprise a family of multidomain proteins with metalloprotease, cell adhesion, and signaling activities. Human ADAM12, which is implicated in diseases such as cancer, is expressed in two splice forms, the transmembrane ADAM12-L and the shorter and soluble ADAM12-S. ADAM12, also known as and Meltrin alpha, is a member of the ADAM protein family, which contains one disintegrin domain, one EGF-like domain and one peptidase M12B domain. ADAM12 is synthesized as a zymogen with the prodomain keeping the metalloprotease inactive through a cysteine-switch mechanism. Maturation and activation of the protease involves the cleavage of the prodomain in the trans-Golgi or possibly at the cell surface by a furin-peptidase. It is a membrane-anchored metalloprotease, which has been implicated in activation-inactivation of growth factors that play an important role in wound healing, including heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) and IGF binding proteins. ADAM12 may also regulate cell-cell and cell-extracellular matrix contacts through interactions with cell surface receptors - integrins and syndecans - potentially influencing the actin cytoskeleton. Moreover, ADAM12 interacts with several cytoplasmic signaling and adaptor molecules through its intracellular domain, thereby directly transmitting signals to or from the cell interior. These ADAM12-mediated cellular effects appear to be critical events in both biological and pathological processes. In addition to protease activity, ADAM12 possesses cell binding and cell signaling properties. In many studies, ADAM12 overexpression has been correlated with disease, and ADAM12 has been shown to promote tumor growth and progression in cancer. On the other hand, protective effects of ADAM12 in disease have also been reported.

Transforming protein RhoA, also known as Rho cDNA clone 12, Ras homolog gene family member A, RHOA and ARH12, is a cell membrane and cytoplasm protein that belongs to the small GTPase superfamily and Rho family. The Rho family of small GTPases plays a key role in the dynamic regulation of the actin cytoskeleton that underlies various important cellular functions such as shape changes, migration, and polarity. RHOA / ARH12 is part of a larger family of related proteins known as the Ras superfamily; proteins involved in the regulation and timing of cell division. RHOA / ARH12 is a small GTPase protein known to regulate the actin cytoskeleton in the formation of stress fibers. It acts upon two known effector proteins: ROCK1 (Rho-associated, coiled-coil containing protein kinase 1) and DIAPH1 ( diaphanous homolog 1 (Drosophila) ). RHOA / ARH12 regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. RHOA / ARH12 serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. RHOA / ARH12 may be an activator of PLCE1. It is activated by ARHGEF2, which promotes the exchange of GDP for GTP.

Pleckstrin is a protein found in platelets. Pleckstrin is the source of the name pleckstrin homology domain. Pleckstrin homology domain (PH domain) is a protein domain of approximately 12 amino acids that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton. This domain can bind Phosphatidylinositol lipids within biological membranes (such as Phosphatidylinositol (3,4,5)-trisphosphate and phosphatidylinositol (4,5)-bisphosphate), and proteins such as the βγ-subunits of heterotrimeric G proteins, and protein kinase C. Through these interactions, PH domains play a role in recruiting proteins to different membranes, thus targeting them to appropriate cellular compartments or enabling them to interact with other components of the signal transduction pathways.

Podoplanin belongs to the podoplanin family, also known as Glycoprotein 38. Podoplanin is synthesized as a 172 amino acid (aa) precursor with a 22 aa signal sequence, a 119 aa extracellular domain (ECD), a 21 aa transmembrane region, and a short, 10 aa cytoplasmic tail. Detected at high levels in lung and brain, at lower levels in kidney, stomach, liver, spleen and esophagus, and not detected in skin and small intestine. Expressed in epithelial cells of choroid plexus, ependyma, glomerulus and alveolus, in mesothelial cells and in endothelia of lymphatic vessels. Also expressed in stromal cells of peripheral lymphoid tissue and thymic epithelial cells. Detected in carcinoma cell lines and cultured fibroblasts. Expressed at higher levels in colon carcinomas than in normal colon tissue. It can interacts with CLEC1B; the interaction is independent of CLEC1B glycosylation and activates CLEC1B. It may be involved in cell migration and/or actin cytoskeleton organization. When expressed in keratinocytes, induces changes in cell morphology with transfected cells showing an elongated shape, numerous membrane protrusions, major reorganization of the actin cytoskeleton, increased motility and decreased cell adhesion. Required for normal lung cell proliferation and alveolus formation at birth. Ligand for CLEC1B, a platelet receptor. Induces platelet aggregation. Does not have any effect on folic acid or amino acid transport. Does not function as a water channel or as a regulator of aquaporin-type water channels.

SEMA4D is a member of the semaphorin family,contains one Ig-like C2-type domain, one PSI domain and one Sema domain. SEMA4D is strongly expressed in lymphoid tissues, especially in the thymus, as well as in the nervous tissues. However, SEMA4D is expressed at lower levels in testes, brain, kidney, small intestine, prostate, heart, placenta, lung and pancreas, but not in colon and liver. SEMA4D is a cell surface receptor for PLXN1B and PLXNB2 that plays an important role in cell-cell signaling. SEMA4D is involved in a number of fundamental biological processes such as promoting reorganization of the actin cytoskeleton, the migration of cerebellar granule cells and of endothelial cells and signaling via SRC and PTK2B/PYK2, which then mediates activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Not only these, it plays a role in axonal growth cone guidance in the developing central nervous system. Semaphorin-4D / SEMA4D may play a functional role in the immune system, as well as in the nervous system. It could induce B-cells to aggregate and improves their viability (in vitro). SEMA4D is involved in regulating dendrite and axon branching and morphogenesis and promoting interaction with PLXNB1 mediates activation of RHOA.

Macrophage Colony-Stimulating Factors (m-csf) are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and themonocytes-macrophages. CSF-1 promotes the release of proinflammatory chemokines, and thereby plays an important role in innate immunity and in inflammatory processes. It also plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone development. CSF-1 is required for normal male and female fertility and promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration. it also plays a role in lipoprotein clearance.

Vinculin is a focal adhesion and cytoskeletal protein that distributed mainly at cell-cell junctions and cell-extracellular matrix (ECM) adhesion that belongs to the Vinculin/α-Catenin family. Vinculin is an Actin-binding protein and component of the Actin-Linking Functional module that senses and feels the mechanical properties of the extracellular environment. Vinculin is also a key factor that couples, transmits, transduces, and regulates mechanical force between the cytoskeleton and adhesion receptors. Vinculin generally forms two structural states, an open (active) and closed (inactive) state, which are controlled by conformational interaction(s) between the head and tail domains. Vinculin is involved in the mechano-chemical signal transmission of cells by binding to a variety of focal adhesion or cytoskeletal proteins, and plays important roles in cell adhesion, extension, motion, proliferation and survival.

Glial Fibrillary Acidic Protein (GFAP) is an intermediate filament (IF) protein which belongs to the intermediate filament family. GFAP is expressed in numerous cell types of the central nervous system (CNS), ependymal cells and phosphorylated by PKN1. GFAP, a class-III intermediate filament, is a cell-specific marker during the development of the central nervous system and distinguishes astrocytes from other glial cells. It is closely related to its non-epithelial family members, vimentin, desmin, and peripherin, which are all involved in the structure and function of the cell’s cytoskeleton. GFAP is thought to help to maintain astrocyte mechanical strength, as well as the shape of cells but its exact function remains poorly understood.

Tyrosine-protein kinase Mer (MERTK) is a single-pass type I membrane protein which belongs to the MER/AXL/TYRO3 receptor kinase family. MERTK include two fibronectin type-III domains, two Ig-like C2-type domains, and one tyrosine kinase domain. It can’t be expressed in normal B- and T-lymphocytes, but it is usually expressed in numerous neoplastic B- and T-cell lines. MERTK could regulate many physiological processes, such as cell survival, migration, differentiation. It was demonstrated that the MERTK plays critical role in the engulfment and efficient clearance of apoptotic cells, platelet aggregation, and cytoskeleton reorganization. Not only these, it also plays an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3. In addition, MERTK could regulate rod outer segments fragments phagocytosis in the retinal pigment epithelium (RPE)， deficiency in MERTK are the cause of retinitis pigmentosa.

Chloride Intracellular Channel Protein 5 (CLIC5) is a single-pass membrane protein which belongs to the chloride channel CLIC family. It contains one GST C-terminal domain. Chloride intracellular channels are involved in chloride ion transport within various subcellular compartments. CLIC5 can insert into membranes and form selective ion channels regulated by actin that may transport chloride ions. It may play a role in the regulation of transepithelial ion absorption and secretion. CLIC5 specifically associates with the cytoskeleton of placenta microvilli. CLIC5 is required for the development and/or maintenance of the proper glomerular endothelial cell and podocyte architecture.

S100A8 and S100A9 (also known as MRP8 and MRP14, respectively) are Ca2 binding proteins belonging to the S100 family. They often exist in the form of heterodimer, while homodimer exists very little because of the stability. S100A8/A9 is constitutively expressed in neutrophils and monocytes as a Ca2 sensor, participating in cytoskeleton rearrangement and arachidonic acid metabolism. S100A9 Protein, Canine, Recombinant (His) is expressed in E. coli expression system with N-His tag. The predicted molecular weight is 15.90 kDa and the accession number is XP_038528057.1.

Coreceptor for SEMA3A. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance in the developing nervous system. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm. Plexin-A4 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 60.0 kDa and the accession number is Q9HCM2.

Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. The non-muscle isoform may have a role in agonist-mediated receptor internalization.

Functions as a pyridoxal phosphate (PLP) phosphatase, which also catalyzes the dephosphorylation of pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), with order of substrate preference PLP > PNP > PMP and therefore plays a role in vitamin B6 metabolism. Also functions as a protein serine phosphatase that specifically dephosphorylates 'Ser-3' in proteins of the actin-depolymerizing factor (ADF)/cofilin family like CFL1 and DSTN. Thereby, regulates cofilin-dependent actin cytoskeleton reorganization, being required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phosphothreonines in LIMK1. Does not dephosphorylate peptides containing phosphotyrosine.

Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization. TMSB10 Protein, Mouse, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 17.8 kDa and the accession number is Q6ZWY8.

Adapter protein in a cytoplasmic complex linking beta-integrins to the actin cytoskeleton, bridges the complex to cell surface receptor tyrosine kinases and growth factor receptors. Involved in the regulation of cell survival, cell proliferation and cell differentiation. LIMS1 Protein, Mouse, Recombinant (His) is expressed in Baculovirus insect cells with N-10xHis tag. The predicted molecular weight is 39.6 kDa and the accession number is Q99JW4.

Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. TPM1 Protein, Rabbit, Recombinant (E. coli, His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 37.7 kDa and the accession number is P58772.

S100 protein is a family of low molecular weight protein found in vertebrates characterized by two EF-hand calcium-binding motifs. There are at least 21 different S100 proteins, and the name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are disulfide-linked homodimer, and is normally present in cells derived from the neural crest, chondrocytes, macrophages, dendritic cells, etc. S100 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. Protein S100-A12, also known as S100 calcium-binding protein A12, Calcium-binding protein in amniotic fluid 1, Calgranulin-C, and S100A12, is a member of the S-101 family. Like the majority of S100 proteins, S100A12 is a dimer, with the interface between the two subunits being composed mostly of hydrophobic residues. The fold of S100A12 is similar to the other known crystal and solution structures of S100 proteins, except for the linker region between the two EF-hand motifs. S100A12 plays an important role in the inflammatory response.

S100 protein is a family of low molecular weight protein found in vertebrates characterized by two EF-hand calcium-binding motifs. There are at least 21 different S100 proteins, and the name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are disulfide-linked homodimer, and is normally present in cells derived from the neural crest, chondrocytes, macrophages, dendritic cells, etc. S1 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. Protein S100-A10, also known as Calpactin I light chain, Cellular ligand of annexin II, S100 calcium-binding protein A10, p10 protein, p11, ANX2LG and S100A10, is a member of the S100 family of small, dimeric EF hand-type Ca(2+)-binding proteins that generally modulate cellular target proteins in response to intracellular Ca(2+) signals. In contrast to all other S100 proteins, S100A10 is Ca(2+) insensitive because of amino acid replacements in its Ca(2+)-binding loops that lock the protein in a permanently active state. S100A10 forms a heterotetramer with annexin IIH and promotes carcinoma invasion and metastasis by plasminogen activation. S100A10 and annexin II contribute to the aggressive characteristics of anaplastic carcinoma, while playing a constitutive role in papillary carcinoma. S100A10 induces the dimerization of ANXA2 / p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target of tyrosine-specific kinase. S100A10 functions as a linker tethering certain transmembrane proteins to annexin A2 thereby assisting their traffic to the plasma membrane and/or their firm anchorage at certain membrane sites.